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FatigueCapsid ProteinsCapsidDatabases, ProteinMolecular Sequence DataVirus AssemblyAmino Acid SequenceRiboflavin SynthaseBacteriophage PRD1Cryoelectron MicroscopyBacteriophage P22Webcasts as TopicLaboratory Animal ScienceEducation, VeterinaryBiological Science DisciplinesBiotechnologyHerpesvirus 4, HumanLaboratoriesEpstein-Barr Virus InfectionsInfectious MononucleosisAntibodies, ViralRNA PhagesLeviviridaeResearch ReportBacteriophagesLevivirusEscherichia coli ProteinsParvovirus B19, HumanErythema InfectiosumParvoviridae InfectionsParvovirusParvoviridaeAntibodiesPolyproteinsAntibody SpecificityIntracranial Hemorrhage, TraumaticRabbitsTetranychidaeGastropexyProton-Translocating ATPasesVirologyJournal Impact FactorHigh-Throughput Screening AssaysDependovirusGenetic VectorsTransduction, GeneticGenetic TherapyNuclear Pore Complex ProteinsNuclear PoreHIV-1beta Karyopherinsalpha KaryopherinsActive Transport, Cell NucleusKaryopherins
Fatigue: The state of weariness following a period of exertion, mental or physical, characterized by a decreased capacity for work and reduced efficiency to respond to stimuli.Capsid Proteins: Proteins that form the CAPSID of VIRUSES.Capsid: The outer protein protective shell of a virus, which protects the viral nucleic acid.Databases, Protein: Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Virus Assembly: The assembly of VIRAL STRUCTURAL PROTEINS and nucleic acid (VIRAL DNA or VIRAL RNA) to form a VIRUS PARTICLE.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Riboflavin Synthase: An enzyme that catalyzes the formation of riboflavin from two molecules of 6,7-dimethyl-8-ribityllumazine, utilizing a four-carbon fragment from one molecule which is transferred to the second molecule. EC 2.5.1.9.Bacteriophage PRD1: Bacteriophage and type species in the genus Tectivirus, family TECTIVIRIDAE. They are specific for Gram-negative bacteria.Cryoelectron Microscopy: Electron microscopy involving rapid freezing of the samples. The imaging of frozen-hydrated molecules and organelles permits the best possible resolution closest to the living state, free of chemical fixatives or stains.Bacteriophage P22: A species of temperate bacteriophage in the genus P22-like viruses, family PODOVIRIDAE, that infects SALMONELLA species. The genome consists of double-stranded DNA, terminally redundant, and circularly permuted.Webcasts as Topic: Transmission of live or pre-recorded audio or video content via connection or download from the INTERNET.Laboratory Animal Science: The science and technology dealing with the procurement, breeding, care, health, and selection of animals used in biomedical research and testing.Education, Veterinary: Use for general articles concerning veterinary medical education.Biological Science Disciplines: All of the divisions of the natural sciences dealing with the various aspects of the phenomena of life and vital processes. The concept includes anatomy and physiology, biochemistry and biophysics, and the biology of animals, plants, and microorganisms. It should be differentiated from BIOLOGY, one of its subdivisions, concerned specifically with the origin and life processes of living organisms.Biotechnology: Body of knowledge related to the use of organisms, cells or cell-derived constituents for the purpose of developing products which are technically, scientifically and clinically useful. Alteration of biologic function at the molecular level (i.e., GENETIC ENGINEERING) is a central focus; laboratory methods used include TRANSFECTION and CLONING technologies, sequence and structure analysis algorithms, computer databases, and gene and protein structure function analysis and prediction.Herpesvirus 4, Human: The type species of LYMPHOCRYPTOVIRUS, subfamily GAMMAHERPESVIRINAE, infecting B-cells in humans. It is thought to be the causative agent of INFECTIOUS MONONUCLEOSIS and is strongly associated with oral hairy leukoplakia (LEUKOPLAKIA, HAIRY;), BURKITT LYMPHOMA; and other malignancies.Laboratories: Facilities equipped to carry out investigative procedures.Epstein-Barr Virus Infections: Infection with human herpesvirus 4 (HERPESVIRUS 4, HUMAN); which may facilitate the development of various lymphoproliferative disorders. These include BURKITT LYMPHOMA (African type), INFECTIOUS MONONUCLEOSIS, and oral hairy leukoplakia (LEUKOPLAKIA, HAIRY).Infectious Mononucleosis: A common, acute infection usually caused by the Epstein-Barr virus (HERPESVIRUS 4, HUMAN). There is an increase in mononuclear white blood cells and other atypical lymphocytes, generalized lymphadenopathy, splenomegaly, and occasionally hepatomegaly with hepatitis.Antibodies, Viral: Immunoglobulins produced in response to VIRAL ANTIGENS.RNA Phages: Bacteriophages whose genetic material is RNA, which is single-stranded in all except the Pseudomonas phage phi 6 (BACTERIOPHAGE PHI 6). All RNA phages infect their host bacteria via the host's surface pili. Some frequently encountered RNA phages are: BF23, F2, R17, fr, PhiCb5, PhiCb12r, PhiCb8r, PhiCb23r, 7s, PP7, Q beta phage, MS2 phage, and BACTERIOPHAGE PHI 6.Leviviridae: A family of bacteriophages that infects enterobacteria, CAULOBACTER, and PSEUDOMONAS. The genome consists of linear, positive-sense single-stranded RNA.Research Report: Detailed account or statement or formal record of data resulting from empirical inquiry.Bacteriophages: Viruses whose hosts are bacterial cells.Levivirus: A bacteriophage genus of the family LEVIVIRIDAE, whose viruses contain the short version of the genome and have a separate gene for cell lysis.Escherichia coli Proteins: Proteins obtained from ESCHERICHIA COLI.Parvovirus B19, Human: The type species of ERYTHROVIRUS and the etiological agent of ERYTHEMA INFECTIOSUM, a disease most commonly seen in school-age children.Erythema Infectiosum: Contagious infection with human B19 Parvovirus most commonly seen in school age children and characterized by fever, headache, and rashes of the face, trunk, and extremities. It is often confused with rubella.Parvoviridae Infections: Virus infections caused by the PARVOVIRIDAE.Parvovirus: A genus of the family PARVOVIRIDAE, subfamily PARVOVIRINAE, infecting a variety of vertebrates including humans. Parvoviruses are responsible for a number of important diseases but also can be non-pathogenic in certain hosts. The type species is MINUTE VIRUS OF MICE.Parvoviridae: A family of very small DNA viruses containing a single molecule of single-stranded DNA and consisting of two subfamilies: PARVOVIRINAE and DENSOVIRINAE. They infect both vertebrates and invertebrates.Antibodies: Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).Polyproteins: Proteins which are synthesized as a single polymer and then cleaved into several distinct proteins.Antibody Specificity: The property of antibodies which enables them to react with some ANTIGENIC DETERMINANTS and not with others. Specificity is dependent on chemical composition, physical forces, and molecular structure at the binding site.Intracranial Hemorrhage, Traumatic: Bleeding within the SKULL induced by penetrating and nonpenetrating traumatic injuries, including hemorrhages into the tissues of CEREBRUM; BRAIN STEM; and CEREBELLUM; as well as into the epidural, subdural and subarachnoid spaces of the MENINGES.Rabbits: The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.Tetranychidae: Family of spider MITES, in the superfamily Tetranychoidea, suborder Trombidiformes.Gastropexy: Surgical fixation of the stomach to the abdominal wall.Proton-Translocating ATPases: Multisubunit enzymes that reversibly synthesize ADENOSINE TRIPHOSPHATE. They are coupled to the transport of protons across a membrane.Virology: The study of the structure, growth, function, genetics, and reproduction of viruses, and VIRUS DISEASES.Journal Impact Factor: A quantitative measure of the frequency on average with which articles in a journal have been cited in a given period of time.High-Throughput Screening Assays: Rapid methods of measuring the effects of an agent in a biological or chemical assay. The assay usually involves some form of automation or a way to conduct multiple assays at the same time using sample arrays.Dependovirus: A genus of the family PARVOVIRIDAE, subfamily PARVOVIRINAE, which are dependent on a coinfection with helper adenoviruses or herpesviruses for their efficient replication. The type species is Adeno-associated virus 2.Genetic Vectors: DNA molecules capable of autonomous replication within a host cell and into which other DNA sequences can be inserted and thus amplified. Many are derived from PLASMIDS; BACTERIOPHAGES; or VIRUSES. They are used for transporting foreign genes into recipient cells. Genetic vectors possess a functional replicator site and contain GENETIC MARKERS to facilitate their selective recognition.Transduction, Genetic: The transfer of bacterial DNA by phages from an infected bacterium to another bacterium. This also refers to the transfer of genes into eukaryotic cells by viruses. This naturally occurring process is routinely employed as a GENE TRANSFER TECHNIQUE.Genetic Therapy: Techniques and strategies which include the use of coding sequences and other conventional or radical means to transform or modify cells for the purpose of treating or reversing disease conditions.Nuclear Pore Complex Proteins: Proteins that form the structure of the NUCLEAR PORE. They are involved in active, facilitated and passive transport of molecules in and out of the CELL NUCLEUS.Nuclear Pore: An opening through the NUCLEAR ENVELOPE formed by the nuclear pore complex which transports nuclear proteins or RNA into or out of the CELL NUCLEUS and which, under some conditions, acts as an ion channel.HIV-1: The type species of LENTIVIRUS and the etiologic agent of AIDS. It is characterized by its cytopathic effect and affinity for the T4-lymphocyte.beta Karyopherins: Nucleocytoplasmic transport molecules that bind to ALPHA KARYOPHERINS in the CYTOSOL and are involved in transport of molecules through the NUCLEAR PORE COMPLEX. Once inside the CELL NUCLEUS beta karyopherins interact with RAN GTP-BINDING PROTEIN and dissociate from alpha karyopherins. Beta karyopherins bound to RAN GTP-BINDING PROTEIN are then re-transported to the cytoplasm where hydrolysis of the GTP of RAN GTP-BINDING PROTEIN causes release of karyopherin beta.alpha Karyopherins: Nucleocytoplasmic transport molecules that bind to the NUCLEAR LOCALIZATION SIGNALS of cytoplasmic molecules destined to be imported into the CELL NUCLEUS. Once attached to their cargo they bind to BETA KARYOPHERINS and are transported through the NUCLEAR PORE COMPLEX. Inside the CELL NUCLEUS alpha karyopherins dissociate from beta karypherins and their cargo. They then form a complex with CELLULAR APOPTOSIS SUSCEPTIBILITY PROTEIN and RAN GTP-BINDING PROTEIN which is exported to the CYTOPLASM.Active Transport, Cell Nucleus: Gated transport mechanisms by which proteins or RNA are moved across the NUCLEAR MEMBRANE.Karyopherins: A family of proteins involved in NUCLEOCYTOPLASMIC TRANSPORT. Karyopherins are heteromeric molecules composed two major types of components, ALPHA KARYOPHERINS and BETA KARYOPHERINS, that function together to transport molecules through the NUCLEAR PORE COMPLEX. Several other proteins such as RAN GTP BINDING PROTEIN and CELLULAR APOPTOSIS SUSCEPTIBILITY PROTEIN bind to karyopherins and participate in the transport process.

CAR-dependent and CAR-independent pathways of adenovirus vector-mediated gene transfer and expression in human fibroblasts. (1/5649)

Primary fibroblasts are not efficiently transduced by subgroup C adenovirus (Ad) vectors because they express low levels of the high-affinity Coxsackie virus and adenovirus receptor (CAR). In the present study, we have used primary human dermal fibroblasts as a model to explore strategies by which Ad vectors can be designed to enter cells deficient in CAR. Using an Ad vector expressing the human CAR cDNA (AdCAR) at high multiplicity of infection, primary fibroblasts were converted from being CAR deficient to CAR sufficient. Efficiency of subsequent gene transfer by standard Ad5-based vectors and Ad5-based vectors with alterations in penton and fiber was evaluated. Marked enhancement of binding and transgene expression by standard Ad5 vectors was achieved in CAR-sufficient fibroblasts. Expression by AdDeltaRGDbetagal, an Ad5-based vector lacking the arginine-glycine-aspartate (RGD) alphaV integrin recognition site from its penton base, was achieved in CAR-sufficient, but not CAR-deficient, cells. Fiber-altered Ad5-based vectors, including (a) AdF(pK7)betagal (bearing seven lysines on the end of fiber) (b) AdF(RGD)betagal (bearing a high-affinity RGD sequence on the end of fiber), and (c) AdF9sK betagal (bearing a short fiber and Ad9 knob), demonstrated enhanced gene transfer in CAR-deficient fibroblasts, with no further enhancement in CAR-sufficient fibroblasts. Together, these observations demonstrate that CAR deficiency on Ad targets can be circumvented either by supplying CAR or by modifying the Ad fiber to bind to other cell-surface receptors.  (+info)

Maturation-induced conformational changes of HIV-1 capsid protein and identification of two high affinity sites for cyclophilins in the C-terminal domain. (2/5649)

Viral incorporation of cyclophilin A (CyPA) during the assembly of human immunodeficiency virus type-1 (HIV-1) is crucial for efficient viral replication. CyPA binds to the previously identified Gly-Pro90 site of the capsid protein p24, but its role remained unclear. Here we report two new interaction sites between cyclophilins and p24. Both are located in the C-terminal domain of p24 around Gly-Pro157 and Gly-Pro224. Peptides corresponding to these regions showed higher affinities (Kd approximately 0.3 microM) for both CyPA and cyclophilin B than the best peptide derived from the Gly-Pro90 site ( approximately 8 microM) and thus revealed new sequence motifs flanking Gly-Pro that are important for tight interaction of peptide ligands with cyclophilins. Between CyPA and an immature (unprocessed) form of p24, a Kd of approximately 8 microM was measured, which corresponded with the Kd of the best of the Gly-Pro90 peptides, indicating an association via this site. Processing of immature p24 by the viral protease, yielding mature p24, elicited a conformational change in its C-terminal domain that was signaled by the covalently attached fluorescence label acrylodan. Consequently, CyPA and cyclophilin B bound with much higher affinities ( approximately 0.6 and 0.25 microM) to the new, i.e. maturation-generated sites. Since this domain is essential for p24 oligomerization and capsid cone formation, CyPA bound to the new sites might impair the regularity of the capsid cone and thus facilitate in vivo core disassembly after host infection.  (+info)

Low temperature and pressure stability of picornaviruses: implications for virus uncoating. (3/5649)

The family Picornaviridae includes several viruses of great economic and medical importance. Poliovirus replicates in the human digestive tract, causing disease that may range in severity from a mild infection to a fatal paralysis. The human rhinovirus is the most important etiologic agent of the common cold in adults and children. Foot-and-mouth disease virus (FMDV) causes one of the most economically important diseases in cattle. These viruses have in common a capsid structure composed of 60 copies of four different proteins, VP1 to VP4, and their 3D structures show similar general features. In this study we describe the differences in stability against high pressure and cold denaturation of these viruses. Both poliovirus and rhinovirus are stable to high pressure at room temperature, because pressures up to 2.4 kbar are not enough to promote viral disassembly and inactivation. Within the same pressure range, FMDV particles are dramatically affected by pressure, with a loss of infectivity of more than 4 log units observed. The dissociation of polio and rhino viruses can be observed only under pressure (2.4 kbar) at low temperatures in the presence of subdenaturing concentrations of urea (1-2 M). The pressure and low temperature data reveal clear differences in stability among the three picornaviruses, FMDV being the most sensitive, polio being the most resistant, and rhino having intermediate stability. Whereas rhino and poliovirus differ little in stability (less than 10 kcal/mol at 0 degrees C), the difference in free energy between these two viruses and FMDV was remarkable (more than 200 kcal/mol of particle). These differences are crucial to understanding the different factors that control the assembly and disassembly of the virus particles during their life cycle. The inactivation of these viruses by pressure (combined or not with low temperature) has potential as a method for producing vaccines.  (+info)

Time-resolved fluorescence investigation of the human immunodeficiency virus type 1 nucleocapsid protein: influence of the binding of nucleic acids. (4/5649)

Depending on the HIV-1 isolate, MN or BH10, the nucleocapsid protein, NCp7, corresponds to a 55- or 71-amino acid length product, respectively. The MN NCp7 contains a single Trp residue at position 37 in the distal zinc finger motif, and the BH10 NCp7 contains an additional Trp, at position 61 in the C-terminal chain. The time-resolved intensity decay parameters of the zinc-saturated BH10 NCp7 were determined and compared to those of single-Trp-containing derivatives. The fluorescence decay of BH10 NCp7 could be clearly represented as a linear combination (with respect to both lifetimes and fractional intensities) of the individual emitting Trp residues. This suggested the absence of interactions between the two Trp residues, a feature that was confirmed by molecular modeling and fluorescence energy transfer studies. In the presence of tRNAPhe, taken as a RNA model, the same conclusions hold true despite the large fluorescence decrease induced by the binding of tRNAPhe. Indeed, the fluorescence of Trp37 appears almost fully quenched, in keeping with a stacking of this residue with the bases of tRNAPhe. Despite the multiple binding sites in tRNAPhe, the large prevalence of ultrashort lifetimes, associated with the stacking of Trp37, suggests that this stacking constitutes a major feature in the binding process of NCp7 to nucleic acids. In contrast, Trp61 only stacked to a small extent with tRNAPhe. The behavior of this residue in the tRNAPhe-NCp7 complexes appeared to be rather heterogeneous, suggesting that it does not constitute a major determinant in the binding process. Finally, our data suggested that the binding of NCp7 proteins from the two HIV-1 strains to nonspecific nucleic acid sequences was largely similar.  (+info)

The haplotype distribution of two genes of citrus tristeza virus is altered after host change or aphid transmission. (5/5649)

Genetic variability of citrus tristeza virus (CTV) was studied using the haplotypes detected by single-strand conformation polymorphism (SSCP) analysis of genes p18 and p20 in six virus populations of two origins. The Spanish group included a CTV isolate and subisolates obtained by graft-transmission to different host species. The other included two subisolates aphid-transmitted from a single Japanese isolate. The homozygosity observed for gene p20 was always significantly higher than that expected under neutral evolution, whereas only three populations showed high homozygosity for p18, suggesting stronger host constraints for p20 than for p18. Sequential transmissions of a Spanish isolate to new host species increased the difference between its population and that of the successive subisolates for gene p18, as estimated by the F statistic. Analysis of molecular variance indicated that variation between both groups of populations was not statistically significant, whereas variations between populations of the same group or within populations were significant for both genes studied. Our data indicate that selection affects the haplotype distribution and that adaptation to a new host can be as important or more as the geographical origin. Variation of the CTV populations after host change or aphid transmission may explain in part the wide biological variability observed among CTV isolates.  (+info)

A new picornavirus isolated from bank voles (Clethrionomys glareolus). (6/5649)

A previously unknown picornavirus was isolated from bank voles (Clethrionomys glareolus). Electron microscopy images and sequence data of the prototype isolate, named Ljungan virus, showed that it is a picornavirus. The amino acid sequences of predicted Ljungan virus capsid proteins VP2 and VP3 were closely related to the human pathogen echovirus 22 (approximately 70% similarity). A partial 5' noncoding region sequence of Ljungan virus showed the highest degree of relatedness to cardioviruses. Two additional isolates were serologically and molecularly related to the prototype.  (+info)

The cleavable carboxyl-terminus of the small coat protein of cowpea mosaic virus is involved in RNA encapsidation. (7/5649)

The site of cleavage of the small coat protein of cowpea mosaic virus has been precisely mapped and the proteolysis has been shown to result in the loss of 24 amino acids from the carboxyl-terminus of the protein. A series of premature termination and deletion mutants was constructed to investigate the role or roles of these carboxyl-terminal amino acids in the viral replication cycle. Mutants containing premature termination codons at or downstream of the cleavage site were viable but reverted to wild-type after a single passage through cowpea plants, indicating that the carboxyl-terminal amino acids are important. Mutants with the equivalent deletions were genetically stable and shown to be debilitated with respect to virus accumulation. The specific infectivity of preparations of a deletion mutant (DM4) lacking all 24 amino acids was 6-fold less than that of a wild-type preparation. This was shown to be a result of DM4 preparations containing a much increased percentage (73%) of empty (RNA-free) particles, a finding that implicates the cleavable carboxyl-terminal residues in the packaging of the virion RNAs.  (+info)

Induction of autoantibodies to mouse CCR5 with recombinant papillomavirus particles. (8/5649)

The vertebrate immune system has evolved to respond vigorously to microbial infection but to ignore self-antigens. Evidence has emerged that B cell responses to viruses are initiated by immune recognition of ordered arrays of antigen on the viral surface. To test whether autoantibodies against a self-antigen can be induced by placing it in a context that mimics the ordered surface of a viral particle, a peptide representing an extracellular loop of the mouse chemokine receptor CCR5 was incorporated into an immunodominant site of the bovine papillomavirus virus L1 coat protein, which self-assembles into virus-like particles. Mice inoculated with chimeric L1-CCR5 particles generated autoantibodies that bound to native mouse CCR5, inhibited binding of its ligand RANTES, and blocked HIV-1 infection of an indicator cell line expressing a human-mouse CCR5 chimera. These results suggest a general method for inducing autoantibodies against self-antigens, with diverse potential basic research and clinical applications.  (+info)

Herpes simplex virus capsids are transported in neuronal axons without an envelope containing the viral glycoproteins<...Herpes simplex virus capsids are transported in neuronal axons without an envelope containing the viral glycoproteins<...
TY - JOUR. T1 - Herpes simplex virus capsids are transported in neuronal axons without an envelope containing the viral glycoproteins. AU - Snyder, Aleksandra. AU - Wisner, Todd W.. AU - Johnson, David. PY - 2006/11. Y1 - 2006/11. N2 - Electron micrographic studies of neuronal axons have produced contradictory conclusions on how alpha-herpesviruses are transported from neuron cell bodies to axon termini. Some reports have described unenveloped capsids transported on axonal microtubules with separate transport of viral glycoproteins within membrane vesicles. Others have observed enveloped virions in proximal and distal axons. We characterized transport of herpes simplex virus (HSV) in human and rat neurons by staining permeabilized neurons with capsid- and glycoprotein-specific antibodies. Deconvolution microscopy was used to view 200-nm sections of axons. HSV glycoproteins were very rarely associated with capsids (3 to 5%) and vice versa. Instances of glycoprotein/capsid overlap frequently ...
Control of capsid disassembly is crucial for efficient HIV-1 cDNA activityControl of capsid disassembly is crucial for efficient HIV-1 cDNA activity
... after access, yet sponsor elements involved in this procedure remain mainly mystery. MELK dictates ideal capsid disassembly through phosphorylation of Ser-149 in the multimerized HIV-1 primary, which prospects to effective virus-like Clonidine hydrochloride supplier cDNA activity in focus on cells. The phosphorylation-mimetic capsid mutation of Ser-149 triggered extravagant capsid disassembly and too-early finalization of invert transcription, and impeded nuclear admittance of HIV-1 cDNA, recommending the importance of well-ordered capsid disassembly in the early levels of virus-like duplication. This breakthrough discovery shall facilitate understanding of the useful hyperlink among pathogen uncoating, invert transcription and nuclear admittance, and is certainly anticipated to lead to developing a story technique for Helps therapy. Launch During the training course of individual immunodeficiency pathogen type 1 (HIV-1) ...
Extent of protein-protein interactions and quasi-equivalence in viral capsidsExtent of protein-protein interactions and quasi-equivalence in viral capsids
Viral capsids are composed of multiple copies of one or a few gene products that self-assemble on their own or in the presence of the viral genome and/or auxiliary proteins into closed shells (capsids). We have analyzed 75 high-resolution virus capsid structures by calculating the average fraction of the solvent-accessible surface area of the coat protein subunits buried in the viral capsids. This fraction ranges from 0 to 1 and represents a normalized protein-protein interaction (PPI) index and is a measure of the extent of protein-protein interactions. The PPI indices were used to compare the extent of association of subunits among different capsids. We further examined the variation of the PPI indices as a function of the molecular weight of the coat protein subunit and the capsid diameter. Our results suggest that the PPI indices in T=1 and pseudo-T=3 capsids vary linearly with the molecular weight of the subunit and capsid size. This is in contrast to quasi-equivalent capsids with T>or=3, ...
Major capsid reinforcement by a minor protein in herpesviruses and pha by Udom Sae-Ueng, Ting Liu et al."Major capsid reinforcement by a minor protein in herpesviruses and pha" by Udom Sae-Ueng, Ting Liu et al.
Herpes simplex type 1 virus (HSV-1) and bacteriophage λ capsids undergo considerable structural changes during self-assembly and DNA packaging. The initial steps of viral capsid self-assembly require weak, non-covalent interactions between the capsid subunits to ensure free energy minimization and error-free assembly. In the final stages of DNA packaging, however, the internal genome pressure dramatically increases, requiring significant capsid strength to withstand high internal genome pressures of tens of atmospheres. Our data reveal that the loosely formed capsid structure is reinforced post-assembly by the minor capsid protein UL25 in HSV-1 and gpD in bacteriophage λ. Using atomic force microscopy nano-indentation analysis, we show that the capsid becomes stiffer upon binding of UL25 and gpD due to increased structural stability. At the same time the force required to break the capsid increases by ∼70% for both herpes and phage. This demonstrates a universal and evolutionarily conserved function
Herpes simplex virus capsids assembled in insect cells infected with recombinant baculoviruses: structural authenticity and...Herpes simplex virus capsids assembled in insect cells infected with recombinant baculoviruses: structural authenticity and...
Recently, recombinant baculoviruses have been used to show that expression of six herpes simplex virus type 1 genes results in the formation of capsid-like particles. We have applied cryoelectron microscopy and three-dimensional image reconstruction to establish their structural authenticity to a resolution of approximately 2.7 nm. By comparing capsids assembled with and without the expression of gene UL35, we have confirmed the presence of six copies of its product, VP26 (12 kDa), around each hexon tip. However, VP26 is not present on pentons, indicating that the conformational differences between the hexon and penton states of the major capsid protein, VP5, extend to the VP26 binding site. ...
Assembly and Structure of Bacteriophage Capsids and Tails - D-Scholarship@PittAssembly and Structure of Bacteriophage Capsids and Tails - [email protected]
Phages HK97 and λ are model systems that have aided in the understanding of capsid and tail assembly. HK97 capsid assembly involves the formation of a T=7 icosahedral lattice from 415 monomers of the major capsid protein (mcp), 12 monomers of portal protein, and ~120 copies of the protease. Salt bridges have been found to play a critical role in the assembly pathway, but it is not clear how capsid size is determined. Phage phi1026b is larger than HK97 but the mcp shares 50% sequence similarity with HK97. We hypothesize that comparing the atomic models of phi1026b and HK97 will help illuminate conserved and unique interactions that may play a role in assembly and potentially size determination. By utilizing the FEI Krios microscope, Falcon II camera, and EPU data acquisition software, high-resolution structures were generated which allowed for the generation of atomic models of the phi1026b Prohead I and Head capsids. Differences were observed in the organization of the delta domain, capsomers, ...
The outer shell of the adenovirus capsid comprises three major types - BET-bromodomain inhibition researchThe outer shell of the adenovirus capsid comprises three major types - BET-bromodomain inhibition research
The outer shell of the adenovirus capsid comprises three major types of protein (hexon, penton base and fiber) that perform the majority of functions facilitating the early stages of adenovirus infection. respect to the delivery of foreign molecules. Adenovirus capsid tasks in early illness The adenovirus (Ad) is definitely a non-enveloped, dsDNA disease whose outer shell of the icosahedral-shaped capsid is definitely comprises three major types of proteins: hexon, penton foundation and dietary fiber (Number 1). The hexon comprises the majority of the outer shell of the Ad capsid, forming 240 homotrimers that encapsidate the majority of the disease, including the viral genome and connected proteins [1]. The dietary fiber protrudes from each of the 12 vertices of the icosahedron, while the penton foundation lies at the base of each dietary fiber. These three capsid proteins contribute to the majority of activities required for the early phases of Ad infection. Number 1 Representation of ...
Genome polyprotein - Coxsackievirus A24 (strain EH24/70)Genome polyprotein - Coxsackievirus A24 (strain EH24/70)
Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host cell receptor to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks (By similarity).
Structural insights into the assembly and regulation of distinct viral capsid complexesStructural insights into the assembly and regulation of distinct viral capsid complexes
The assembly and regulation of viral capsid proteins into highly ordered macromolecular complexes is essential for viral replication. Here, we utilize crystal structures of the capsid protein from the smallest and simplest known viruses capable of autonomously replicating in animal cells, circoviruses, to establish structural and mechanistic insights into capsid morphogenesis and regulation. The beak and feather disease virus, like many circoviruses, encode only two genes: a capsid protein and a replication initiation protein. The capsid protein forms distinct macromolecular assemblies during replication and here we elucidate these structures at high resolution, showing that these complexes reverse the exposure of the N-terminal arginine rich domain responsible for DNA binding and nuclear localization. We show that assembly of these complexes is regulated by single-stranded DNA (ssDNA), and provide a structural basis of capsid assembly around single-stranded DNA, highlighting novel binding ...
An HIV-1 capsid binding protein TRIM11 accelerates viral uncoating | Retrovirology | Full TextAn HIV-1 capsid binding protein TRIM11 accelerates viral uncoating | Retrovirology | Full Text
Several members of the TRIM family have been implicated in antiviral defense. Our previous report showed that human TRIM11 potently inhibited HIV-1 transduction by reducing the viral reverse transcripts. These results prompted us to examine the effect of TRIM11 on HIV-1 uncoating, which is closely related to viral reverse transcription. Using a combination of in vitro binding and in situ proximity ligation assay, we showed that TRIM11 could interact with HIV-1 capsid. Overexpression of TRIM11 accelerates HIV-1 uncoating and reduces viral reverse transcription indicated by the fate-of-capsid assay and quantitative PCR respectively. Knockdown of TRIM11 enhanced HIV-1 capsid stability and increased viral reverse transcription. However, the replication of another retrovirus MLV is not affected by TRIM11. Moreover, the reverse transcription of HIV-1 mutant bearing capsid G89V showed insensitivity to restriction by TRIM11, indicating that the viral determinant of restriction by TRIM11 might reside on capsid.
Proteasomal Degradation of Herpes Simplex Virus Capsids in Macrophages Releases DNA to the Cytosol for Recognition by DNA...Proteasomal Degradation of Herpes Simplex Virus Capsids in Macrophages Releases DNA to the Cytosol for Recognition by DNA...
The innate immune system is important for control of infections, including herpesvirus infections. Intracellular DNA potently stimulates antiviral IFN responses. It is known that plasmacytoid dendritic cells sense herpesvirus DNA in endosomes via TLR9 and that nonimmune tissue cells can sense herpesvirus DNA in the nucleus. However, it remains unknown how and where myeloid cells, such as macrophages and conventional dendritic cells, detect infections with herpesviruses. In this study, we demonstrate that the HSV-1 capsid was ubiquitinated in the cytosol and degraded by the proteasome, hence releasing genomic DNA into the cytoplasm for detection by DNA sensors. In this context, the DNA sensor IFN-γ-inducible 16 is important for induction of IFN-β in human macrophages postinfection with HSV-1 and CMV. Viral DNA localized to the same cytoplasmic regions as did IFN-γ-inducible 16, with DNA sensing being independent of viral nuclear entry. Thus, proteasomal degradation of herpesvirus capsids ...
Systemic delivery of siRNA by chimeric capsid protein: Tumor targeting and RNAi activity in vivo<...Systemic delivery of siRNA by chimeric capsid protein: Tumor targeting and RNAi activity in vivo<...
TY - JOUR. T1 - Systemic delivery of siRNA by chimeric capsid protein. T2 - Tumor targeting and RNAi activity in vivo. AU - Choi, Kyung Mi. AU - Kim, Kwang Meyung. AU - Kwon, Ick Chan. AU - Kim, In-San. AU - Ahn, Hyung Jun. PY - 2013/1/7. Y1 - 2013/1/7. N2 - Recently, we reported that a chimeric capsid protein assembled into a macromolecular container-like structure with capsid shell and the resulting siRNA/capsid nanocarrier complexes efficiently suppressed RFP gene expression in the cell culture system. To extend RNAi to the in vivo applications, we here demonstrated that the siRNA/capsid nanocarrier complexes could have tumor-specific targeting ability in vivo as well as the increased stability of siRNA during body circulation. When systemically administered, our siRNA/capsid nanocarrier complexes delivered siRNA to tumor tissues and efficiently suppressed RFP gene expression in tumor-bearing mice. The enhanced longevity of siRNA in vivo could be explained by shielding effect derived from the ...
Intermediate capsid protein VP6 - Rotavirus A (strain RVA/SA11-Both/G3P5B[2]) (RV-A)Intermediate capsid protein VP6 - Rotavirus A (strain RVA/SA11-Both/G3P5B[2]) (RV-A)
Intermediate capsid protein that self assembles to form an icosahedral capsid with a T=13 symmetry, which consists of 230 trimers of VP6, with channels at each of its five-fold vertices. This capsid constitutes the middle concentric layer of the viral mature particle. The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nascent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels at the five-fold axes. VP6 is required for the transcription activity of the DLP (By similarity).
The study of the mechanism of formation of HIV capsid can be the basis for developing a new type of therapy - Life4me+The study of the mechanism of formation of HIV capsid can be the basis for developing a new type of therapy - Life4me+
Scientists from the University of New South Wales (#UNSW, UK) found that the special protein capsid envelope created by HIV at the time of entry into the human body uses a specific host cell molecule, inositol-hexakisphosphate, as a shield from immunity. The latter gives the capsid stability and allows unhindered to carry the genetic material of the virus to the nucleus of the cell. According to experts, this discovery can be the first step to changing the strategy of #HIV treatment. A new goal for antiviral therapy, scientists suggest to make the capsid itself.
Rabbit Polyclonal to NCBP2. | healthweblognews.infoRabbit Polyclonal to NCBP2. | healthweblognews.info
Herpes simplex virus type 1 (HSV-1) capsids are initially assembled with an interior proteins scaffold. capsids upon DNA product packaging we show that VP24 (formulated with the protease area) is certainly quantitatively retained. To research elements managing UL26 capsid incorporation and retention we used a mutant computer virus that fails to express UL26.5 (?virus). Purified ?B capsids showed altered sucrose gradient sedimentation and lacked the dense scaffold core seen in micrographs of wild-type B capsids but contained capsid shell proteins in wild-type amounts. Despite C-terminal sequence identity between UL26 and UL26.5 ?capsids lacking UL26.5 products did not contain compensatory high levels of UL26 proteins. Therefore HSV capsids can be maintained and/or assembled on a minimal scaffold made up of only wild-type levels of UL26 proteins. In contrast to UL26.5 increased expression of UL26 did not compensate for the ?growth defect. While indirect these findings are consistent with the view ...
Origin of unenveloped capsids in the cytoplasm of cells infected with herpes simplex virus 1. | Journal of VirologyOrigin of unenveloped capsids in the cytoplasm of cells infected with herpes simplex virus 1. | Journal of Virology
In cells infected with herpes simplex viruses the capsids acquire an envelope at the nuclear membrane and are usually found in the cytoplasm in structures bound by membranes. Infected cells also accumulate unenveloped capsids alone or juxtaposed to cytoplasmic membranes. The juxtaposed capsids have been variously interpreted as either undergoing terminal deenvelopment resulting from fusion of the envelope with the membrane of the cytoplasmic vesicles or undergoing sequential envelopment and deenvelopment as capsids transit the cytoplasm into the extracellular space. Recent reports have shown that (i) wild-type virus attaches to but does not penetrate cells expressing glycoprotein D (G. Campadelli-Fiume, M. Arsenakis, F. Farabegoli, and B. Roizman, J. Virol. 62:159-167, 1988) and that (ii) a mutation in glycoprotein D enables the mutant virus to productively infect cells expressing the wild-type glycoprotein (G. Campadelli-Fiume, S. Qi, E. Avitabile, L. Foa-Tomasi, R. Brandimarti, and B. Roizman, ...
Nuclear Herpesvirus Capsid Motility Is Not Dependent on F-Actin | mBioNuclear Herpesvirus Capsid Motility Is Not Dependent on F-Actin | mBio
We provide evidence that F-actin is not involved in intranuclear capsid motility of herpesvirus capsids in primary fibroblasts. We found no indication of nuclear F-actin in cells infected with representative members of all three subfamilies of the Herpesviridae. This finding is consistent with reports showing that steady-state somatic cells do not exhibit phalloidin-stainable nuclear F-actin but that most nuclear actin is in a monomeric, G-actin form. This idea was underlined by a recent report that Lifeact- and phalloidin-stainable nuclear F-actin could be found in somatic cells only as a transient effect of serum stimulation (24). Another recent report describes submicron-length actin polymers using a truncated form of utrophin as a novel nuclear F-actin probe (25). But as the described polymers were extremely short, the authors suggested that it is unlikely they are involved in transport processes. Moreover, they also ruled out directed propulsive force generation by these novel actin ...
Permeability of the HIV-1 capsid to metabolites modulates viral DNA synthesis | Biophysics LabPermeability of the HIV-1 capsid to metabolites modulates viral DNA synthesis | Biophysics Lab
Reverse transcription, an essential event in the HIV-1 lifecycle, requires deoxynucleotide triphosphates (dNTPs) to fuel DNA synthesis, thus requiring penetration of dNTPs into the viral core. The central cavity of the capsid protein (CA) hexamer reveals itself as a plausible channel that allows the passage of dNTPs into assembled capsids. Nevertheless, the molecular mechanism of nucleotide import into the capsid remains unknown. Employing all-atom molecular dynamics simulations, we established that cooperative binding between nucleotides inside a CA hexamer cavity results in energetically-favorable conditions for passive translocation of dNTPs into the HIV-1 capsid. Furthermore, binding of the host cell metabolite inositol hexakisphosphate (IP6) enhances dNTP import, while binding of synthesized molecules like benzenehexacarboxylic acid (BHC) inhibits it. The enhancing effect on reverse transcription by IP6 and the consequences of interactions between CA and nucleotides were corroborated using ...
Institute Of Molecular Biophysics | Master CalendarInstitute Of Molecular Biophysics | Master Calendar
Title: HIV Capsid Pattern Sensing by the Host Cell. Abstract. The mature HIV capsid provides a range of interfaces recognizable by host factors and, during its post-entry journey from the cell periphery to the nucleus, the virus encounters a variety of them-some co-opted for optimal infectivity, others evolutionarily designed to prevent infection. A common feature of these interactions is the ability of capsid pattern sensing by the host. This feature allows a host factor to preferably bind intact capsid cores that contain the viral genome, and to avoid the numerous unassembled CA molecules present in the cell. However, high-order capsid recognition is challenging to study in vitro. Here I present various protein-engineering strategies for the production of a repertoire of soluble capsid assemblies and the use of these assemblies in the study of native capsid structure and capsid-host factor interactions. Our studies contribute to a better understanding of the diverse molecular mechanisms by ...
1gwp - Proteopedia, life in 3D1gwp - Proteopedia, life in 3D
The capsid protein (CA) of the mature human immunodeficiency virus (HIV) contains an N-terminal beta-hairpin that is essential for formation of the capsid core particle. CA is generated by proteolytic cleavage of the Gag precursor polyprotein during viral maturation. We have determined the NMR structure of a 283-residue N-terminal fragment of immature HIV-1 Gag (Gag(283)), which includes the intact matrix (MA) and N-terminal capsid (CA(N)) domains. The beta-hairpin is unfolded in Gag(283), consistent with the proposal that hairpin formation occurs subsequent to proteolytic cleavage of Gag, triggering capsid assembly. Comparison of the immature and mature CA(N) structures reveals that beta-hairpin formation induces a approximately 2 A displacement of helix 6 and a concomitant displacement of the cyclophylin-A (CypA)-binding loop, suggesting a possible allosteric mechanism for CypA-mediated destabilization of the capsid particle during infectivity. Structure of the N-terminal 283-residue fragment ...
Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function. - Nuffield...Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function. - Nuffield...
Mature HIV-1 particles contain conical-shaped capsids that enclose the viral RNA genome and perform essential functions in the virus life cycle. Previous structural analysis of two- and three-dimensional arrays of the capsid protein (CA) hexamer revealed three interfaces. Here, we present a cryoEM study of a tubular assembly of CA and a high-resolution NMR structure of the CA C-terminal domain (CTD) dimer. In the solution dimer structure, the monomers exhibit different relative orientations compared to previous X-ray structures. The solution structure fits well into the EM density map, suggesting that the dimer interface is retained in the assembled CA. We also identified a CTD-CTD interface at the local three-fold axis in the cryoEM map and confirmed its functional importance by mutagenesis. In the tubular assembly, CA intermolecular interfaces vary slightly, accommodating the asymmetry present in tubes. This provides the necessary plasticity to allow for controlled virus capsid dis/assembly.
Machine-guided engineering of AAV capsids | Beer ReviewedMachine-guided engineering of AAV capsids | Beer Reviewed
Taking a more systematic approach to the capsid protein-engineering problem, researchers mutated one by one each of the 735 amino acids within the AAV2 capsid, the best-known member of the AAV family, including all possible codon substitutions, insertions and deletions at each position. They generated a virus library containing about 200,000 variants and identified capsid changes that both maintained AAV2s viability and improved its homing potential (tropism) to specific organs in mice.. This full article appears on ,a href="https://www.sciencedaily.com/releases/2019/11/191128172334.htm",Science Daily,/a,. ...
Icosahedral virus capsid, illustration - Stock Image F018/4295 - Science Photo LibraryIcosahedral virus capsid, illustration - Stock Image F018/4295 - Science Photo Library
Computer artwork of the inner surface of an icosahedral virus capsid. The capsid is the protein shell of the virus and encloses its genetic material. - Stock Image F018/4295
FCGR3A - BET-bromodomain inhibition researchFCGR3A - BET-bromodomain inhibition research
The outer shell of the adenovirus capsid comprises three major types of protein (hexon, penton base and fiber) that perform the majority of functions facilitating the early stages of adenovirus infection. respect to the delivery of foreign molecules. Adenovirus capsid tasks in early illness The adenovirus (Ad) is definitely a non-enveloped, dsDNA disease whose outer shell of the icosahedral-shaped capsid is definitely comprises three major types of proteins: hexon, penton foundation and dietary fiber (Number 1). The hexon comprises the majority of the outer shell of the Ad capsid, forming 240 homotrimers that encapsidate the majority of the disease, including the viral genome and connected proteins [1]. The dietary fiber protrudes from each of the 12 vertices of the icosahedron, while the penton foundation lies at the base of each dietary fiber. These three capsid proteins contribute to the majority of activities required for the early phases of Ad infection. Number 1 Representation of ...
neverendingbooksneverendingbooks
Little is known about capsid formation, that is the process in which the capsid proteins self-assemble into an icosahedral shape, nor about the precise interplay between the genome and the capsid proteins. If we would understand these two things better it might open new possibilities for anti-viral drugs, by either blocking the self-assembly process or by breaking the genome-capsid interaction.. A first proposal for the capsid structure was put forward by Caspar and Klug. Their quasi-equivalence principle asserts that each of the 20 triangular faces of the icosahedron is subdivided in 3 subunits, each consisting of at least one protein.. Most viruses have much more than 60 proteins in their capsid, so Caspar and Klug introduced their $T$-number giving the number of proteins per subunit. One superimposes the triangulation of the icosahedron with the hexagonal plane lattice, then $T$ is the number of sub-triangles of these hexagons contained in each subunit. For $T = 7$ we have the following ...
Universitätsklinikum Heidelberg: AG UrbanUniversitätsklinikum Heidelberg: AG Urban
In the infected cell, newly synthesized genomic RNA is packaged together with the viral Pol-protein and a cellular chaperone complex into capsids. The RNA is then reverse transcribed into a partially double-stranded DNA within the capsid. Under natural conditions, almost exclusively mature capsids containing DNA are enveloped to be secreted as virions. The selectivity of this process depends on a still undefined maturation signal that communicates the RNA-DNA-transition from the interior to the capsid exterior.. The large envelope protein of HBV (L-protein) adopts two transmembrane topologies: At first, its preS-region is located on the cytosolic side of the ER-membrane and acts as a matrix-domain that binds the mature capsid to enable its envelopment. The same region is thereafter required on the viron surface as a receptor binding domain to initiate the next round of infection. So far, it is unknown if the dual topology is already pre-formed prior to viral budding and therefore stably present ...
Immune ResponseImmune Response
It is relatively easy to determine that the poliovirus capsid is made up of just four proteins, and that the four capsid proteins VP1, VP2, VP3, and VP4 are present in equimolar amounts in the capsid. Groups of five copies of each protein are arranged at each of the 12 vertices of the icosahedral capsid see Chapters 5 and 15 . If the proteins are uniformly labeled with radioactive amino acids, more radioactivity will be in each large polypeptide chain than in each small one. A gel fractionation.... ...
Herpesviruses remodel host membranes for virus egress<...Herpesviruses remodel host membranes for virus egress<...
TY - JOUR. T1 - Herpesviruses remodel host membranes for virus egress. AU - Johnson, David C.. AU - Baines, Joel D.. PY - 2011/5/1. Y1 - 2011/5/1. N2 - Herpesviruses replicate their DNA and package this DNA into capsids in the nucleus. These capsids then face substantial obstacles to their release from cells. Unlike other DNA viruses, herpesviruses do not depend on disruption of nuclear and cytoplasmic membranes for their release. Enveloped particles are formed by budding through inner nuclear membranes, and then these perinuclear enveloped particles fuse with outer nuclear membranes. Unenveloped capsids in the cytoplasm are decorated with tegument proteins and then undergo secondary envelopment by budding into trans-Golgi network membranes, producing infectious particles that are released. In this Review, we describe the remodelling of host membranes that facilitates herpesvirus egress.. AB - Herpesviruses replicate their DNA and package this DNA into capsids in the nucleus. These capsids then ...
DCV capsid polyprotein抗体|Abcam中国|Anti-DCV capsid polyprotein抗体DCV capsid polyprotein抗体|Abcam中国|Anti-DCV capsid polyprotein抗体
DCV capsid polyprotein兔多克隆抗体(ab92954)可与重组片段样本反应并经WB, ELISA实验严格验证并得到1个独立的用户反馈。所有产品均提供质保服务，中国75%以上现货。
EMDB-6037: Capsid Expansion Mechanism Of Bacteriophage T7 Revealed By Multi-... - YorodumiEMDB-6037: Capsid Expansion Mechanism Of Bacteriophage T7 Revealed By Multi-... - Yorodumi
Details: Particles were selected from scanned micrograph images, first automatically by the ethan method and then by manual screening with the boxer program in EMAN. The TEM instrument contrast transfer function parameters were determined automatically using fitctf2.py and were then visually validated using the EMAN ctfit program. The datasets were then divided into two subsets (even and odd) and processed completely independently, including both initial models and refinements. For 3D reconstructions, the whole datasets were divided into even-odd halves and the initial de novo models and subsequent iterative refinements were all independently performed for each half dataset. The images were first binned 4x to obtain initial models and particle parameters assuming icosahedral symmetry. De novo initial models were built using the random model approach. Random subsets of particles were assigned random initial orientations and iteratively refined until convergence. Consistent icosahedral capsid ...
Electrostatic theory of viral self-assembly: a toy model - CBGSEElectrostatic theory of viral self-assembly: a toy model - CBGSE
Abstract: Viruses self-assemble from identical capsid proteins and their genome consisting, for example, of a long single stranded (ss) RNA. For a big class of T = 3 viruses capsid proteins have long positive N-terminal tails. We explore the role played by the Coulomb interaction between the brush of positive N-terminal tails rooted at the inner surface of the capsid and the negative ss RNA molecule. We show that viruses are most stable when the total contour length of ss RNA is close to the total length of the tails. For such a structure the absolute value of the total RNA charge is approximately twice larger than the charge of the capsid. This conclusion agrees with structural data. ...
Capsid proteins self-assemble to form stable shell : Viruses - AskNatureCapsid proteins self-assemble to form stable shell : Viruses - AskNature
Viruses are nanosized, genome-filled protein containers with remarkable thermodynamic and mechanical properties. They form by spontaneous self-assembly inside the crowded, heterogeneous cytoplasm of infected cells. Self-assembly of viruses seems to obey the principles of thermodynamically reversible self-assembly but assembled shells (capsids) strongly resist disassembly. Following assembly, some viral shells pass through a sequence of coordinated maturation steps that progressively strengthen the capsid. Viral shells have effective Youngs moduli ranging from that of polyethylene to that of plexiglas. Some of them can withstand internal osmotic pressures that are tens of atmospheres." (Roos et al. 2010:733). "Viruses do not carry out metabolic activity and rely entirely on host-cell molecular machinery for reproduction. This absence of metabolic and reproductive activity suggests that, unlike cells, the assembly of viruses could perhaps be understood on the basis of equilibrium ...
Phage lytic cyclePhage lytic cycle
This give the virus specificity, meaning that it will only be able to infect a certain host range. Once the viral genome is injected into the cell, then for a DNA phage, bacterial cells RNAP begins transcribing RNAs from certain promoters. The first class of viral genes is intermediate-early genes. Following translation of these genes, the early viral genes are transcribed. These genes encode proteins which get virus ready for DNA replication.. After DNA replication, usually into hundreds of copies, the late viral RNAs are made and translated into proteins. These act as structural components, either for capsid formation or cleaving and packaging of DNA into capsid, or to form the receptor on the capsid surface.. Nucleocapsid:. ...
Theoretical Condensed Matter | Gelbart LabTheoretical Condensed Matter | Gelbart Lab
Bacteriophage lambda, shown in the electron micrograph, consists of a protein capsid 30 nm in radius that has a long cylindrical tail. Its genome, double stranded DNA (dsDNA), is protected by the capsid from attack by nuclease enzymes that would break it down into its nucleotides and therefore lose the genetic information needed to replicate the phage. The DNA contains 48.6 kilo-base pairs; if it were fully extended it would be 17 micrometers long. When the phage is replicated in the host cell, an early form of the capsid, the procapsid, is formed and the DNA is driven into it by a molecular motor at one of the procapsid vertices. This is quite feat! Imagine packing a length of string into an object that is only 1/400th its size. To make the job harder, add negative charges to the string and make it stiff. The stiffness of ds DNA is very high; a measure of this stiffness is its persistence length. It is difficult to bend objects on a scale smaller than the persistence length. The persistence ...
single-molecule biophysics | Gelbart Labsingle-molecule biophysics | Gelbart Lab
Bacteriophage lambda, shown in the electron micrograph, consists of a protein capsid 30 nm in radius that has a long cylindrical tail. Its genome, double stranded DNA (dsDNA), is protected by the capsid from attack by nuclease enzymes that would break it down into its nucleotides and therefore lose the genetic information needed to replicate the phage. The DNA contains 48.6 kilo-base pairs; if it were fully extended it would be 17 micrometers long. When the phage is replicated in the host cell, an early form of the capsid, the procapsid, is formed and the DNA is driven into it by a molecular motor at one of the procapsid vertices. This is quite feat! Imagine packing a length of string into an object that is only 1/400th its size. To make the job harder, add negative charges to the string and make it stiff. The stiffness of ds DNA is very high; a measure of this stiffness is its persistence length. It is difficult to bend objects on a scale smaller than the persistence length. The persistence ...
Mathematical models for tubular structures in the family of Papovaviridae - White Rose Research OnlineMathematical models for tubular structures in the family of Papovaviridae - White Rose Research Online
An important part of a virus is its protein shell, called the viral capsid, that protects the viral genome. While the viral capsids of viruses in the family of Papovaviridae are usually spherical, their protein building blocks are known to assemble also as tubular structures [Kiselev, N.A., Klug, A., 1969. J. Mol. Biol. 40, 155]. In Twarock [2004. J. Theor. Biol. 226, 477] Viral Tiling Theory has been introduced for the structural description of the protein stoichiometry of the spherical capsids in this family. This approach is extended here to the tubular case and is used to classify the surface lattices of tubular structures in the family of Papovaviridae. The predictions of the theory are compared with the experimental results in Kiselev and Klug [1969. J. Mol. Biol. 40, 155]. ...
Maturation | Technology TrendsMaturation | Technology Trends
The capsid protein of HK97, gp5, cross-links upon maturation to form a concatenated chain-mail like structure ... The bacteriophage undergoes a maturation process upon DNA packaging during which it expands by nearly 5 nm and changes from spherically symmetrical to icosahedrally symmetrical ... of gp5 monomers comprise further capsid maturation and lead to formation of a mature phage head ...
Optimization of an Elastic Network Augmented Coarse Grained Model to Study CCMV Capsid Deformation - pdf descargarOptimization of an Elastic Network Augmented Coarse Grained Model to Study CCMV Capsid Deformation - pdf descargar
Optimization of an Elastic Network Augmented Coarse Grained Model to Study CCMV Capsid Deformation. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
Anti-DCV capsid polyprotein antibody (ab92954) | AbcamAnti-DCV capsid polyprotein antibody (ab92954) | Abcam
Rabbit polyclonal DCV capsid polyprotein antibody validated for WB, ELISA, ICC. Referenced in 1 publication and 1 independent review. Immunogen corresponding…
TRIM34 acts with TRIM5 to restrict HIV-1 and SIV capsids - The Luban LabTRIM34 acts with TRIM5 to restrict HIV-1 and SIV capsids - The Luban Lab
Our manuscript, "TRIM34 acts with TRIM5 to restrict HIV-1 and SIV capsids", is now online at bioRxiv. This manuscript is the result of a great tri-lab collaboration. The story springs from a CRISPR loss-of-function screen that was brilliantly designed and expertly conducted by Molly Ohainle in the lab of lab of Michael Emerman at the Hutch in Seattle. Kyusik Kim from my lab at UMass Medical School confirmed the role of these TRIM proteins in primary human blood cells. Our wonderful collaborator Sevnur Komurlu in Ed Campbells lab at Loyola Univ in Chicago provides the groovy images. ...
Team:Heidelberg/Notebook/Capsid Shuffling/ViroBytes - 2010.igem.orgTeam:Heidelberg/Notebook/Capsid Shuffling/ViroBytes - 2010.igem.org
Virobytes is a rational approach to fragment-based DNA shuffling of Adeno-associated viral Cap genes. The method is complementary to our conventional [http://2010.igem.org/Team:Heidelberg/Project/Capsid_Shuffling/Homology_Based homology based DNA shuffling]. ViroByte strategy is based on [http://2009.igem.org/Team:Alberta BioByte] protocol which have been modified in order to enable for randomized fragment assembly ...
Team:Heidelberg/Notebook/Capsid Shuffling/ViroBytes - 2010.igem.orgTeam:Heidelberg/Notebook/Capsid Shuffling/ViroBytes - 2010.igem.org
Virobytes is a rational approach to fragment-based DNA shuffling of Adeno-associated viral Cap genes. The method is complementary to our conventional [http://2010.igem.org/Team:Heidelberg/Project/Capsid_Shuffling/Homology_Based homology based DNA shuffling]. ViroByte strategy is based on [http://2009.igem.org/Team:Alberta BioByte] protocol which have been modified in order to enable for randomized fragment assembly ...
Difference between revisions of Virus - Soft-MatterDifference between revisions of "Virus" - Soft-Matter
Viruses are very small biological constructs which contain either DNA or RNA. As they lack cellular machinery and rely on an infected cell to actually replicate their viral genomes, there is debate as to whether viruses should be considered "living." A virus consists of three main parts. 1) Genetic Material - This can be either DNA or RNA. Upon a viral infection, the virus inserts its genome into the host cell, where it is processed by various polymerases. 2) Protein capsid - this is a simple protein "shell" which envelops the genetic material and gives the virus structure. 3) Coat - there may exist certain proteins or lipids on the surface of the virus that identify the virus and aid in receptor binding to the cell surface. These surface modifications to the virus can induce an immune response in the host organism. The figure to the right is a schematic of a bacteriophage (virus that infects bacteria) inserting its DNA . Viral replication is essentially a positive feedback loop in which the ...
Brian A Kelch PhDBrian A Kelch PhD
I aim to take apart the engine that drives the production of many disease-causing viruses. Most viruses consist of a set of genetic instructions-either DNA or RNA-inside a container made of protein. For viruses that use double-stranded DNA as their genetic material, including herpes virus and the adenovirus that causes respiratory infections, the protein-based shell or "capsid" is assembled first, and the viral DNA is then pumped into it. The molecular machine that performs this pumping is one of the strongest biological motors known: the pressure inside the tight confines of the filled viral capsid is 10 times that of bottled champagne. My laboratory will explore how this motor recognizes the viral DNA and how it pushes this DNA into the capsid, using an innovative combination of structural, biochemical and biophysical techniques. This work will reveal in exceptional detail the workings of this remarkable motor and provide new targets for antiviral therapies ...
X-ray StructuresX-ray Structures
Descriptions of various icosahedral virus capsid structures in terms of their complete capsids, along with detailed structural and computational analysis
Viruses and the Prokaryotic WorldViruses and the Prokaryotic World
Viruses. Viruses and bacteria are too small to be seen without the aid of microscopes. As disease agents, their effects on mankind are well known. Both are ubiquitous and adaptable.. The Bridge Between Living and Non-Living. Someone once suggested that if people were the size of viruses, the entire population of the U.S. would fit on the end of two pencil erasers. There would be room left over for future generations. Extremely small, simple in structure, and widely distributed, viruses exist in a realm all their own. Viruses do not qualify as cells yet affect cells and so exist as if on a bridge between the living and nonliving.. Structure and Classification of Viruses. Viruses differ from cellular organisms in many ways. A virus contains only a single type of nucleic acid. This DNA or RNA may be single or double-stranded. The core of nucleic acid is covered by a protein coat called a capsid. Some of the proteins in the capsid are enzymes. A complete virus particle is called a virion. Some ...
VIPER: EM DatabaseVIPER: EM Database
Descriptions of various icosahedral virus capsid structures in terms of their complete capsids, along with detailed structural and computational analysis
NR 3.0 59619.1NR 3.0 59619.1
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Display of a PorA peptide from Neisseria meningitidis on the bacteriophage T4 capsid surface. | Infection and ImmunityDisplay of a PorA peptide from Neisseria meningitidis on the bacteriophage T4 capsid surface. | Infection and Immunity
The exterior of bacteriophage T4 capsid is coated with two outer capsid proteins, Hoc (highly antigenic outer capsid protein; molecular mass, 40 kDa) and Soc (small outer capsid protein; molecular mass, 9 kDa), at symmetrical positions on the icosahedron (160 copies of Hoc and 960 copies of Soc per capsid particle). Both these proteins are nonessential for phage infectivity and viability and assemble onto the capsid surface after completion of capsid assembly. We developed a phage display system which allowed in-frame fusions of foreign DNA at a unique cloning site in the 5 end of hoc or soc. A DNA fragment corresponding to the 36-amino-acid PorA peptide from Neisseria meningitidis was cloned into the display vectors to generate fusions at the N terminus of Hoc or Soc. The PorA-Hoc and PorA-Soc fusion proteins retained the ability to bind to the capsid surface, and the bound peptide was displayed in an accessible form as shown by its reactivity with specific monoclonal antibodies in an ...
The herpesvirus capsid surface protein, VP26, and the majority of the tegument proteins are dispensable for capsid transport...The herpesvirus capsid surface protein, VP26, and the majority of the tegument proteins are dispensable for capsid transport...
TY - JOUR. T1 - The herpesvirus capsid surface protein, VP26, and the majority of the tegument proteins are dispensable for capsid transport toward the nucleus. AU - Antinone, Sarah E.. AU - Shubeita, George T.. AU - Coller, Kelly E.. AU - Lee, Joy I.. AU - Haverlock-Moyns, Sarah. AU - Gross, Steven P.. AU - Smith, Gregory A.. N1 - Copyright: Copyright 2011 Elsevier B.V., All rights reserved.. PY - 2006/6. Y1 - 2006/6. N2 - Upon entering a cell, alphaherpesvirus capsids are transported toward the minus ends of microtubules and ultimately deposit virus DNA within the host nucleus. The virus proteins that mediate this centripetal transport are unknown but are expected to be either viral tegument proteins, which are a group of capsid-associated proteins, or a surface component of the capsid itself. Starting with derivatives of pseudorabies virus that encode a fluorescent protein fused to a structural component of the virus, we have made a collection of 12 mutant viruses that lack either the VP26 ...
Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics. - Nuffield Department of MedicineMature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics. - Nuffield Department of Medicine
Retroviral capsid proteins are conserved structurally but assemble into different morphologies. The mature human immunodeficiency virus-1 (HIV-1) capsid is best described by a fullerene cone model, in which hexamers of the capsid protein are linked to form a hexagonal surface lattice that is closed by incorporating 12 capsid-protein pentamers. HIV-1 capsid protein contains an amino-terminal domain (NTD) comprising seven α-helices and a β-hairpin, a carboxy-terminal domain (CTD) comprising four α-helices, and a flexible linker with a 310-helix connecting the two structural domains. Structures of the capsid-protein assembly units have been determined by X-ray crystallography; however, structural information regarding the assembled capsid and the contacts between the assembly units is incomplete. Here we report the cryo-electron microscopy structure of a tubular HIV-1 capsid-protein assembly at 8 Å resolution and the three-dimensional structure of a native HIV-1 core by cryo-electron tomography. The
Post-translational modifications in capsid proteins of recombinant adeno-associated virus (AAV) 1-rh10 serotypes [Mass...Post-translational modifications in capsid proteins of recombinant adeno-associated virus (AAV) 1-rh10 serotypes [Mass...
Post-translational modifications in viral capsids are known to fine-tune and regulate several aspects of the infective life cycle of several viruses in the host. Recombinant viruses that are generated in a specific producer cell line are likely to inherit unique post-translational modifications during intra-cellular maturation of its capsid proteins. Data on such post-translational modifications in the capsid of recombinant adeno-associated virus serotypes (AAV1-rh10) is limited. We have employed liquid chromatography and mass spectrometry analysis to characterize post-translational modifications in AAV1-rh10 capsid protein. Our analysis revealed a total of 52 post-translational modifications in AAV2-AAVrh10 capsids, including ubiquitination (17%), glycosylation (36%), phosphorylation (21%), SUMOylation (13%) and acetylation (11%). While AAV1 had no detectable post-translational modification, at least four AAV serotypes had ,7 post-translational modifications in their capsid protein. About 82% ...
Herpesvirus capsid protein - Stock Image F006/9435 - Science Photo LibraryHerpesvirus capsid protein - Stock Image F006/9435 - Science Photo Library
Herpesvirus capsid protein. Molecular model of the major capsid protein VP5 from herpes simplex virus-1 (HSV-1). This virus infects epithelial cells around the mouth, causing fluid-filled blisters known as cold sores. There is no known cure for herpes infection and the virus remains in the body for life. - Stock Image F006/9435
The Structure of the Rotavirus Inner Capsid Studied by Electron Microscopy of Chemically Disrupted Particles | Microbiology...The Structure of the Rotavirus Inner Capsid Studied by Electron Microscopy of Chemically Disrupted Particles | Microbiology...
Summary The inner capsid structure of the OSU strain of porcine rotavirus was studied by electron microscopy of freeze-dried preparations and of negatively stained chemically disrupted virus particles. The analysis of the particles by the freeze-drying technique revealed a T:13 l (laevo) symmetry for the organization of the inner capsid. Treatment of single-capsid rotavirus particles with 30% formamide or 5 m-urea resulted in their degradation, giving rise to very similar products, corresponding to isolated vertices, edges and faces of the virus icosahedron. An analysis of such structures confirmed the triangulation number and handedness of the rotavirus inner capsid, and provided evidence for the open-mesh model, in which the five- and six-coordinated axes are represented by holes formed by smaller trimeric morphological subunits.
The herpesvirus VP1/2 protein is an effector of dynein-mediated capsid transport and neuroinvasion<...The herpesvirus VP1/2 protein is an effector of dynein-mediated capsid transport and neuroinvasion<...
TY - JOUR. T1 - The herpesvirus VP1/2 protein is an effector of dynein-mediated capsid transport and neuroinvasion. AU - Zaichick, Sofia V.. AU - Bohannon, Kevin P.. AU - Hughes, Ami. AU - Sollars, Patricia J.. AU - Pickard, Gary E.. AU - Smith, Gregory A.. PY - 2013/2/13. Y1 - 2013/2/13. N2 - Microtubule transport of herpesvirus capsids from the cell periphery to the nucleus is imperative for viral replication and, in the case of many alphaherpesviruses, transmission into the nervous system. Using the neuroinvasive herpesvirus, pseudorabies virus (PRV), we show that the viral protein 1/2 (VP1/2) tegument protein associates with the dynein/dynactin microtubule motor complex and promotes retrograde microtubule transport of PRV capsids. Functional activation of VP1/2 requires binding to the capsid protein pUL25 or removal of the capsid-binding domain. A proline-rich sequence within VP1/2 is required for the efficient interaction with the dynein/dynactin microtubule motor complex as well as for PRV ...
Metabolic biotinylation of the adenoviral capsid: Avidin-based applications and studies of ligand-targeted gene deliveryMetabolic biotinylation of the adenoviral capsid: Avidin-based applications and studies of ligand-targeted gene delivery
Adenoviral vectors have great potential for use in gene therapy and genetic immunization. The targeting of Ad vectors to the relevant tissue and cell types in vivo could greatly improve their safety and performance by lowering the effective dosage required for therapeutic levels of gene expression. Redirection of Ad vector tropism will require physical modifications of the adenoviral capsid but direct genetic modification of the Ad capsid has so far been limited to small peptides. A novel system for the attachment of targeting ligands to the Ad capsid, based on the extremely strong avidin-biotin interaction, is described herein. The genetic insertion of a biotin acceptor peptide (BAP) into the fiber, protein IX, or hexon components of the Ad capsid has resulted in vectors that are metabolically biotinylated upon production in host cells. Avidin-dependent redirection of transduction through a variety of biotinylated ligands is greatly dependent on the nature of the biotinylated capsid protein. ...
Permalien vers TRIM5 is an innate immune sensor for the retrovirus capsid latticePermalien vers TRIM5 is an innate immune sensor for the retrovirus capsid lattice
Lien vers Pubmed [PMID] - 21512573. Nature 2011 Apr;472(7343):361-5. TRIM5 is a RING domain-E3 ubiquitin ligase that restricts infection by human immunodeficiency virus (HIV)-1 and other retroviruses immediately following virus invasion of the target cell cytoplasm. Antiviral potency correlates with TRIM5 avidity for the retrovirion capsid lattice and several reports indicate that TRIM5 has a role in signal transduction, but the precise mechanism of restriction is unknown. Here we demonstrate that TRIM5 promotes innate immune signalling and that this activity is amplified by retroviral infection and interaction with the capsid lattice. Acting with the heterodimeric, ubiquitin-conjugating enzyme UBC13-UEV1A (also known as UBE2N-UBE2V1), TRIM5 catalyses the synthesis of unattached K63-linked ubiquitin chains that activate the TAK1 (also known as MAP3K7) kinase complex and stimulate AP-1 and NFκB signalling. Interaction with the HIV-1 capsid lattice greatly enhances the UBC13-UEV1A-dependent E3 ...
Immunoinformatics Approach for Designing Epitope-Based Peptides Vaccine of L1 Major Capsid Protein against HPV Type 16 - IJMCRImmunoinformatics Approach for Designing Epitope-Based Peptides Vaccine of L1 Major Capsid Protein against HPV Type 16 - IJMCR
Human papilloma viruses (HPV) are small DNA, non-enveloped, double-stranded and closed circular viruses. There are more than 150 HPV identified types. Genital HPV types are categorized according to their epidemiologic association with cervical cancer to high and low risk types. The high risk type HPV 16 is the most common in the world. we aimed to design a universal peptide based vaccine against HPV type 16 virus using Immunoinformatics Approach through prediction of highly conserved T and B-cell epitopes from the most abundant and highly immunogenic protein (L1 major capsid protein) derived from HPV type 16 strains all over the world. All sequences of the L1 major capsid protein were retrieved from NCBI database. Potentially continuous B and T cell epitopes were predicted using tools from immune epitope data base analysis resource (IEDB-AR). The Allergenicity of predicted epitopes was analyzed by AllerTOP Tool and the coverage was determined throughout the worlds. The B cell epitope 243KSEV246 ...
Self-assembly of hexahistidine-tagged tobacco etch virus capsid protein into microfilaments that induce IgG2-specific response...Self-assembly of hexahistidine-tagged tobacco etch virus capsid protein into microfilaments that induce IgG2-specific response...
Assembly of recombinant capsid proteins into virus-like particles (VLPs) still represents an interesting challenge in virus-based nanotechnologies. The structure of VLPs has gained importance for the development and design of new adjuvants and antigen carriers. The potential of Tobacco etch virus capsid protein (TEV CP) as adjuvant has not been evaluated to date. Two constructs for TEV CP expression in Escherichia coli were generated: a wild-type version (TEV-CP) and a C-terminal hexahistidine (His)-tagged version (His-TEV-CP). Although both versions were expressed in the soluble fraction of E. coli lysates, only His-TEV-CP self-assembled into micrometric flexuous filamentous VLPs. In addition, the His-tag enabled high yields and facilitated purification of TEV VLPs. These TEV VLPs elicited broader IgG2-specific antibody response against a novel porcine reproductive and respiratory syndrome virus (PRRSV) protein when compared to the potent IgG1 response induced by the protein alone. His-TEV CP was
Mutagenesis of N-terminal residues of feline foamy virus Gag reveals entirely distinct functions during capsid formation,...Mutagenesis of N-terminal residues of feline foamy virus Gag reveals entirely distinct functions during capsid formation,...
Foamy viruses (FVs) of the Spumaretrovirinae subfamily are distinct retroviruses, with many features of their molecular biology and replication strategy clearly different from those of the Orthoretroviruses, such as human immunodeficiency, murine leukemia, and human T cell lymphotropic viruses. The FV Gag N-terminal region is responsible for capsid formation and particle budding via interaction with Env. However, the critical residues or motifs in this region and their functional interaction are currently ill-defined, especially in non-primate FVs. Mutagenesis of N-terminal Gag residues of feline FV (FFV) reveals key residues essential for either capsid assembly and/or viral budding via interaction with the FFV Env leader protein (Elp). In an in vitro Gag-Elp interaction screen, Gag mutations abolishing particle assembly also interfered with Elp binding, indicating that Gag assembly is a prerequisite for this highly specific interaction. Gradient sedimentation analyses of cytosolic proteins indicate
JCI - Unique region of the minor capsid protein of human parvovirus B19 is exposed on the virion surface.JCI - Unique region of the minor capsid protein of human parvovirus B19 is exposed on the virion surface.
Capsids of the B19 parvovirus are composed of major (VP2; 58 kD) and minor (VP1; 83 kD) structural proteins. These proteins are identical except for a unique 226 amino acid region at the amino terminus of VP1. Previous immunization studies with recombinant empty capsids have demonstrated that the presence of VP1 was required to elicit virus-neutralizing antibody activity. However, to date, neutralizing epitopes have been identified only on VP2. Crystallographic studies of a related parvovirus (canine parvovirus) suggested the unique amino-terminal portion of VP1 assumed an internal position within the viral capsid. To determine the position of VP1 in both empty capsids and virions, we expressed a fusion protein containing the unique region of VP1. Antisera raised to this protein recognized recombinant empty capsids containing VP1 and VP2, but not those containing VP2 alone, in an enzyme-linked immunosorbent assay. The antisera immunoprecipitated both recombinant empty capsids and human ...
Samuel K-Campos | BIO5Samuel K-Campos | BIO5
Samuel Campos, PhD, studies early events of Human Papillomavirus (HPV) infection. HPVs are small, non-enveloped DNA viruses that cause a variety of lesions ranging from benign waters to cervical cancers. Although over 100 types of HPVs have been identified, HPV16 is the most prevalent, and is alone responsible for more than 50% of cervical cancers in women worldwide. Dr. Campos and his lab study the mechanisms of HPV virus transmission at a cellular level, in hopes to discover new approaches for the prevention and treatment of HPV.HPV16 virions consist of an ~8kb circular dsDNA genome packaged into a ~60 nm protein capsid. The genome is condensed with cellular histones and exists in a chromatin-like state. The capsid is comprised of 72 pentamers of the major capsid protein L1 and up to 72 molecules of the minor capsid protein L2, localized along the inner capsid surface, within the central cavities beneath the L1 pentamers. Mature HPV16 virions exist in an oxidized state, with adjacent L1 ...
EMDB-1710: Cryo-EM 3D model of the icosahedral particle composed of Rous sar... - YorodumiEMDB-1710: Cryo-EM 3D model of the icosahedral particle composed of Rous sar... - Yorodumi
In a mature and infectious retroviral particle, the capsid protein (CA) forms a shell surrounding the genomic RNA and the replicative machinery of the virus. The irregular nature of this capsid shell precludes direct atomic resolution structural analysis. CA hexamers and pentamers are the fundamental building blocks of the capsid, however the pentameric state, in particular, remains poorly characterized. We have developed an efficient in vitro protocol for studying the assembly of Rous sarcoma virus (RSV) CA that involves mild acidification and produces structures modeling the authentic viral capsid. These structures include regular spherical particles with T = 1 icosahedral symmetry, built from CA pentamers alone. These particles were subject to cryoelectron microscopy (cryo-EM) and image processing, and a pseudo-atomic model of the icosahedron was created by docking atomic structures of the constituent CA domains into the cryo-EM-derived three-dimensional density map. The N-terminal domain ...
Identification of Critical Amino Acid in Capsid Protein of PCV2 | The Pig SiteIdentification of Critical Amino Acid in Capsid Protein of PCV2 | The Pig Site
One monoclonal antibody (mAb; 8E4), against the capsid protein of PCV2, was generated and characterised in this study. 8E4 reacted with the genotype PCV2a (CL, LG and JF2) strains but not PCV2b (YJ, SH and JF) strains by an immunoperoxidase mono-layer assay (IPMA) and a capture ELISA. Furthermore, the mAb had the capacity to neutralise PCV2a (CL, LG and JF2) strains but not PCV2b (YJ, SH and JF) strains. One critical amino acid that determined a conformational neutralising epitope was identified using mAb 8E4 and PCV2 infectious clone technique. Amino acid residues 47-72 in the capsid protein of PCV2a/CL were replaced with the corresponding region of PCV2b/YJ, and the reactivity of mAb 8E4 was lost. Further experiments demonstrated that one amino acid substitution, the alanine for arginine at position 59 (A59R) in the capsid protein of PCV2a (CL, LG and JF2) strains, inhibited completely the immunoreactivity of three PCV2a strains with mAb 8E4 ...
Role of RNA Branchedness in the Competition for Viral Capsid Proteins | Avinoam Ben-ShaulRole of RNA Branchedness in the Competition for Viral Capsid Proteins | Avinoam Ben-Shaul
Singararn SW, Garmann RF, Knobler CM, Gelbart WM, Ben-Shaul A. Role of RNA Branchedness in the Competition for Viral Capsid Proteins. JOURNAL OF PHYSICAL CHEMISTRY B. 2015;119 :13991-14002.
The individual papillomavirus type 11 (HPV-11) L1 main capsid protein could - HIV Subtypes B and C gp120 and Methamphetamine...The individual papillomavirus type 11 (HPV-11) L1 main capsid protein could - HIV Subtypes B and C gp120 and Methamphetamine...
The individual papillomavirus type 11 (HPV-11) L1 main capsid protein could be trypsinized to create recombinant capsomeres that retain HPV genotype-restricted capsid antigenicity (M. immunogenic highly, genotype-restricted HPV capsid-neutralizing antigenic domains are included within capsomeres entirely. Thus, capsomeres may be viable vaccine applicants for preventing HPV disease. Papillomaviruses trigger hyperproliferative cutaneous and/or mucosal epithelial lesions in higher vertebrates, including human beings (31). A lot more than 70 genotypically specific human being papillomaviruses (HPVs) have already been identified (12) and may be categorized based on observed variations in disease phenotype (i.e., desired cells tropisms and/or disease organizations). For instance, most HPVs preferentially infect cutaneous pores and skin and usually trigger only harmless disease (e.g., plantar or common warts), while other styles even more infect PF 477736 oral or anogenital mucosal epithelium often. ...
British Library EThOS: Interactions of retroviral capsid proteins with restriction factorsBritish Library EThOS: Interactions of retroviral capsid proteins with restriction factors
It is becoming increasingly clear that mammalian cells can express a variety of factors that limit retroviral replication. One class of these factors blocks replication at a stage post-entry but prior to nuclear import and integration of the viral genome. Members of this family arc known as restriction factors. The best characterised member is the mouse gene hvl which determines susceptibility to infection by MLV. I-vl has two alleles known as Fvl" and Fv/ whose restriction characteristics determine the host range of different MLV strains. It has become apparent that the phenomenon of restriction is not limited to MLV and murine cells. HIV-1, as well as MLV is restricted at a post-entry step in a number of primate species including rhesus macaques. African green monkeys and owl monkeys. The Thm5 gene in these species is the main determinant of both HIV-1 and MLV restriction. Viral determinants of this restriction map to the virus capsid protein, however despite strong genetic ev idence, no ...
Recent advances in the development of HBV capsid assembly modulatorsRecent advances in the development of HBV capsid assembly modulators
Hepatitis B virus (HBV) infections represent a significant burden on global public health. Current HBV treatments using nucleos(t)ide analogs (NAs) and PEG interferons cannot fully alleviate this burden as they do not affect the transcriptional activity of the tenacious covalently closed circular DNA (cccDNA) responsible for viral persistence. Capsid assembly modulators (CAMs) disrupt the encapsidation of pre-genomic RNA and can cause nucleocapsid disassembly, thereby affecting multiple steps of HBV replication and reduction of cccDNA pools. This review provides a concise overview of the development of CAMs and the progress achieved in understanding their interactions with HBV core proteins. ...
Subgenomic capsid protein elisa and antibodySubgenomic capsid protein elisa and antibody
Shop Subgenomic capsid protein ELISA Kit, Recombinant Protein and Subgenomic capsid protein Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
Outer capsid glycoprotein elisa and antibodyOuter capsid glycoprotein elisa and antibody
Shop Outer capsid glycoprotein ELISA Kit, Recombinant Protein and Outer capsid glycoprotein Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
RVA infections induce neutralizing Ab muscles in opposition to outer capsid proteins VP4 and VP7 | IDH Inhibitor idhinhibitor...RVA infections induce neutralizing Ab muscles in opposition to outer capsid proteins VP4 and VP7 | IDH Inhibitor idhinhibitor...
Nevertheless, up to now, this passive immune technique has not been carried out as a therapy for RVA-linked diarrhea. Although Ab muscles can have higher
What Additional Protective Layer Of Protein Surrounds Some Viruses - gabrieldroberts.comWhat Additional Protective Layer Of Protein Surrounds Some Viruses - gabrieldroberts.com
What Additional Protective Layer Of Protein Surrounds Some Viruses - The capsid and envelope play many roles in viral contamination, inclusive of virus attachment to cells, entry into cells, release of the capsid contents into the cells, and packaging of newly fashioned viral debris. The capsid and envelope are also answerable for transfer of the viral genetic material from one mobile to another. these systems also decide the stableness traits of the virus particle, which includes resistance to chemical or bodily inactivation.. The primary role of capsid is to bundle the viral genome. There are strategies related to this feature: the recruitment of the viral RNA all through assembly and the discharge of the genome at some stage in infection. even though particle assembly takes vicinity on endoplasmic reticulum membranes, capsid localizes in nucleoli and lipid droplets.. Because the capsid is outermost, most agents of inactivation must act on the capsid before they can reach the viral RNA, and in ...
EBV Antibody To Viral Capsid Antigen, IgMEBV Antibody To Viral Capsid Antigen, IgM
... ,ARUP Laboratories is a national reference laboratory and a worldwide leader in innovative laboratory research and development. ARUP offers an extensive test menu of highly complex and unique medical tests in clinical and anatomic pathology. Owned by the University of Utah, ARUP Laboratories client,medicine,medical supply,medical supplies,medical product
EBV Antibodies to Viral Capsid Antigen, IgM TestEBV Antibodies to Viral Capsid Antigen, IgM Test
Place an order for EBV Antibodies to Viral Capsid Antigen, IgM testing with Request A Test. Our direct to consumer lab testing service makes it easy and affordable for anyone to get tested.
Birkbeck Institutional Research OnlineBirkbeck Institutional Research Online
The structure of bacteriophage SPP1 capsid was determined at sub-nanometer resolution by cryo-electron microscopy and single-particle analysis. The icosahedral capsid is composed of the major capsid protein gp13 and the auxiliary protein gp12 that are organized in a T=7 lattice. DNA is arranged in layers with a distance of ∼24.5 Å. Gp12 forms spikes that are anchored at the centre of gp13 hexamers. In a gp12-deficient mutant the centres of hexamers are closed by loops of gp13 coming together to protect the SPP1 genome from the outside environment. The HK97-like fold was used to build a pseudo-atomic model of gp13. Its structural organization remains unchanged upon tail binding and following DNA release. Gp13 exhibits enhanced thermostability in the DNA-filled capsid. A remarkable convergence between thermostability of the capsid and of the other virion components was found, revealing that the overall architecture of the SPP1 infectious particle co-evolved towards high robustness.. ...
The refined structure of a protein catenane: the HK97 bacteriophage capsid at 3.44 Å resolutionThe refined structure of a protein catenane: the HK97 bacteriophage capsid at 3.44 Å resolution
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology, Structural Molecular Biology. STRUCTURAL MOLECULAR BIOLOGY. ...
Herpes Simplex Virus Infections | Harrisons Principles of Internal Medicine, 19e | AccessMedicine | McGraw-Hill MedicalHerpes Simplex Virus Infections | Harrison's Principles of Internal Medicine, 19e | AccessMedicine | McGraw-Hill Medical
The viral genome is packaged in a regular icosahedral protein shell (capsid) composed of 162 capsomeres (see Fig. 214e-1). The outer covering of the virus is a lipid-containing membrane (envelope) acquired as the DNA-containing capsid buds through the inner nuclear membrane of the host cell. Between the capsid and lipid bilayer of the envelope is the tegument. Viral replication has both nuclear and cytoplasmic phases. Initial attachment to the cell membrane involves interactions of viral glycoproteins C and B with several cellular heparan sulfate-like surface receptors. Subsequently, viral glycoprotein D binds to cellular co-receptors that belong to the tumor necrosis factor receptor family of proteins, the immunoglobulin superfamily (nectin family), or both. The ubiquity of these receptors contributes to the wide host range of herpesviruses. HSV replication is highly regulated. After fusion and entry, the nucleocapsid enters the cytoplasm and several viral proteins are released from the virion. ...
Order - Herpesvirales - Institut PasteurOrder - Herpesvirales - Institut Pasteur
The virions of Herpesvirales order have complex and characteristic structures consisting of both symmetrical and nonsymmetrical components. The spherical virion is composed of the core, capsid, tegument and envelope. The core consists of the viral genome packaged as a single, linear, dsDNA molecule into a preformed capsid and the DNA is packed in a liquid-crystalline array that fills the entire internal volume of the capsid. The capsids assemble by cocondensation around a protein scaffold to form a procapsid in which the subunits are weakly connected. Proteolytic cleavage of the scaffolding protein triggers loss of scaffold and reorganization of the shell into the characteristic capsid form. The structure of the tegument is poorly defined, with evidence of symmetry only in the region immediately adjacent to the capsid. The tegument contains various proteins, not all of which are required for the formation of virions. The genomes are composed of linear dsDNA ranging from 125 to 295 kbp in size and from
Scientific Protocols - Selection of Phage-displayed peptides that bind to cancer following treatmentScientific Protocols - Selection of Phage-displayed peptides that bind to cancer following treatment
Phage display is a method to discover peptide ligands while minimizing and optimizing the structure and function of proteins (Hallahan, 2003). The phage is used as a scaffold to display recombinant libraries of peptides and provides a means to recover and amplify the peptides that bind to putative receptor molecules in vivo. In vivo selection simultaneously provides positive and subtractive screens because organs and tissues such as tumors are spatially separated. Phage DNA can then be sequenced to determine the amino acid sequence of peptides on the capsid that have been recovered from tumors. The T7 phage display system exploits the T7 capsid protein as a scaffold to display peptides on the capsid protein unique to the 10B protein on the surface of the phage. Gene 10 encoding the capsid protein is cloned with a series of multiple cloning sites at the C-terminus of the 10B protein. The natural translational frame shift site within the capsid gene has been removed so that only a single form of ...
AAV Capsid EngineeringAAV Capsid Engineering
Video, Wyss researchers have created a high-throughput platform to generate an Adeno-associated virus 2 (AAV2) library containing 200,000 variants, each carrying a distinct mutation in the virus capsid protein.
Host cofactors and pharmacologic ligands share an essential interface in HIV-1 capsid that is lost upon disassemblyHost cofactors and pharmacologic ligands share an essential interface in HIV-1 capsid that is lost upon disassembly
The HIV-1 capsid is involved in all infectious steps from reverse transcription to integration site selection, and is the target of multiple host cell and pharmacologic ligands. However, structural studies have been limited to capsid monomers (CA), and the mechanistic basis for how these ligands inf …
How physics can be used to understand viruses - Advanced Science NewsHow physics can be used to understand viruses - Advanced Science News
In a recent study published in WIREs Nanomedicine & Nanobiotechnology, Dr. Wouter Roos and co-workers from the Rijksuniversiteit Groningen in the Netherlands explore physics-based studies of viral systems and the recently fast-growing field of physical virology. Capsid formation can occur through the self-assembly of all the viral components or by actively packaging genome using a molecular motor after a pro-capsid has been formed. "In the simplest scenario of capsid formation, the functional capacity to self-assemble resides in the primary amino-acid sequence of the capsid proteins and, hence, the folded structure of the viral protein subunits. Thus, the assembly process is solely driven by protein-protein and, for co-assembly with viral nucleic acids, protein-genome interactions," according to the authors in their study. "The balancing of these interactions…, implicitly conditioned by the surrounding environment, will ultimately determine the assembly pathway(s)." Indeed, different ...
Protein-RNA interactions in an icosahedral virus at 3.0 A resolution | ScienceProtein-RNA interactions in an icosahedral virus at 3.0 A resolution | Science
Nearly 20 percent of the packaged RNA in bean-pod mottle virus (BPMV) binds to the capsid interior in a symmetric fashion and is clearly visible in the electron density map. The RNA displaying icosahedral symmetry is single-stranded with well-defined polarity and stereochemical properties. Interactions with protein are dominated by nonbonding forces with few specific contacts. The tertiary and quaternary structures of the BPMV capsid proteins are similar to those observed in animal picornaviruses, supporting the close relation between plant comoviruses and animal picornaviruses established by previous biological studies. ...
A Carnivorous Plant and its Bug - In Defense of PlantsA Carnivorous Plant and its Bug - In Defense of Plants
Living on Roridula plants are tiny capsid bugs that are covered in a special waxy substance that keeps them from getting stuck in the sticky traps. The bugs move about the sticky leaves, looking for trapped insects. When the insects are found, the capsid bugs impale them with their proboscis and suck them dry. As the capsid bugs feed, their droppings end up littering the Roridula leaves. This is how Roridula gets the added nutrients it needs to survive. Although the plants are not capable of actively digesting the full insects, they are capable of absorbing the components of the capsid bug feces. They are literally getting a little bit of fertilizer every time a capsid bug goes to the bathroom. By offering the capsid bugs a place to live and plenty of free, immobilized prey, the plant is able to get nitrogen-rich meals in return!. Photo Credit: Alex Lomas, CARNIVORASLAND, and Darwiniana. Further Reading ...
620bv) Enzyme Encapsulation Using Cell Free Protein Synthesis | AIChE620bv) Enzyme Encapsulation Using Cell Free Protein Synthesis | AIChE
Enzyme Encapsulation using Cell Free Protein Synthesis Seung-Ook Yang, Bradley C. Bundy Abstract. Nature has evolved to bear a micro-compartmentalization strategy for a number of various functions, such as protection and delivery of cargo molecules, regulation of chemical reaction, assisting proper folding of proteins, etc. These characteristics interest many biotechnologists to utilize viral and non-viral capsids to mimic nature for many applications. To date, a small number of viral capsids have been used to encompass enzymes to build nanoreactors. For example, Bacteriophage Q-betas coat protein self-assembles into a 180-membered virus capsid. Recent studies show this capsid has an ability to encapsulate enzymes when co-produced. Substrates and product diffuse through pores in the capsid, while the encapsulated enzyme is protected and stabilized from biologically harsh conditions. Here we demonstrate the utility of a cell free protein synthesis (CFPS) environment for improved control over the ...
Highlights of our WorkHighlights of our Work
When human immundeficiency virus (HIV) infects a human cell, it releases into the interior of the cell its capsid (made of about 1,300 identical so-called CA proteins), a closed, stable container that protects the viral genetic material (see also June 2013 highlight Elusive HIV-1 Capsid and August 2015 highlight Anatomy of a Dormant Killer). Once in the cell ― while avoiding detection by cellular proteins ― the capsid deceives the cell and directs the cell machinery to transport it to the nucleus. The human-cell protein Cyclophilin A (CypA) is thereby exploited to act against the cells well being and to assist the HIV infection by getting the capsid to access the cell nucleus; this results in a delicate choreography accomplished by escaping anti-viral proteins in the cell and deceiving transport proteins at the nucleus, all of which contain a CypA domain that interacts directly with the capsid. Despite the availability of the crystal structure of the complex of CypA and CA proteins ...
LCO Technical FilesLCO Technical Files
This section of the Laboratory of Cellular Oncologys website gives detailed technical information about the production and manipulation of human papillomavirus (HPV) and polyomavirus (PyV) based gene delivery vectors. Such vectors are also known as pseudoviruses. They are generated by co-expressing the two viral capsid proteins (L1 and L2 (HPVs) or VP1 and VP2/3 (PyVs)) using codon-modified expression constructs. The two capsid proteins are necessary and sufficient for intracellular packaging of reporter plasmids within mammalian 293TT cells. The resulting high-titer pseudovirus stocks can deliver packaged reporter plasmids to a wide variety of cell types in vitro and in vivo ...
VirusesViruses
Introduction to Virus Structure Tutorial Jonathan King, Peter Weigele, Greg Pintilie, David Gossard (MIT) v.November, 2008 Virus Structure • Size вЂ" • Basic shape вЂ" вЂ" • 17 nm вЂ" 3000 nm diameter Rod-like “Spherical” Protective Shell - Capsid вЂ" Made of many identical protein subunits вЂ" Symmetrically organized вЂ" 50% of weight вЂ" Enveloped or non-enveloped • Genomic material вЂ" DNA or RNA вЂ" Single- or double-stranded Virus Structure • Virus capsids function in: вЂ" Packaging and protecting nucleic acid вЂ" Host cell recognition • Protein on coat or envelope “feels” or “recognizes” host cell receptors вЂ" Genomic material delivery • Enveloped: cell fusion event • Non-enveloped: more complex strategies & specialized structures Electron Microscopy Mitra, K. & Frank, J., 2006. Ribosome dynamics: insights from atomic structure modeling into cryo-electron microscopy maps. Annual review of ...
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SubunitsVirusesViral capsid proteinsMaturationAssemblyMolecularMoleculeHerpesvirus capsidsNucleusMoleculesGenesSubunitShellsMammalian cellsStabilityStructuresProtein shellBindInfectionVivoMacromolecularStructureInduceProteinsGenomeInhibitorStructuralAntibodiesAntibodyProtein capsidReplicationEncloses the genetic materialBacteriophageTransductionParts of the capsidStructure of the capsidInhibitors2018GeneticViruses have capsidsSubunits called capsomeresPeptidesHexamersComplex capsidVirionPentamersWhole capsidUnique capsidHerpesvirus capsidIcosahedral capsidsCryo-Electron MEgressGeneAntiviral activityResiduesSelf-assemblesNuclearAsymmetric unitPicornavirusVectorsMeSHCapsomeres
Subunits5
Viruses3
  • Self-assembly of viruses seems to obey the principles of thermodynamically reversible self-assembly but assembled shells ('capsids') strongly resist disassembly. (asknature.org)
  • Here, we utilize crystal structures of the capsid protein from the smallest and simplest known viruses capable of autonomously replicating in animal cells, circoviruses, to establish structural and mechanistic insights into capsid morphogenesis and regulation. (edu.au)
  • with the support of Stuart Turville from the Kirby Institute team developed special viruses with fluorescent labels to monitor the life of the capsid. (life4me.plus)
Viral capsid proteins1
Maturation1
Assembly3
  • In these cases, the genome is usually inserted, after capsid assembly has been completed, by the action of a rotary molecular motor imbedded in the capsid. (asknature.org)
  • However, we do not understand how key nuclear processes, including capsid assembly, genome replication, capsid packaging, and nuclear egress, are dynamically connected in space and time. (asm.org)
  • We show that assembly of these complexes is regulated by single-stranded DNA (ssDNA), and provide a structural basis of capsid assembly around single-stranded DNA, highlighting novel binding interfaces distinct from the highly positively charged N-terminal ARM domain. (edu.au)
Molecular8
  • Moreover, no direct link between nuclear capsid motility and a molecular motor has been established. (asm.org)
  • Nevertheless, the molecular mechanism of nucleotide import into the capsid remains unknown. (udel.edu)
  • Employing all-atom molecular dynamics simulations, we established that cooperative binding between nucleotides inside a CA hexamer cavity results in energetically-favorable conditions for passive translocation of dNTPs into the HIV-1 capsid. (udel.edu)
  • We further examined the variation of the PPI indices as a function of the molecular weight of the coat protein subunit and the capsid diameter. (scripps.edu)
  • Our results suggest that the PPI indices in T=1 and pseudo-T=3 capsids vary linearly with the molecular weight of the subunit and capsid size. (scripps.edu)
  • The striking outcome of this analysis is the distinctive clustering of the "T=2" capsids, which are distinguished by higher subunit molecular weights and a much lower degree of protein-protein interactions. (scripps.edu)
  • A group of British specialists, using a new method of unimolecular microscopy, developed at the Faculty of Molecular Science of UNSW at the Medical Faculty, found that HIV, creating a shield against immunity, to strengthen its capsid includes a specific molecule of the host cell, inositol-hexakisphosphate. (life4me.plus)
  • The HIV Capsid has been studied extensively for a long time, but the question of its stability and balance at the time of the" merger "has so far been one of the key in HIV biology," commented Dr. Leo James, head of the research group at the Laboratory molecular biology Research Council in Cambridge. (life4me.plus)
Molecule2
  • Scientists from the University of New South Wales (UNSW, UK) found that the special protein capsid envelope created by HIV at the time of entry into the human body uses a specific host cell molecule, inositol-hexakisphosphate, as a shield from immunity. (life4me.plus)
  • When you bind this molecule, you stabilize the capsid and open the path to the cell to penetrate it", explains Becking. (life4me.plus)
Herpesvirus capsids2
Nucleus3
  • Only latrunculin A treatment stalled nuclear capsids but did so by an unexpected effect: the drug induced actin rods in the nucleus. (asm.org)
  • The latter gives the capsid stability and allows unhindered to carry the genetic material of the virus to the nucleus of the cell. (life4me.plus)
  • The diffusive way out: Herpesviruses remodel the host nucleus, enabling capsids to access the inner nuclear membrane. (princeton.edu)
Molecules3
  • Collectively, our results provide an atomistic description of the permeability of the HIV-1 capsid to small molecules and reveal a novel mechanism for the involvement of metabolites in HIV-1 capsid stabilization, nucleotide import and reverse transcription. (udel.edu)
  • Now we can see the influence of different molecules on the capsid and accurately determine when it starts to break down," Bucking said. (life4me.plus)
  • While there are methods for sequencing RNA molecules, these methods are not applicable to Fig. 11.6 The famous Kleinschmidt electron micrograph of phage T4 DNA extruded from the capsid. (americorpshealth.biz)
Genes1
Subunit1
Shells1
Mammalian cells1
  • The scientists found that inositol-hexakisphosphate, which is present in large numbers inside mammalian cells, makes the capsid much stronger, stabilizing it for 10-20 hours. (life4me.plus)
Stability2
  • These resilient proteinaceous packets self-assemble in response to a variety of weak forces that, in concert, provide the capsid with a great deal of stability. (asknature.org)
  • To extend RNAi to the in vivo applications, we here demonstrated that the siRNA/capsid nanocarrier complexes could have tumor-specific targeting ability in vivo as well as the increased stability of siRNA during body circulation. (elsevier.com)
Structures2
  • The weak forces at work include attraction or repulsion between electrostatic charges, water solubility, and constituent amino acid structures in various parts of the capsid. (asknature.org)
  • The capsid protein forms distinct macromolecular assemblies during replication and here we elucidate these structures at high resolution, showing that these complexes reverse the exposure of the N-terminal arginine rich domain responsible for DNA binding and nuclear localization. (edu.au)
Protein shell1
Bind1
  • Immobile capsids accumulated around actin rods, and immunoprecipitation experiments suggested that capsid motility stopped because latrunculin-induced actin rods nonspecifically bind nuclear capsids. (asm.org)
Infection2
  • We show for representative members of all three herpesvirus subfamilies that nuclear capsid motility is not dependent on nuclear F-actin and that herpesvirus infection does not induce nuclear F-actin in primary fibroblasts. (asm.org)
  • Capsids should be much more stable inside the cell, because the process of infection takes several hours, not minutes. (life4me.plus)
Vivo2
  • The enhanced longevity of siRNA in vivo could be explained by shielding effect derived from the capsid shell, where the encapsulated siRNAs are protected from nucleases in plasma. (elsevier.com)
  • Moreover, the prolonged in vivo circulation time of our siRNA/capsid nanocarrier complexes increased the potential to serve as siRNA carriers for optimal in vivo RNAi. (elsevier.com)
Macromolecular1
  • Recently, we reported that a chimeric capsid protein assembled into a macromolecular container-like structure with capsid shell and the resulting siRNA/capsid nanocarrier complexes efficiently suppressed RFP gene expression in the cell culture system. (elsevier.com)
Structure1
Induce1
  • Interestingly, capsid motility was unaffected in cells that do not induce actin rods. (asm.org)
Proteins47
  • The capsid faces may consist of one or more proteins. (wikipedia.org)
  • For example, the foot-and-mouth disease virus capsid has faces consisting of three proteins named VP1-3. (wikipedia.org)
  • The capsid of spherical viruses is built from a limited number of proteins and often displays icosahedral symmetry. (ebi.ac.uk)
  • The proteins forming the capsid are VP2 (internal layer, with triangulation T = 1 and an asymmetric dimer in the icosahedral repeating unit), VP6 (intermediate layer, T = 13 symmetry), VP7 (external layer, T = 13) and VP4, which forms a spike inserted in the outermost two layers. (ebi.ac.uk)
  • Extensive antigenic mimicry by retrovirus capsid proteins. (nih.gov)
  • The viral capsid of Picornaviruses is composed of 60 icosahedral copies of four capsid proteins, VP1, VP2, VP3 and VP4, enclosing the viral positive-strand RNA genome. (ebi.ac.uk)
  • VP4 lies on the inner surface of the protein shell formed by the major capsid proteins, VP1, VP2 and VP3. (ebi.ac.uk)
  • The three major capsid proteins have a conserved beta-barrel fold, while VP4 has little regular secondary structure. (ebi.ac.uk)
  • The organisation of the three major capsid proteins leads to surface depressions, or pits, thought to be involved in receptor binding, while the variable outer rim is involved in antibody recognition. (ebi.ac.uk)
  • Water-soluble Au 102 ( para -mercaptobenzoic acid) 44 clusters, functionalized by maleimide linkers to target cysteines of viral capsid proteins, were synthesized and conjugated to enteroviruses echovirus 1 and coxsackievirus B3. (pnas.org)
  • TaV particles have a buoyant density of 1.296 g/cm3 in CsCl and consist of two capsid proteins of 56 and 6 kDa. (nih.gov)
  • The N-terminal sequences of the capsid proteins were compared with the nucleotide sequence of the capsid open reading frame. (nih.gov)
  • The sequences indicate that the pre-protein is cleaved at two positions to produce the 56 and 6 kDa capsid proteins as well as a predicted third protein that was not detected in the mature virion. (nih.gov)
  • Phylogenetic analysis of the capsid proteins indicated that TaV is more closely related to NbetaV than to the Nudaurelia omega-like viruses. (nih.gov)
  • These capsids show structural variations of the same framework, with 60 asymmetric or symmetric homodimers for ScV-L-A and PsV-F, respectively, monomers with a duplicated similar domain for PcV, and heterodimers of two different proteins for RnQV1. (mdpi.com)
  • Mycovirus capsid proteins (CP) share a conserved α-helical domain, although the latter may carry different peptides inserted at preferential hotspots. (mdpi.com)
  • Infectivity of these mutants ranged from 5 to 100% of that of the wild-type, demonstrating for the first time the ability to alter capsid proteins without interfering with infectivity. (nih.gov)
  • Picornaviruses are non-enveloped plus-strand ssRNA animal viruses with icosahedral capsids composed of 60 copies each of 4 virus encoded proteins. (abcam.com)
  • The core is surrounded by a protective coat of proteins called the capsid. (jove.com)
  • Some viruses have capsids that are enclosed by an envelope of lipids and proteins outside of the capsid. (jove.com)
  • In the strain UCD 67-385, these both proteins were identified as viral capsid protein (CP), allow to confirm the gag predicted ORFs in XdV-L1A, XdV-L1B, and XdV-L2, with CPs of 76.6, 76.2, and 38.8 kDa, respectively. (springer.com)
  • Dai and Zhou used electron microscopy to determine a high-resolution structure of the HSV-1 capsid bound to the tegument proteins that occupy the space between the capsid and the nuclear envelope. (sciencemag.org)
  • By using cryo-electron microscopy, we obtained an atomic model of the HSV-1 capsid with CATC, comprising multiple conformers of the capsid proteins VP5, VP19c, VP23, and VP26 and tegument proteins pUL17, pUL25, and pUL36. (sciencemag.org)
  • The single C-terminal helix of pUL36 resolved in the CATC links the capsid to the outer tegument and envelope: As the largest tegument protein in all herpesviruses and essential for virion formation, pUL36 has been shown to interact extensively with other tegument proteins, which in turn interact with envelope glycoproteins. (sciencemag.org)
  • The HIV-1 Gag consists of four domains-matrix (MA), capsid (CA), nucleocapsid (NC) and p6-and two short peptides, SP1 and SP2, that are cleaved into distinct proteins by the viral protease during maturation. (springer.com)
  • Bluetongue virus outer capsid proteins are sufficient to trigger apoptosis in mammalian cells. (semanticscholar.org)
  • In vitro recoating of reovirus cores with baculovirus-expressed outer-capsid proteins mu1 and sigma3. (semanticscholar.org)
  • Immature or B capsids of herpes simplex virus type 1 (HSV-1) are composed of seven proteins encoded by six viral genes. (semanticscholar.org)
  • These modifications were achieved by chemical coupling of a ligand by the formation of a thiourea functionality between the amino group of the capsid proteins and the reactive isothiocyanate motif incorporated into the ligand. (rsc.org)
  • Gilead's tool compound, GS-CA1 (light green, right), binds between two capsid proteins in the pinwheel-like hexamer. (acs.org)
  • But when Gilead began the project, not much was known about the capsid, which is made up of 1,500 capsid proteins that organize themselves into hexamers and pentamers to form an eggplant-shaped shell. (acs.org)
  • A major focus has been on the use of systems that express the structural proteins of the virus that self-assemble to generate "empty capsid" particles which share many features with the intact virus but lack the ribonucleic acid genome and are therefore non-infectious. (dovepress.com)
  • Pre-clinical immunogenicity of human papillomavirus alpha-7 and alpha-9 major capsid proteins. (nih.gov)
  • Phylogenetic relationship between the major capsid proteins of the Alpha-7 and Alpha-9 genotypes. (nih.gov)
  • A) Amino acid sequences of the L1 major capsid proteins representing both VLP and pseudoviruses of the Alpha-7 (HPV18, HPV39, HPV45, HPV59, HPV68) and Alpha-9 (HPV16, HPV31, HPV33, HPV35, HPV52, HPV58) genotypes and the control BPV . (nih.gov)
  • This communication describes the in vitro assembly of genetically recombinant Cucumber Mosaic Virus (CMV) viral capsid proteins (CPs) into biological nanotubes, several micrometres long yet with a diameter of only 17 nm, triggered by double-stranded DNAs of different lengths. (whiterose.ac.uk)
  • Here, we provide electron microscopy-based data demonstrating the association of both nuclear capsids and NEC proteins at nuclear lamina budding sites. (mdpi.com)
  • Rubella virus is an enveloped positive-strand RNA virus of the family TOGAVIRIDAE: Virions are composed of three structural proteins: a capsid and two membrane-spanning glycoproteins, E2 and E1. (acris-antibodies.com)
  • Proteins of the fungal virus capsid (RnQV1) with the different domains and insertions highlighted in different colours. (csic.es)
  • Evolution has allowed modifications in very specific domains of the proteins that form the capsid. (csic.es)
  • To reach this conclusion, the authors studied the atomic structure of the proteins that form the viral capsid and identified two domains with enzyme activity. (csic.es)
  • Impact of Naturally Occurring Variation in the Human Papillomavirus (HPV) 58 Capsid Proteins on Recognition by Type-Specific Neutralizing Antibodies. (bioportfolio.com)
  • We investigate the impact of variation within the major (L1) and minor (L2) capsid proteins of HPV58 on susceptibility to neutralizing antibodies. (bioportfolio.com)
  • Impact of naturally occurring variation in the human papillomavirus 52 capsid proteins on recognition by type-specific neutralising antibodies. (bioportfolio.com)
  • We investigated the impact of naturally occurring variation within the major (L1) and minor (L2) capsid proteins on the antigenicity of human papillomavirus (HPV) type 52 (HPV52). (bioportfolio.com)
  • They are often composed of CAPSID PROTEINS, especially L1 protein, from various types of ALPHAPAPILLOMAVIRUS. (bioportfolio.com)
  • A vaccine containing L1 capsid proteins from four types of HPV (ALPHAPAPILLOMAVIRUS), types 6, 11, 16 and 18 that is used to prevent infections from HUMAN PAPILLOMAVIRUSES of these subtypes. (bioportfolio.com)
Genome26
  • Rotaviruses have a segmented double-stranded RNA genome enclosed in a complex capsid formed by three concentric protein layers. (ebi.ac.uk)
  • Viral protein that forms an icosahedral capsid with a T=25 symmetry to protect the viral genome. (uniprot.org)
  • These capsids, which remain structurally undisturbed throughout the viral cycle, nevertheless, are dynamic particles involved in the organization of the viral genome and the viral polymerase necessary for RNA synthesis. (mdpi.com)
  • Within the capsid, fungal dsRNA viruses show a low degree of genome compaction compared to reoviruses, and contain one to two copies of the RNA-polymerase complex per virion. (mdpi.com)
  • The capsid and genome-containing core are together known as the nucleocapsid. (jove.com)
  • The nucleic acid genome fits inside the grooves of the helical capsid. (jove.com)
  • The viral capsid not only protects the virus's genome, but it also plays a critical role in interactions with host cells. (jove.com)
  • In these cases, the genome is usually inserted, after capsid assembly has been completed, by the action of a rotary molecular motor imbedded in the capsid. (asknature.org)
  • Herpesviruses comprise a large DNA genome enclosed in a large and complex protein cage called a capsid (see the Perspective by Heldwein). (sciencemag.org)
  • As an HBV inhibitor, NZ-4 leads to the formation of genome-free capsids, including a new population of capsid that runs faster on agarose gels. (sigmaaldrich.com)
  • In this regard, successful viral spread relies on the capability of viral capsids to (i) shelter the viral genome, (ii) display molecular determinants for cell receptor recognition, (iii) facilitate efficient genome delivery, and (iv) escape from the immune system. (frontiersin.org)
  • The outer capsid protein of rice dwarf virus is encoded by genome segment S8. (semanticscholar.org)
  • However, we do not understand how key nuclear processes, including capsid assembly, genome replication, capsid packaging, and nuclear egress, are dynamically connected in space and time. (asm.org)
  • The HIV capsid (left) protects the viral genome so it can be delivered into host cells. (acs.org)
  • Aside from its obvious appeal as a vital shield for the viral genome, the capsid offers a potential solution to the resistance problem that plagues HIV treatment. (acs.org)
  • The region of the viral genome that encodes for the capsid protein is among its most unchanged stretches, explains Vanderbilt University virologist Christopher Aiken. (acs.org)
  • genome is 16µm and it is stored in a 58 nm diameter spherical capsid (primary source). (harvard.edu)
  • genome takes up a volume of roughly 50,000nm^3 which should be compared to 100,000nm^3, the approximate volume available within the capsid. (harvard.edu)
  • A point mutation in the core protein in which a phenylalanine at position 97 is exchanged for a smaller leucine leads to premature envelopment of the capsid before the genome maturation is fully completed. (pdbj.org)
  • Upon membrane insertion, L2 recruits the cytosolic retromer, which enables the L2 viral genome complex to enter the retrograde transport pathway and traffic to the Golgi en route for infection. (rupress.org)
  • To hide from components of our immune system that are active inside the cell, HIV uses a protein shell called a capsid, which protects its genome from detection and destruction. (elifesciences.org)
  • This is because the capsid must be strong enough to survive for hours inside the cell but not so strong that it cannot quickly open when the virus needs to release its genome. (elifesciences.org)
  • This allows HIV to copy its genome inside the capsid, meaning it remains protected while the virus prepares to produce new viruses. (elifesciences.org)
  • Before the virus can integrate its genes into the host genome, it must reverse transcribe its RNA into DNA, travel to the nucleus, remove its protective capsid (uncoating) and target actively transcribing chromatin. (elifesciences.org)
  • Here, we use timeresolved small-angle X-ray scattering to uncover the nonequilibrium self-assembly dynamics of icosahedral viral capsids packaging their full RNA genome. (cea.fr)
  • The binding energy of capsid subunits on the genome is moderate (~7k B T 0 , with k B the Boltzmann constant and T 0 = 298 K, the room temperature), while the energy barrier separating the complexes and the virions is high (~ 20k B T 0 ). (cea.fr)
Inhibitor6
  • Effect of a hepatitis B virus inhibitor, NZ-4, on capsid formation. (sigmaaldrich.com)
  • In 2017, GS-CA1, a highly potent capsid inhibitor, was described that holds promise for clinical development. (ovid.com)
  • FOSTER CITY, Calif.--( BUSINESS WIRE )--Gilead Sciences, Inc. (NASDAQ:GILD) today announced data on GS-6207, an investigational, novel, selective, first-in-class inhibitor of HIV-1 capsid function, that support its further development and potential role as a component in long-acting HIV combination therapy. (businesswire.com)
  • This is an ongoing double-blind, placebo-controlled, proof-of-concept Phase 1b study in people living with HIV who are capsid inhibitor-naïve. (businesswire.com)
  • By 2018, Gilead expects to begin human studies of a capsid inhibitor with the potential to be dosed once a month or less frequently. (acs.org)
  • It will be the first time a capsid inhibitor makes it to the clinic. (acs.org)
Structural8
Antibodies8
Antibody3
Protein capsid1
  • Enteroviruses belong to a large family of picornaviridae, which are about 30- to 35-nm icosahedral bionanoparticles consisting of a protein capsid without a lipid envelope ( 1 ). (pnas.org)
Replication3
  • Human immunodeficiency virus-1 capsid (HIV-1 CA) is involved in different stages of the viral replication cycle. (springer.com)
  • CAMs also inhibit formation of HBV covalently closed circular DNA (cccDNA), probably by interfering with capsid disassembly, an early step in viral replication. (worldhepatitisalliance.org)
  • Our previous work established that little, if any, wild type AAV replication occurs in mouse tissues whether a mouse or human adenovirus is used as the helper virus (1), thus preventing the cross-selection for mouse cell transduction by AAV capsids. (cavd.org)
Encloses the genetic material2
Bacteriophage2
  • Johnson, John E. 2009-02-08 00:00:00 Lambda-like double-stranded (ds) DNA bacteriophage undergo massive conformational changes in their capsid shell during the packaging of their viral genomes. (deepdyve.com)
  • Although various mature capsids have been characterized at atomic resolution, no such procapsid structure is available for a dsDNA virus or bacteriophage. (deepdyve.com)
Transduction5
  • The relative transduction of the new capsid serotypes will be compared with standard AAV vector serotypes currently used in, or being considered for, clinical trials. (cavd.org)
  • Selection approaches that use replicating AAVs have the potential to lessen problems of cross-packaging (a phenomenon whereby capsids package gene sequences that are unrelated to the capsid utilized for transduction) after multiple rounds of passaging. (cavd.org)
  • Perhaps even more importantly, it has become clear that capsid-mediated cellular AAV binding and uptake are not the only parameters that influence the efficiency, cell-type and species-specific transduction properties. (cavd.org)
  • In this report, we describe the development of a modified adeno-associated virus (AAV) capsid and promoter for transduction of retinal ON-bipolar cells. (harvard.edu)
  • Avidin-dependent redirection of transduction through a variety of biotinylated ligands is greatly dependent on the nature of the biotinylated capsid protein. (rice.edu)
Parts of the capsid2
  • The weak forces at work include attraction or repulsion between electrostatic charges, water solubility, and constituent amino acid structures in various parts of the capsid. (asknature.org)
  • Here, the rates at which chloride and sodium ions do so differ substantially, and the two ions also bind to different parts of the capsid. (thebodypro.com)
Structure of the capsid1
  • We have used electron cryo-microscopy and image processing to investigate how the point mutation affects the structure of the capsid at 2.6- to 2.8 Å-resolution. (pdbj.org)
Inhibitors6
  • Ke, Y.Y. & Lin, T.H. Modeling the ligand-receptor interaction for a series of inhibitors of the capsid protein of enterovirus 71 using several three-dimensional quantitative structure-activity relationship techniques. (nature.com)
  • To summarize recent advances in the discovery of chemical inhibitors targeting the HIV capsid and research on their mechanisms of action. (ovid.com)
  • Inhibitors may bind to several different positions on the capsid protein, including sites in both protein domains. (ovid.com)
  • However, the antiviral activity of many reported capsid-targeting inhibitors has not been definitively linked to capsid binding. (ovid.com)
  • Until recently, the low-to-moderate potency of reported capsid-targeting inhibitors has precluded their further clinical development. (ovid.com)
  • Small molecules that bind to the viral capsid protein can be potent inhibitors of HIV infection. (ovid.com)
20181
  • CAPSID (2018-19) incorporated 250 artworks, and was the result of a collaboration between the artist and molecular virologist Professor Greg Towers of University College London. (artscouncilcollection.org.uk)
Genetic13
  • Once the virus has infected a cell and begins replicating itself, new capsid subunits are synthesized according to the genetic material of the virus, using the protein biosynthesis mechanism of the cell. (wikipedia.org)
  • Researchers report that they have determined the precise chemical structure of the HIV capsid, a protein shell that protects the virus' genetic material and is a key to its virulence. (nsf.gov)
  • One of the functions of the capsid is to aid the transmission of the viral genetic material into host cells. (sciencephoto.com)
  • Viral determinants of this restriction map to the virus capsid protein, however despite strong genetic ev idence, no direct interaction has been shown between capsid and restriction factor using a variety of biochemical approaches. (bl.uk)
  • This strategy does not require genetic engineering of the capsid sequence. (rsc.org)
  • HIV's capsid is a complex, protein-rich shell that protects the genetic payload the virus is trying to sneak into the cells of its host. (acs.org)
  • BOSTON & WALTHAM, Mass.--( BUSINESS WIRE )--Vertex Pharmaceuticals Incorporated (Nasdaq:VRTX) and Affinia Therapeutics announced today that the two companies have entered into a strategic research collaboration to engineer novel adeno-associated virus (AAV) capsids to deliver transformative genetic therapies to people with serious diseases. (businesswire.com)
  • The collaboration will leverage Affinia Therapeutics' capsid engineering expertise and Vertex's scientific, clinical and regulatory capabilities to accelerate the development of genetic therapies for people affected by Duchenne muscular dystrophy (DMD), myotonic dystrophy type 1 (DM1) and cystic fibrosis (CF). (businesswire.com)
  • Affinia Therapeutics' innovative approach to the discovery and design of AAV capsids brings yet another tool to our Vertex Cell and Genetic Therapies toolkit, and we're excited to partner with them to bring together their technology platform with our research and development expertise. (businesswire.com)
  • Vertex will be responsible for and will fund the design and manufacturing of genetic therapies incorporating the selected capsids, preclinical and clinical development efforts, and commercialization of any approved products in the licensed diseases. (businesswire.com)
  • In plant, animal and bacterial viruses, the primary function of the virus capsid is to protect the genetic material and identify its hosts, but in fungal viruses these functions are less important. (csic.es)
  • Redirection of Ad vector tropism will require physical modifications of the adenoviral capsid but direct genetic modification of the Ad capsid has so far been limited to small peptides. (rice.edu)
  • The genetic insertion of a biotin acceptor peptide (BAP) into the fiber, protein IX, or hexon components of the Ad capsid has resulted in vectors that are metabolically biotinylated upon production in host cells. (rice.edu)
Viruses have capsids2
Subunits called capsomeres2
Peptides1
Hexamers3
  • The triangulation number T for the capsid is defined as: T = h 2 + h ⋅ k + k 2 {\displaystyle T=h^{2}+h\cdot k+k^{2}} Icosahedral capsids contain 12 pentamers plus 10(T − 1) hexamers. (wikipedia.org)
  • It is similar to the stochastic model of fullerene growth, but takes into account variations in the composition of pentamers and hexamers that are responsible for the final capsid size. (hindawi.com)
  • An arginine ring within the pore coordinates IP 6 , which strengthens capsid hexamers by almost 10°C. Single molecule measurements demonstrate that this renders native HIV capsids highly stable and protected from spontaneous collapse. (elifesciences.org)
Complex capsid1
Virion3
Pentamers2
Whole capsid2
  • whole capsid was built from instances of one capsomere unit, makes the file very small, fast, and easy to use. (turbosquid.com)
  • That leads to a "delicate equilibrium in the whole capsid shell, which we thought could really be its Achilles' heel," Cihlar, who conceived of the capsid program back in 2006, adds. (acs.org)
Unique capsid2
  • This paper presents evidence that Thosea asigna virus (TaV) has a unique capsid expression strategy and is a member of the Nudaurelia beta-like genus of the Tetraviridae. (nih.gov)
  • Replicating rAAV libraries containing 10e6 to 10e7 unique capsid sequences will be used to serially infect a mouse model containing chimeric human-mouse muscle fibers. (cavd.org)
Herpesvirus capsid1
Icosahedral capsids1
Cryo-Electron M2
  • Filling Adeno-Associated Virus Capsids: Estimating Success by Cryo-Electron Microscopy. (harvard.edu)
  • This is a three-dimensional reconstruction of a Herpes Simplex Virus type 1 B-capsid solved by cryo-electron microscopy. (shapeways.com)
Egress1
  • The pUL17 monomer in each CATC bridges over triplexes Ta and Tc on the capsid surface and supports a coiled-coil helix bundle of a pUL25 dimer and a pUL36 dimer, thus positioning their flexible domains for potential involvement in nuclear egress and axonal transport of the capsid. (sciencemag.org)
Gene3
  • The capsid gene of TaV is carried on both the genomic and subgenomic RNA molecules, while the RNA polymerase gene is present only on the genomic RNA. (nih.gov)
  • Cloning and sequencing of the TaV capsid gene identified an open reading frame that could potentially encode a capsid precursor protein of up to 82.5 kDa. (nih.gov)
  • Comprehensive AAV capsid fitness landscape reveals a viral gene and enables machine-guided design. (harvard.edu)
Antiviral activity1
  • Noting that there was a limited increase in antiviral activity at higher doses, Jordan Feld of University Health Network in Toronto, who presented a 'debrief' of viral hepatitis studies at The Liver Meeting, suggested that a higher dose may be needed to disrupt formed capsids and prevent replenishment of cccDNA. (worldhepatitisalliance.org)
Residues5
  • Synthetic peptide corresponding to C terminal residues of Drosophila C virus DCV capsid polyprotein. (abcam.com)
  • Amino acid residues 47-72 in the capsid protein of PCV2a/CL were replaced with the corresponding region of PCV2b/YJ, and the reactivity of mAb 8E4 was lost. (thepigsite.com)
  • Sea bass serum samples reacted strongly with three regions of the capsid protein comprising amino acid residues 1-32, 91-162 and 181-212. (stir.ac.uk)
  • Phosphorylation of serine residues in the unresolved C-terminal domain of the mutant leaves the structure of the ordered capsid largely unchanged. (pdbj.org)
  • These residues pack against the neighboring subunits and increase the inter-dimer contact suggesting that the C-termini play an important role in capsid stabilization and provide a much larger interaction interface than previously observed. (pdbj.org)
Self-assembles1
Nuclear9
  • Previous studies have suggested that nuclear capsid motility is directed and dependent on actin filaments (F-actin), possibly using a myosin-based, ATP-dependent mechanism. (asm.org)
  • They either relied on the effects of F-actin depolymerizing drugs to deduce an F-actin dependency or they visualized nuclear F-actin but failed to show a direct link to capsid motility. (asm.org)
  • Only latrunculin A treatment stalled nuclear capsids but did so by an unexpected effect: the drug induced actin rods in the nucleus. (asm.org)
  • Immobile capsids accumulated around actin rods, and immunoprecipitation experiments suggested that capsid motility stopped because latrunculin-induced actin rods nonspecifically bind nuclear capsids. (asm.org)
  • Based on these data, we conclude that herpesvirus nuclear capsid motility is not dependent on F-actin. (asm.org)
  • To date, the mechanism of the association of human cytomegalovirus (HCMV) capsids with the NEC, which in turn initiates the specific steps of nuclear capsid budding, remains undefined. (mdpi.com)
  • Data strongly suggest that nuclear capsids interact with pUL53 and pUL97. (mdpi.com)
  • Combined, the findings support a refined concept of HCMV nuclear trafficking and NEC-capsid interaction. (mdpi.com)
  • Moreover, none of the capsid cofactors required for nuclear entry or integration are necessary for RT. (elifesciences.org)
Asymmetric unit1
Picornavirus2
Vectors2
  • To overcome these limitations, we chemically modified the surface of the capsid of AAV vectors. (rsc.org)
  • We are currently making vectors from the top 10 selected capsids and planning to test their ability to transduce the human chimeric muscle tissue in vivo . (cavd.org)
MeSH1
  • Capsid" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)
Capsomeres1