capsid protein

Isoform VP2 is a structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Participates in host cell receptor binding together with VP1. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or Vp3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus in particular through a DNA-binding domain located in the C-terminal region. A N-terminal myristoylation suggests a scaffold function for virion assembly.; structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or Vp3 nuclear localization signal (shared C-terminus). Isoform VP3 plays a role in virion assembly within the nucleus. May participate in host cell lysis when associated with VP4.; Isoform VP4 is a viroporin inducing perforation of cellular membranes to trigger virus progeny release. Forms pores of 3 nm inner diameter. VP4 is expressed about 24 hours after the late structural proteins and is not incorporated into the mature virion.

Porcine circovirus 2 (PCV2) Capsid Protein (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 23.8 kDa.

Hepatitis B virus (HBV) capsid assembly is a critical step in the propagation of the virus and is mediated by the core protein. The first cytoplasmic step in the formation of an infectious HBV virion is the formation of a capsid containing pregenomic RNA (pgRNA) and the viral polymerase (Pol). HBV capsid assembly is an attractive target for new antiviral therapies.

Human parvovirus B19 (isolate AU) Non-capsid protein NS-1 (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 44.6 kDa and the accession number is P07298.

Stimulates translation by blocking the activation of the dsRNA-dependent protein kinase EIF2AK2 PKR, thereby inhibiting the host interferon response. Sigma3 prevents the activation of EIF2AK2 by competing with the kinase for dsRNA-binding.; The viral outer shell polypeptides, of which sigma-3 is one, impose structural constraints that prevent elongation of nascent transcripts by the RNA-dependent RNA polymerase lambda-3. Reovirus type 3 (strain Dearing) Outer capsid protein sigma-3 (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 45.2 kDa and the accession number is P03527.

Most abundant structural protein of the nucleocapsid produced during the infection cycle. The monomers are arranged in stacked rings around the nucleoprotein core. AcMNPV Major capsid Protein (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 46.4 kDa and the accession number is P17499.

HBV-C subtype ayw (isolate China Tibet127 2002) Capsid protein (Yeast, His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 23.0 kDa and the accession number is P0C6H7.

HBV-A subtype adw2 (isolate Germany 991 1990) Capsid protein (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 28.9 kDa and the accession number is P0C693.

HBV-C subtype ayw (isolate China Tibet127 2002) Capsid protein (E. coli, His) is expressed in E. coli expression system with N-10xHis tag. The predicted molecular weight is 27.1 kDa and the accession number is P0C6H7.

Stabilizes the expansion of the capsid head shell after genome packaging. The packaging of viral genome in the procapsid triggers a dramatic reconfiguration of the capsid shell, expanding from roughly 50nm to 60nm while the capsid thickness decreases. 415 capsid decoration protein molecules cooperatively bind the expanded capsid, thereby stabilizing the mature capsid shell. Capsid decoration Protein, Escherichia phage lambda, Recombinant (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 32.5 kDa and the accession number is P03712.

Human Papilloma Virus type 16 (HPV 16) Minor capsid Protein L2 (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 66.7 kDa and the accession number is P03107.

Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome. The capsid contains also 1 copy of the A2 maturation protein.; Acts as a translational repressor of viral replicase synthesis late in infection. This latter function is the result of capsid protein interaction with an RNA hairpin which contains the replicase ribosome-binding site.

HBV-A subtype adw2 (strain Rutter 1979) Capsid protein (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 25.4 kDa and the accession number is P03148.

Major viral capsid protein that encapsidates the viral genome. Binds to the 5' end of the genomic RNA. Hepatitis E virus genotype 3 (HEV-3) Capsid protein (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 29.3 kDa and the accession number is Q9YLQ9.

Human herpesvirus 6A (HHV-6 variant A) (strain Uganda-1102) Triplex capsid protein 1 (His) is expressed in E. coli.

Human Papilloma Virus type 18 (HPV 18) Minor capsid Protein L2 (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 51.6 kDa and the accession number is P06793.

Porcine circovirus 2 (PCV2) Capsid Protein (E. coli, His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 32.0 kDa and the accession number is O56129.

Dengue virus DENV-2 (Strain New Guinea C) Capsid protein DENV-C Protein (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 14 kDa and the accession number is W0GCK5.

Essential for the correct processing of both structural polyproteins and for the maturation of viral precursor membranes at the viral factories. ASFV (strain Ba71V) p17 Protein (His) is expressed in E. coli expression system with N-10xHis tag. The predicted molecular weight is 19.2 kDa and the accession number is Q89424.

Forms an icosahedral capsid with a T=7 symmetry and a 40 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with VP2 or VP3 proteins. Interacts with sialic acids on the cell surface to provide virion attachment to target cell. Once attached, the virion is internalized by endocytosis and traffics to the endoplasmic reticulum. Inside the endoplasmic reticulum, the protein folding machinery isomerizes VP1 interpentamer disulfide bonds, thereby triggering initial uncoating. Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 Vp3 nuclear localization signal. In late phase of infection, neo-synthesized VP1 encapsulates replicated genomic DNA in the nucleus, and participates in rearranging nucleosomes around the viral DNA.

Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. It is subsequently lost, together with VP7, following virus entry into the host cell. Following entry into the host cell, low intracellular or intravesicular Ca(2+) concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7.; Forms the spike 'foot' and 'body' and acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. During entry, the part of VP5* that protrudes from the virus folds back on itself and reorganizes from a local dimer to a trimer. This reorganization may be linked to membrane penetration.; Forms the head of the spikes and mediates the recognition of specific host cell surface glycans. It is the viral hemagglutinin and an important target of neutralizing antibodies.

Rotavirus A (strain St. Thomas 3) VP6 Protein (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 46.9 kDa and the accession number is B1NKU0.

Isoform VP2 is a structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Participates in host cell receptor binding together with VP1. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or Vp3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus in particular through a DNA-binding domain located in the C-terminal region. A N-terminal myristoylation suggests a scaffold function for virion assembly.; structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or Vp3 nuclear localization signal (shared C-terminus). Isoform VP3 plays a role in virion assembly within the nucleus. May participate in host cell lysis when associated with VP4.; Isoform VP4 is a viroporin inducing perforation of cellular membranes to trigger virus progeny release. Forms pores of 3 nm inner diameter. VP4 is expressed about 24 hours after the late structural proteins and is not incorporated into the mature virion.

Murine polyomavirus (MPyV) (strain Kilham) VP2 Protein (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 41.4 kDa and the accession number is P24596.

BK polyomavirus (BKPyV) VP1 Protein (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 45.1 kDa and the accession number is P03088.

Canine parvovirus type 2 (CPV-2) VP2 Protein (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 65.9 kDa and the accession number is P61826.

Murine polyomavirus (MPyV) (strain Kilham) VP1 Protein (E. coli, His) is expressed in E. coli expression system with C-6xHis tag. The predicted molecular weight is 42.4 kDa and the accession number is P24595.

Rotavirus A (strain Nebraska calf diarrhea virus) VP4 Protein (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 33.2 kDa and the accession number is P17465.

Rotavirus A (strain Nebraska calf diarrhea virus) VP6 Protein (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 50.8 kDa and the accession number is A7J3A1.

Rotavirus A (strain St. Thomas 3) VP4 Protein (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 28.3 kDa and the accession number is P11200.

Murine polyomavirus (MPyV) (strain Kilham) VP1 Protein (His) is expressed in Baculovirus insect cells with C-6xHis tag. The predicted molecular weight is 42.5 kDa and the accession number is P24595.

Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate the genomic RNA and VP2 proteins. Attaches virion to target cells by binding histo-blood group antigens present on gastroduodenal epithelial cells.; Soluble capsid protein may play a role in viral immunoevasion.

Rotavirus A (strain RVA Human United States Wa 1974 G1P1A[8]) VP6 Protein (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 50.9 kDa and the accession number is P03530.

Rotavirus A (strain RVA Cow France RF 1975 G6P6[1]) VP6 Protein (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 48.8 kDa and the accession number is P04509.

Human enterovirus 71 genome polyprotein is a member of the picornaviruses polyprotein family. It contains two peptidase C3 domains, one RdRp catalytic domain, one SF3 helicase domain. Genome polyprotein is cleaved into the following 12 chains: Protein VP (VP4-VP2), Protein VP4 (P1A), Protein VP2 (P1B), Protein VP3 (P1C), Protein VP1 (P1D), Picornain 2A (P2A), Protein 2B (P2B), Protein 2C (P2C), Protein 3A (P3A), Protein 3B (P3B), Picornain 3C (Protease 3C) and RNA-directed RNA polymerase 3D-POL (P3D-POL). VP precursor is a component of immature procapsids. Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid composed of 6 copies of each VP1, VP2, and VP3, with a diameter of approximately 3 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes.

Plays a role in the inhibition of host antibody-mediated neutralization without blocking viral cell entry.; Forms an icosahedral capsid with a T=1 symmetry and a 34 nm diameter. The capsid is composed of 60 copies linked to each other. Binds to the 5' end of the genomic RNA to mediate genome encapsidation. Binds to heparin surface proteoglycans (HSPGs) to mediate viral entry. Additionally, the interactions with host ASGR1 and ASGR2 facilitate viral infection of hepatocytes. Hepatitis E virus genotype 1 (HEV-1) Secreted protein ORF2 (His) is expressed in Baculovirus insect cells with N-10xHis tag. The predicted molecular weight is 71.3 kDa and the accession number is Q68985.

Major capsid protein that self-associates to form 240 hexon trimers, each in the shape of a hexagon, building most of the pseudo T=25 capsid. Assembled into trimeric units with the help of the chaperone shutoff protein. Transported by pre-protein VI to the nucleus where it associates with other structural proteins to form an empty capsid. Might be involved, through its interaction with host dyneins, in the intracellular microtubule-dependent transport of incoming viral capsid to the nucleus. Human adenovirus B serotype 3 Hexon protein (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 33.7 kDa and the accession number is P36849.

Peptidyl-prolyl cis-trans isomerase A is a cytoplasm protein which belongs to the cyclophilin-type PPIase family and PPIase A subfamily. Cyclophilins(CyPs) are a family of proteins found in organisms ranging from prokaryotes to humans. These molecules exhibit peptidyl-prolyl isomerase activity, suggesting that they influence the conformation of proteins in cells. Cyclophilin A accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Cyclophilin A can interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions.

Tripartite motif-containing Motif 5 is a protein that in humans is encoded by the TRIM5 gene.It is a 493 amino acids protein that belongs to the TRIM RBCC family.It contains 1 B box-type zinc finger, 1 B30.2 SPRY domain and 1 RING-type zinc finger. TRIM5 present in the cytoplasm recognizes motifs within the capsid proteins and interferes with the uncoating process, therefore preventing successful reverse transcription and transport to the nucleus of the viral genome. The exact mechanism of action has not been shown conclusively, but capsid protein from restricted viruses is removed by proteasome-dependent degradation

Matrix protein p15 forms the outer shell of the core of the virus, lining the inner surface of the viral membrane.; Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex.; Nucleocapsid protein p13 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. FIV (isolate Petaluma) Gag polyprotein (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 22.1 kDa and the accession number is P16087.

Forms spikes that protrude from each vertex of the icosahedral capsid. Interacts with host receptor CD46 to provide virion initial attachment to target cell. Fiber proteins are shed during virus entry, when virus is still at the cell surface. Human adenovirus B serotype 11 (strain BC34) Fiber protein (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 40.6 kDa and the accession number is P35773.