Capsid protein, 5-R(P*UP*UP*AP*AP*UP*AP*UP*UP*UP*UP*UP*AP*UP*UP*UP*UP*U)-3, Capsid protein, Capsid protein, Capsid protein, 5-R(P*UP*UP*AP*AP*UP*AP*UP*UP*UP*UP*UP*AP*UP*UP*UP*UP*U)-3, Capsid protein, Capsid protein, Capsid protein, 5-R(P*UP*UP*AP*AP*UP*AP*UP*UP*UP*UP*UP*AP*UP*UP*UP*UP*U)-3, Capsid protein, Capsid protein, Capsid protein, 5-R(P*UP*UP*AP*AP*UP*AP*UP*UP*UP*UP*UP*AP*UP*UP*UP*UP*U)-3, Capsid protein, Capsid protein, Capsid protein, 5-R(P*UP*UP*AP*AP*UP*AP*UP*UP*UP*UP*UP*AP*UP*UP*UP*UP*U)-3, Capsid protein, Capsid protein, Capsid protein, 5-R(P*UP*UP*AP*AP*UP*AP*UP*UP*UP*UP*UP*AP*UP*UP*UP*UP*U)-3, Capsid protein, Capsid protein, Capsid protein, 5-R(P*UP*UP*AP*AP*UP*AP*UP*UP*UP*UP*UP*AP*UP*UP*UP*UP*U)-3, Capsid protein, Capsid protein, Capsid protein, 5-R(P*UP*UP*AP*AP*UP*AP*UP*UP*UP*UP*UP*AP*UP*UP*UP*UP*U)-3, Capsid protein, Capsid protein, Capsid protein, 5-R(P*UP*UP*AP*AP*UP*AP*UP*UP*UP*UP*UP*AP*UP*UP*UP*UP*U)-3, Capsid protein, Capsid protein, Capsid protein, ...
TY - JOUR. T1 - Derivation of a triple mosaic adenovirus based on modification of the minor capsid protein IX. AU - Tang, Yizhe. AU - Le, Long P.. AU - Matthews, Qiana L.. AU - Han, Tie. AU - Wu, Hongju. AU - Curiel, David T.. N1 - Funding Information: Ad5IXFlag and Ad5IXHis 6 are kind gifts from Dr. Anton Borovjagin, the stable cell line expressing sCAR protein is a kind gift from Dr. Maaike Everts. Discussions with Dr. Hideyo Ugai, Dr. Anton Borovjagin and Dr. Igor Dmitriev were helpful and stimulating throughout this work. The authors also thank Dr. Lacey McNally for technical support of immunogold electron microscopy and Minghui Wang for assistance in quantitative PCR analysis. This work was supported by the following grants: NIH R01CA111569 (Dr. David T. Curiel), NIH 5T32AI07493-11 (Dr. Casey Morrow), Juvenile Diabetes Research Foundation 1-2005-71 (Dr. Hongju Wu) and 5-2007-660 (Dr. Hongju Wu). PY - 2008/8/1. Y1 - 2008/8/1. N2 - Adenoviral capsid protein IX (pIX) has been shown to be a ...
Outer capsid protein VP4: Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. It is subsequently lost, together with VP7, following virus entry into the host cell. Following entry into the host cell, low intracellular or intravesicular Ca(2+) concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7.
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
Viral particles derived from mouse polyomavirus can be potentially used as a delivery system for therapeutic genes and drugs into target cells. This thesis focuses on preparation and characterization of polyomaviral particles that are modified with cell-penetrating peptides in order to increase efficiency of transduction of reporter genes into human cells. Viral particles that are composed of major capsid protein VP1 in combination with minor capsid protein VP2 and minor capsid protein VP3 that is modified with octaarginine, LAH4 peptide or with transduction domain of adenoviral protein VI are analysed in transduction assays. The thesis also provides information about the effect of the modification on encapsidation of heterologous DNA. The results of transduction assays performed with modified particles containing encapsidated luciferase gene revealed that efficiency of transduction did not increase but decreased in comparison with unmodified particles. These findings help to elucidate the role ...
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
The high prevalence of pre-existing anti-Ad5 immunity in human populations may substantially limit the immunogenicity and clinical utility of rAd5 vector-based vaccines for HIV-1 and other pathogens. Our studies demonstrate ,90% Ad5 seroprevalence in sub-Saharan Africa with median NAb titers ,10-fold higher than those found in the United States. These data suggest that rAd5 vectors should be engineered to evade dominant Ad5-specific NAbs before their use as vaccine vectors in the developing world. To determine the principal targets of Ad5-specific NAbs, we exploited the lack of detectable serologic cross-reactivity between Ad5 and Ad35 (8). Virus neutralization studies using capsid chimeric rAd5/rAd35 vectors and serum samples from both humans and mice demonstrated that Ad5-specific NAbs were directed primarily against the Ad5 hexon protein. Fiber-specific NAbs were detected at low frequencies in vitro but were substantially less efficient than hexon-specific NAbs at blunting rAd5 vaccine ...
The L1 major capsid proteins of human papillomavirus (HPV) types 11 and 16 were purified and analyzed for structural integrity and in vitro self-assembly. Proteins were expressed in Escherichia coli as glutathione-S-transferase-L1 (GST-L1) fusions and purified to near homogeneity as pentamers (equiv …
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 ...
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 ...
The utility of recombinant adenovirus serotype 5 (rAd5) vector-based vaccines for HIV-1 and other pathogens will likely be limited by the high prevalence of pre-existing Ad5-specific neutralizing Abs (NAbs) in human populations. However, the immunodominant targets of Ad5-specific NAbs in humans remain poorly characterized. In this study, we assess the titers and primary determinants of Ad5-specific NAbs in individuals from both the United States and the developing world. Importantly, median Ad5-specific NAb titers were ,10-fold higher in sub-Saharan Africa compared with the United States. Moreover, hexon-specific NAb titers were 4- to 10-fold higher than fiber-specific NAb titers in these cohorts by virus neutralization assays using capsid chimeric viruses. We next performed adoptive transfer studies in mice to evaluate the functional capacity of hexon- and fiber-specific NAbs to suppress the immunogenicity of a prototype rAd5-Env vaccine. Hexon-specific NAbs were remarkably efficient at ...
The mature HIV-1 conical core formation proceeds through highly regulated protease cleavage of the Gag precursor, which ultimately leads to substantial rearrangements of the capsid (CAp24) molecule involving both inter- and intra-molecular contacts of the CAp24 molecules. In this aspect, Asp51 which is located in the N-terminal domain of HIV-1 CAp24 plays an important role by forming a salt-bridge with the free imino terminus Pro1 following proteolytic cleavage and liberation of the CAp24 protein from the Pr55Gag precursor. Thus, previous substitution mutation of Asp51 to alanine (D51A) has shown to be lethal and that this invariable residue was found essential for tube formation in vitro, virus replication and virus capsid formation. We extended the above investigation by introducing three different D51 substitution mutations (D51N, D51E, and D51Q) into both prokaryotic and eukaryotic expression systems and studied their effects on in vitro capsid assembly and virus infectivity. Two substitution
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 ...
Background: Human papillomavirus (HPV)-45 genotype circulates in high percentage in Bandung area - Indonesia, after HPV-16 and HPV-18. The aim of this study was to analyse variations of major capsid (L1) HPV-45 and its phylogeny. Furthermore in silico protein structure and epitope prediction was explored. Methods: L1 gene of HPV-45 was amplified, sequenced and aligned. Phylogenetic tree had been built and compared with a complete L1 HPV-45 sequence. Structure and epitope prediction of L1 protein were then developed in silico. Results: Of 5 L1 HPV-45 sequences collected, we have detected one variant of sub lineage A2 which was considered as a new variant, and two variants of B2. Superimposition of structure of these two variants with reference showed very similar structure. Furthermore, seven amino acid substitutions were found within these L1 variants of which two substitutions might change the polarity of corresponding amino acid I329T and S383G. The S383G occurred in surface loop (HI-Loop) of new L1
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
We have presented several lines of evidence that the papillomavirus minor capsid protein mediates the endosomal escape of the viral genome. A C-terminal 23-amino-acid peptide from the L2 protein was identified that is essential for transit of the viral DNA across the endosomal membrane during papillomavirus infection. This peptide is also highly cytotoxic to bacteria, fungi, and mammalian cells after exogenous application due to membrane depolarization and permeabilization and induces the integration of GFP fusion proteins and full-length L2 protein into cellular membranes when expressed in mammalian cells, eventually resulting in cell death. Since the full-length L2 protein but not C-terminally mutated L2 nor L1 protein integrated into cellular membranes, an artificial effect of the observations with peptides and fusion proteins can be excluded. These critical functions render this peptide sequence indispensable for PV infection. The activity of this peptide is highest at modestly acidic pH, ...
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.
Shop Subgenomic capsid protein ELISA Kit, Recombinant Protein and Subgenomic capsid protein Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
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. ...
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 ...
Fingerprint Dive into the research topics of Recognition of the HIV capsid by the TRIM5α restriction factor is mediated by a subset of pre-existing conformations of the TRIM5α SPRY domain. Together they form a unique fingerprint. ...
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 ...
Beginning in 2012, our understanding of human papillomavirus (HPV) subcellular trafficking has undergone a drastic paradigm shift. Work from multiple laboratories has revealed that HPV has evolved a unique means to deliver its viral genome (vDNA) to the cell nucleus, relying on a myriad of host cell proteins and processes. The major breakthrough finding from these recent endeavors was the realization of L2-dependent utilization of cellular sorting factors for the retrograde transport of vDNA away from degradative endo/lysosomal compartments to the Golgi, prior to mitosis-dependent nuclear accumulation of L2/vDNA. An overview of current models of HPV entry, subcellular trafficking, and the role of L2 during initial infection is provided below, highlighting unresolved questions and gaps in knowledge.
We have professional and advanced research and production capacity for WNV Capsid protein reagents production, including cDNA Clones,etc. All WNV-C products are produced in house and quality controlled.
The official website for HHMI and the University of Pittsburghs Science Education Alliance program: Phage Hunters Advancing Genomics and Evolutionary Science.
1E6O: Mutual Conformational Adaptations in Antigen and Antibody Upon Complex Formation between an Fab and HIV-1 Capsid Protein P24
1E6J: Mutual Conformational Adaptations in Antigen and Antibody Upon Complex Formation between an Fab and HIV-1 Capsid Protein P24
TY - JOUR. T1 - A model of protein association based on their hydrophobic and electric interactions. AU - Mozo-Villarías, Angel. AU - Cedano, Juan. AU - Querol, Enrique. PY - 2014/10/17. Y1 - 2014/10/17. N2 - © 2014 Mozo-Villarías et al. The propensity of many proteins to oligomerize and associate to form complex structures from their constituent monomers, is analyzed in terms of their hydrophobic (H), and electric pseudo-dipole (D) moment vectors. In both cases these vectors are defined as the product of the distance between their positive and negative centroids, times the total hydrophobicity or total positive charge of the protein. Changes in the magnitudes and directions of H and D are studied as monomers associate to form larger complexes. We use these descriptors to study similarities and differences in two groups of associations: a) open associations such as polymers with an undefined number of monomers (i.e. actin polymerization, amyloid and HIV capsid assemblies); b) closed ...
Side-chain details from regions in subunit B shown with map and model.Comparable regions from the other two capsid subunits are shown in Supplementary Fig. 5.
The Effect of Limited Proteolysis on the Amino Acid Composition of Five Potyviruses and on the Serological Reaction and Peptide Map of the Tobacco Etch Virus Capsid Protein. Ernest Hiebert, J. H. Tremaine, and W. P. Ronald. Pages 411-416. VIEW ABSTRACT , VIEW ARTICLE. ...
applicable for standard unlabeled Pentamers and ProVE® Pentamers). Biotin-labeled Pentamer staining protocol. Pentamer staining for whole blood. Staining a single cell sample with multiple labeled Pentamers. Staining a single cell sample with multiple unlabeled Pentamers. Pentamer immunohistochemistry protocol. ...
The presence of HPV capsid protein 14 positive cases was associated with local recurrence in nine cases The genital transmission of HPV[5,7,11] Virusul HPV, de obicei, intr n corpul uman happens during sexual intercourse vaginal, anal prin soluii de continuitate la nivelul epidermului and oral.
Summary Direct evidence linking the capsid protein to specific dsRNA segments from the three killer strains of Ustilago maydis virus (P1, P4, P6) is presented. The capsid proteins of the three strains cross-react immunologically, have similar mol. wt. and similar peptide maps after limited proteolysis. The capsid proteins from P1 and P4 were translated from their respective H2 dsRNA segments, whereas the capsid protein for P6 was translated from H1 dsRNA. These in vitro translation products were each precipitated by the antiserum to capsid proteins of all three strains, had similar mol. wt. and similar peptide maps. All in vitro translation products competed effectively with native capsid proteins of all of the three strains in immunocompetition assays. These results suggest that the three strains code for a similar capsid protein, and that the information for capsid protein resides in the H2 segment of strain P1 and P4, and in the H1 segment of strain P6.
Control 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) ...
Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. According to the considered strain, VP4 seems to essentially target sialic acid and/or the integrin heterodimer ITGA2/ITGB1 (By similarity).
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. ...
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 ...
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
TKH HIV caSVLd, a SURWHLQ VKHOO cRPSRVHd RI PRQRPHULc XQLWV RI CA, IRUPV a IXOOHUHQH cRQH WKaW SURWHcWV HIV¶V YLUaO JHQRPH aQd enzymes during infection. I am interested in elucidating the factors that influence stability of the capsid shell and capturing the structural interactions between HIV capsid, host restriction factors, and small molecules using biochemical and structural biology techniques. HIV capsid shell was broken down and purified into hexamer and pentamer units for in vitro study. Structural assays were performed using X-ray crystallography and biochemical analysis was performed using pelleting assays. By understanding capsid structure with factors that confer stability, treatments can be designed to target the protective HIV capsid before the critical step of viral genome integration with host DNA.
We modified the capsid protein of a human enterovirus 71 (HEV71) belonging to subgenogroup C4 (HEV71-C4) to generate a mouse virulent strain, based on the genetic information derived from our previous subgenogroup B3 mouse-adapted virus. Infectious clone-derived mutant virus populations containing the capsid protein mutations VP1-Q145E and VP1-Q145G were generated by site-directed mutagenesis of an infectious clone of a subgenogroup C4 strain. Viruses expressing the VP1-Q145E were virulent in 5-day-old BALB/c mice with 100 % mortality rate observed. Skeletal muscle appears to be the primary site of replication of this virus with limb muscle showing severe myositis. Virus was also isolated from spleen, liver, heart and brain of infected mice. This study demonstrates that introducing a key mutation into the HEV71 VP1 capsid protein is able to generate a mouse virulent HEV71 strain from a different genogroup as well as providing an alternative strategy for the generation of mouse virulent HEV71.
Author Summary Viruses are obligate intracellular pathogens, and all of them share one crucial step in their life cycle-the attachment to their host cell via cellular receptors, which are usually proteins or carbohydrates. This step is decisive for the selection of target cells and virus entry. In this study, we investigated murine polyomavirus (MuPyV), which attaches to host gangliosides with its major capsid protein, VP1. We have solved the crystal structures of VP1 in complex with previously known interaction partners as well as with the ganglioside GT1a, which we have identified as a novel functional receptor for MuPyV. Earlier studies have shown that different strains with singular amino acid exchanges in the receptor binding pocket of VP1 display altered pathogenicity and viral spread. Our investigations show that, while these exchanges do not abolish binding or significantly alter interaction modes to our investigated carbohydrates, they have subtle effects on glycan affinity. The combination of
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, ...
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 ...
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 ...
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, ...
TY - JOUR. T1 - NONO Detects the Nuclear HIV Capsid to Promote cGAS-Mediated Innate Immune Activation. AU - Lahaye, Xavier. AU - Gentili, Matteo. AU - Silvin, Aymeric. AU - Conrad, Cécile. AU - Picard, Léa. AU - Jouve, Mabel. AU - Zueva, Elina. AU - Maurin, Mathieu. AU - Nadalin, Francesca. AU - Knott, Gavin J.. AU - Zhao, Baoyu. AU - Du, Fenglei. AU - Rio, Marlène. AU - Amiel, Jeanne. AU - Fox, Archa H.. AU - Li, Pingwei. AU - Etienne, Lucie. AU - Bond, Charles S.. AU - Colleaux, Laurence. AU - Manel, Nicolas. PY - 2018/10/4. Y1 - 2018/10/4. N2 - Detection of viruses by innate immune sensors induces protective antiviral immunity. The viral DNA sensor cyclic GMP-AMP synthase (cGAS) is necessary for detection of HIV by human dendritic cells and macrophages. However, synthesis of HIV DNA during infection is not sufficient for immune activation. The capsid protein, which associates with viral DNA, has a pivotal role in enabling cGAS-mediated immune activation. We now find that NONO is an ...
Peptides from different regions of the poliovirus type 1 capsid protein VP1 were synthesized. Antibodies raised against these peptides in rabbits and rats recognized the cognate peptides and denatured VP1. Peptides from four regions of VP1 generated antisera with neutralizing titers specifically against poliovirus type 1. Antisera against all other regions of VP1 failed to neutralize virus infectivity, although some of the antisera clearly bound to native virions. Thus, the neutralizing determinants on VP1 reside in specific noncontiguous regions of the protein and can be defined by specific peptides from these regions. ...
Cloning and expression of the gene encoding for the major capsid protein, VP-1, of the D-variant of encephalomyocarditis virus in Escherichia ...
PepTivator® Zika Capsid Protein C is a pool of lyophilized peptides, consisting mainly of 15-mer sequences with 11 amino acids overlap, covering the sequence of the Zika capsid protein C domain from virus isolate Z1106033 polyprotein gene (GenBank Acc. no. KU312312.1).In vitro stimulation of antigen-specific T cells with PepTivator Peptide Pools causes the secretion of effector cytokines and the up-regulation of activation markers, which then allow the detection and isolation of antigen-specific T cells. | Singapore
The HIV-1 capsid protein performs multiple roles in virus replication both during assembly and particle release and during virus trafficking into the nucleus. In order to decipher the roles of capsid protein during early replication, a reliable method to follow its intracellular distribution is required. To complement existing approaches to track HIV-1 capsid during early infection, we developed an HIV-1 imaging strategy, relying on viruses incorporating eGFP-tagged capsid (CA-eGFP) protein and mCherry-tagged integrase (IN-mCherry). Wild type infectivity and sensitivity to inhibition by PF74 point to the functionality of CA-eGFP containing complexes. Low numbers of CA-eGFP molecules are located inside the viral core and imported in the nucleus without significant loss in intensity. Less than 5% of particles carrying both CA-eGFP and IN-mCherry retain both labelled proteins after nuclear entry implying a major uncoating event at the nuclear envelope dissociating IN and CA. Still, 20% of all ...
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 ...
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 ...
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 ...
Vol 10: High yield production of pigeon circovirus capsid protein in the E. coli by evaluating the key parameters needed for protein expression.. . 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.
An interaction between the HSV-1 UL25 capsid protein and cellular microtubule-associated protein was found using a yeast two-hybrid screen and β-D-galactosidase activity assays. Immunofluorescence microscopy of the UL25 protein demonstrated its co-localization with cellular microtubule-associated protein in the plasma membrane. Further investigations with deletion mutants suggest that UL25 is likely to have a function in the nucleus.
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 ...
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 ...
Enlarge Adult common green capsid Enlarge Capsid damage Enlarge Capsid damage to red Charles Ross fruit Common green capsid is a widespread and abundant
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. ...
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.... ...
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 ...
Mouse anti Adenovirus Hexon antibody, clone 7C11 reacts with human, canine, bovine, monkey and rat adenoviruses. It is very likely that it
Bücher, K. S.; Yan, H.; Creutznacher, R.; Ruoff, K.; Mallagaray, A.; Grafmüller, A.; Dirks, J. S.; Kilic, T.; Weickert, S.; Rubailo, A. et al.; Drescher, M.; Schmidt, S.; Hansman, G.; Peters, T.; Uetrecht, C.; Hartmann, L.: Fucose-functionalized precision glycomacromolecules targeting human norovirus capsid protein. Macromolecules 19 (9), S. 3714 - 3724 (2018 ...
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 ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Replication deficient adenoviruses type 5 (Ad5) are widely used vectors for cancer gene therapy. The retargeting of Ad5 is achieved by incorporation of a targeting motifs into the adenovirus capsid proteins, mostly in the HI-loop of fiber or hexon hypervariable region 5 (HVR5). Increased expression of αv integrins has been frequently shown in tumor cells as compared to normal cells. The targeting motif within Ad5 that retargets its transduction to cells expressing αv integrins is RGD. One of the strategies of tumor gene therapy is inhibition of angiogenesis. Endothelial cells in angiogenesis express aminopeptidase N (APN) which binds targeting motifs containing NGR. It is known that different amino acid environment and/or cysteine residues flanking targeting peptides RGD and NGR influence the affinity and specificy of binding to corresponding receptors. The aim of this work was to investigate the existance of disulfide bond/s in two replication deficient Ad5 vectors: (i) Ad5HCRGDC containing ...
AAV capsid titer quantification for full/empty capsid ratio calculations with Gyrolab immunoassay: low sample volume, serotype specific, wide dynamic range
Using GPU-based simulations researchers at the Beckman Institute, University of Illinois have solved the entire molecular structure of the HIV capsid (protein shell). X-ray crystallography is used to probe the structure of the proteins that make up a virus. This is however inadequate when trying to determine how those proteins are assembled to build the virus. The solution: simulate the process with data from both ends of the process using high powered computers. This is exactly what the researchers did using the Blue Waters supercomputer at the University of Illinois. The machine has 237 Cray XE6 cabinets and 32 Cray XK7 cabinets with Nvidia Tesla Kepler GPU cluster. This provided simulations for detailed molecular motion on the 1300 identical proteins contained in the capsid. ...
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。
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:. ...
When it comes to viral vector based gene therapies, it is necessary to evaluate the stability and integrity of viral vector capsids. Having the right analytics for your gene therapy helps you bring a safe and effective drug to market. Time is also critical when getting a drug to market. That is why finding a robust technique that produces fast, reliable results is key.. However, current methods can be very time consuming and may not provide the sensitivity required to efficiently determine the quality of the capsids. There is also a lack of reliable and reproducible methods to cost-effectively manufacture these gene therapies.. This is where SCIEX comes in. SCIEX CE and LC-MS solutions provide you with precision analytics that give you the answers you need the first time around, while using small sample amounts, so you can bring a safe, effective drug to market faster.. ...
ID R4K521_CLOPA Unreviewed; 191 AA. AC R4K521; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 20-DEC-2017, entry version 19. DE SubName: Full=Phage minor structural protein GP20 {ECO:0000313,EMBL:AGK95624.1}; GN ORFNames=Clopa_0576 {ECO:0000313,EMBL:AGK95624.1}; OS Clostridium pasteurianum BC1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=86416 {ECO:0000313,EMBL:AGK95624.1, ECO:0000313,Proteomes:UP000013523}; RN [1] {ECO:0000313,EMBL:AGK95624.1, ECO:0000313,Proteomes:UP000013523} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BC1 {ECO:0000313,EMBL:AGK95624.1, RC ECO:0000313,Proteomes:UP000013523}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Dunn J., RA Taghavi S., Francis A., van der Lelie D., Woyke ...