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 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) ...
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, ...
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. ...
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, ...
Human herpesvirus 6B (HHV-6B) belongs to the β-herpesvirus subfamily of the Herpesviridae. To understand capsid assembly and capsid-tegument interactions, here we report atomic structures of HHV-6B capsid and capsid-associated tegument complex (CATC) obtained by cryoEM and sub-particle reconstruction. Compared to other β-herpesviruses, HHV-6B exhibits high similarity in capsid structure but organizational differences in its CATC (pU11 tetramer). 180
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 ...
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.
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, ...
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 ...
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 ...
Retrovirus capsid dimerization domain-like alignments. Alignments can be refined by adding alignments from other genomes, adding your own sequences and/or aligning to other models from the same superfamily. The display of alignments can also be customised.
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 ...
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 ...
Enlarge Adult common green capsid Enlarge Capsid damage Enlarge Capsid damage to red Charles Ross fruit Common green capsid is a widespread and abundant
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 ...
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.
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,. ...
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 ...
The previously characterized monoclonal antibodies (MAbs) A1, A69, B1, and A20 are directed against assembled or nonassembled adeno-associated virus type 2 (AAV-2) capsid proteins (A. receptor attachment by binding an epitope created during AAV-2 capsid assembly. The newly isolated antibodies C24-B and C37-B inhibit AAV-2 binding to cells, probably by realizing a loop region involved in binding of AAV-2 to the cellular receptor. In contrast, binding of D3 to a loop close to the forecasted threefold spike will not neutralize AAV-2 an infection. The discovered antigenic regions over the AAV-2 capsid surface area are ZD6474 price discussed regarding their possible assignments in different techniques from the viral lifestyle cycle. Adeno-associated infections (AAVs) are little, icosahedral viruses from the grouped family using a capsid of 20 to 25 nm in diameter. The capsid harbors a linear, single-stranded DNA genome of 4.7 kb which contains two open up reading structures flanked by inverted ...
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 ...
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 ...
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.... ...
AAV capsid titer quantification for full/empty capsid ratio calculations with Gyrolab immunoassay: low sample volume, serotype specific, wide dynamic range
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。
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.. ...
Q What do capsid bugs look like? A Capsids look like small beetles with long legs and antennae and are about 6mm long. They move quickly...
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 ...
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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 ...
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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.
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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 ...
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 ...
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 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% ...
Author summary The picornavirus family includes clinically important human and animal pathogens, for example: poliovirus, rhinovirus (causing the common cold) and foot-and-mouth disease virus (FMDV) that infects cloven-hoofed animals. Picornaviruses contain a positive-sense RNA genome surrounded by a protein shell, also called a capsid. The capsid proteins are made from a precursor and correct processing and assembly of these capsid proteins is necessary in the virus life cycle to create new infectious virus particles. In this study, we have identified a short motif (just 5 amino acids long) within the capsid precursor, which is highly conserved among picornaviruses. Deletion of this motif inhibited processing of the junctions between the mature structural proteins within this precursor, with one junction being more than 400 amino acids away from this region. This motif also seems to be required for the optimal accumulation of the capsid precursor in cells. We hypothesize that the motif may be involved
Viral capsids are metastable structures that perform many essential processes; they also act as robust cages during the extracellular phase. Viruses can use multifunctional proteins to optimize resources (e.g., VP3 in avian infectious bursal disease virus, IBDV). The IBDV genome is organized as ribonucleoproteins (RNP) of dsRNA with VP3, which also acts as a scaffold during capsid assembly. We characterized mechanical properties of IBDV populations with different RNP content (ranging from none to four RNP). The IBDV population with the greatest RNP number (and best fitness) showed greatest capsid rigidity. When bound to dsRNA, VP3 reinforces virus stiffness. These contacts involve interactions with capsid structural subunits that differ from the initial interactions during capsid assembly. Our results suggest that RNP dimers are the basic stabilization units of the virion, provide better understanding of multifunctional proteins, and highlight the duality of RNP as capsid-stabilizing and genetic ...
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
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.
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 ...
The crystal structure of the double-stranded DNA bacteriophage HK97 mature empty capsid was determined at 3.6 angstrom resolution. The 660 angstrom diameter icosahedral particle contains 420 subunits with a new fold. The final capsid maturation step is an autocatalytic reaction that creates 420 isopeptide bonds between proteins. Each subunit is joined to two of its neighbors by ligation of the side-chain lysine 169 to asparagine 356. This generates 12 pentameric and 60 hexameric rings of covalently joined subunits that loop through each other, creating protein chainmail: topologically linked protein catenanes arranged with icosahedral symmetry. Catenanes have not been previously observed in proteins and provide a stabilization mechanism for the very thin HK97 capsid. ...
TY - JOUR. T1 - Partial amino-terminal sequences of the polyoma nonhistone proteins VP1, VP2, and VP3 synthesized in vitro. AU - Hewick, R. M.. AU - Mellor, A.. AU - Smith, A. E.. AU - Waterfield, M. D.. N1 - Copyright: Copyright 2020 Elsevier B.V., All rights reserved.. PY - 1980. Y1 - 1980. N2 - The three polyoma virus capsid proteins VP1, VP2, and VP3 were synthesized in vitro in the presence of several radiolabeled amino acids and, after purification on sodium dodecyl sulfate-polyacrylamide gels, were subjected to sequential Edman degradation. The partial amino-terminal amino acid sequences obtained were compared with the sequence of amino acids predicted from the polyoma virus DNA sequencing. Together, these results showed that the 5 ends of the VP1, VP2, and VP3 coding sequences are located 1,217, 289, and 634 nucleotides, respectively, from the junction of HpaII restriction fragments 3 and 5.. AB - The three polyoma virus capsid proteins VP1, VP2, and VP3 were synthesized in vitro in the ...
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. ...
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 ...
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 ...
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
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
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 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 ...
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 ...
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 ...
PubMed journal article: High prevalence of immunoglobulin A antibody against Epstein-Barr virus capsid antigen in adult patients with lupus with disease flare: case control studies. Download Prime PubMed App to iPhone, iPad, or Android
Our main goal was to produce a library of Adeno-associated viruses that infect cells with different specificities and efficiencies, due to differing capsid composition, and select from this library the best AAVs that are highly specific. Since it is not the case that viruses that work well in vitro will work as good in vivo, we had the aim of testing our candidates in mice as well. To achieve this, the capsid genes from AAV serotypes 1,2,5,6,8 and 9 were shuffled between each other in a primerless PCR reaction that relies on the close homology between the different cap genes. Those capsid genes were first digested with DNase I, then pooled together and allowed to anneal to each other. A second PCR was done then to amplify the shuffled cap gene fragments that were generated in the first PCR while introducing AscI and PacI restriction sites, which are used to clone the cap genes into a helper vector. AAVs that were then produced in HEK293 cells, which were transfected with the cap-gene-ITR ...
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 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 ...
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. ...
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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
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 …
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 ...
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Minor protein of the capsid that localizes along the inner surface of the virion, within the central cavities beneath the L1 pentamers. Plays a role in capsid stabilization through interaction with the major capsid protein L1. Once the virion enters the host cell, L2 escorts the genomic DNA into the nucleus by promoting escape from the endosomal compartments and traffic through the host Golgi network. Mechanistically, the C-terminus of L2 possesses a cell-penetrating peptide that protudes from the host endosome, interacts with host cytoplasmic retromer cargo and thereby mediates the capsid delivery to the host trans-Golgi network. Plays a role through its interaction with host dynein in the intracellular microtubule-dependent transport of viral capsid toward the nucleus. Mediates the viral genome import into the nucleus through binding to host importins. Once within the nucleus, L2 localizes viral genomes to host PML bodies in order to activate early gene expression for establishment of ...
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.. ...
ViroBytes is a modified BioBytes procedure for rational shuffling of capsid genes from natural isolates of Adeno-Associated Virus. Main motivation for the new protocol is unsatisfactory incorporation of certain serotypes (and especially certain parts of AAV capsid regions eg. from AAV5) using conventional shuffling strategies (Grimm et al., 2008). Application of magnetic beads for controlled assembly and the principle of BioByte formation and annealing persists. Sticky overhangs are used for selective combination of the bytes but different method is used for the production of individual ViroBytes. AAV serotypes 1,2,5,6,8 and 9 were selected as suitable candidates for fragmentation due to their exceptional individual properties. The analysis of Cap gene sequences revealed multiple homology regions which were then used for rational fragment formation. Total number of fragments per Cap gene is eight in our case and all fragments have similar length around ~250bp to assure similar behaviour in the ...
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. ...
Defensins are effectors of the innate immune response with potent antibacterial activity. Their role in antiviral immunity, particularly for non-enveloped viruses, is poorly understood. We recently found that human alpha-defensins inhibit human adenovirus (HAdV) by preventing virus uncoating and rel …
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. ...
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
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 ...
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.