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 ...
... 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) ...
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
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 ...
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).
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 ...
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.
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 ...
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 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).
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.
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 ...
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, ...
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 ...
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 ...
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
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 ...
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.... ...
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。
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 ...
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. ...
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 ...
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:. ...
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 ...
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 ...
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]. ...
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. . 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.
Rabbit polyclonal DCV capsid polyprotein antibody validated for WB, ELISA, ICC. Referenced in 1 publication and 1 independent review. Immunogen corresponding…
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 ...
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 ...
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 ...
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 ...
Descriptions of various icosahedral virus capsid structures in terms of their complete capsids, along with detailed structural and computational analysis
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 ...
Descriptions of various icosahedral virus capsid structures in terms of their complete capsids, along with detailed structural and computational analysis
The Ty3 retrotransposon assembles into 50-nm virus-like particles that occur in large intracellular clusters in the case of wild-type (wt) Ty3. Within these particles, maturation of the Gag3 and Gag3-Pol3 polyproteins by Ty3 protease produces the structural proteins capsid (CA), spacer, and nucleocapsid. Secondary and tertiary structure predictions showed that, like retroviral CA, Ty3 CA contains a large amount of helical structure arranged in amino-terminal and carboxyl-terminal bundles. Twenty-six mutants in which alanines were substituted for native residues were used to study CA subdomain functions. Transposition was measured, and particle morphogenesis and localization were characterized by analysis of protein processing, cDNA production, genomic RNA protection, and sedimentation and by fluorescence and electron microscopy. These measures defined five groups of mutants. Proteins from each group could be sedimented in a large complex. Mutations in the amino-terminal domain reduced the ...
Viruses have a protein shell called a capsid that protects the genetic material that viruses use to reproduce, and to infect host cells. In some viruses the capsid appears to be completely self-assembled. Some researchers believe that understanding capsid self-assembly could present new ways to fight disease by disrupting virus reproduction.. ...
Bosse JB, Hogue IB, Feric M, Thiberge SY, Sodeik B, Brangwynne CP, et al. Remodeling nuclear architecture allows efficient transport of herpesvirus capsids by diffusion. Proc Natl Acad Sci U S A. 2015 ;112(42):E5725-33. ...
4INB: Monitoring Binding of HIV-1 Capsid Assembly Inhibitors Using (19) F Ligand-and (15) N Protein-Based NMR and X-ray Crystallography: Early Hit Validation of a Benzodiazepine Series.
Kirsi Pakkanen haki väitöstutkimuksessaan monitieteellisen lähestymistavan avulla uusia näkökulmia virustutkimukseen. Tutkimus tuo uutta tietoa lipidikalvojen merkityksestä viruksen ja viruksen isäntäsolun elämässä. Tutkimuksessa selvisi, että koiran parvovirus, jota tutkimuksessa käytettiin mallina parvoviruksille ja yleisemmin vaipattomille viruksille, tarvitsee tietynlaisia isäntäsolun lipidikalvojen ominaisuuksia voidakseen vapautua solunsisäisten endosomirakkuloiden sisältä. Erityisen tärkeää tässä vapautumisessa näytti olevan kalvojen juoksevuus sekä jäykkien alueiden hallittu järjestäytyminen kolesterolin avulla. Hyödyntämällä molekyylejä, lääkeaineita, jotka muuttavat kolesteroliavusteista kalvon järjestäytymistä, voidaan estää virusta infektoimasta solua. Tällöin virus ei pääse vapautumaan solunsisäisistä rakkularakenteista eikä siten pääse solun tumaan, jossa infektio tapahtuisi. Solunsisäisten kalvojen ominaisuuksien muokkaaminen ...
As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
59. Outer covering of virus made up of protein is A. capsid B. coat C. virion D. VirioidWhat do you think? . @sunleaf01 , What do you think it s...
MS2 COAT PROTEIN, MS2 COAT PROTEIN, MS2 COAT PROTEIN, 5-R(*AP*CP*AP*UP*CP*GP*CP*GP*AP*UP *UP*AP*CP*GP*GP*AP*UP*GP*U)-3, 5-R(*AP*CP*AP*UP*CP*GP*CP*GP*AP*UP *UP*AP*CP*GP*GP*AP*UP*GP*U)-3 ...
MS2 COAT PROTEIN, MS2 COAT PROTEIN, MS2 COAT PROTEIN, 5-R(*AP*CP*AP*UP*GP*AP*GP*GP*AP*U ONEP *AP*CP*CP*CP*AP*UP*GP*U)-3, 5-R(*AP*CP*AP*UP*GP*AP*GP*GP*AP*U ONEP *AP*CP*CP*CP*AP*UP*GP*U)-3 ...
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 ...
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. 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