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| | <SX load='6gg0' size='340' side='right' viewer='molstar' caption='[[6gg0]], [[Resolution|resolution]] 4.24Å' scene=''> | | <SX load='6gg0' size='340' side='right' viewer='molstar' caption='[[6gg0]], [[Resolution|resolution]] 4.24Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6gg0]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Bk_polyomavirus Bk polyomavirus] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GG0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6GG0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6gg0]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_polyomavirus_1 Human polyomavirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GG0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GG0 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VP1, vp1, BK1035_00004, BK1055_00004 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1891762 BK polyomavirus])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.24Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6gg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gg0 OCA], [http://pdbe.org/6gg0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gg0 RCSB], [http://www.ebi.ac.uk/pdbsum/6gg0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gg0 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6gg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gg0 OCA], [https://pdbe.org/6gg0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gg0 RCSB], [https://www.ebi.ac.uk/pdbsum/6gg0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gg0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q65613_POVBK Q65613_POVBK]] Forms an icosahedral capsid with a T=7 symmetry.[PIRNR:PIRNR003376] | + | [https://www.uniprot.org/uniprot/VP1_POVBK VP1_POVBK] Forms an icosahedral capsid with a T=7 symmetry and a 50 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 gangliosides GT1b and GD1b containing terminal alpha(2-8)-linked sialic acids on the cell surface to provide virion attachment to target cell. This attachment induces virion internalization predominantly through caveolin-mediated 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 (By similarity).<ref>PMID:15479799</ref> <ref>PMID:16415013</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6gg0" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6gg0" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Bk polyomavirus]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]] | + | [[Category: Human polyomavirus 1]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Srinivas, H]] | + | [[Category: Srinivas H]] |
| - | [[Category: Bk polyoma virus]]
| + | |
| - | [[Category: Cross neutralizing antibody]]
| + | |
| - | [[Category: Single chain antibody]]
| + | |
| - | [[Category: Virus like particle]]
| + | |
| Structural highlights
Function
VP1_POVBK Forms an icosahedral capsid with a T=7 symmetry and a 50 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 gangliosides GT1b and GD1b containing terminal alpha(2-8)-linked sialic acids on the cell surface to provide virion attachment to target cell. This attachment induces virion internalization predominantly through caveolin-mediated 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 (By similarity).[1] [2]
Publication Abstract from PubMed
Human polyomaviruses cause a common childhood infection worldwide and typically elicit a neutralizing antibody and cellular immune response, while establishing a dormant infection in the kidney with minimal clinical manifestations. However, viral reactivation can cause severe pathology in immunocompromised individuals. We developed a high-throughput, functional antibody screen to examine the humoral response to BK polyomavirus. This approach enabled the isolation of antibodies from all peripheral B cell subsets and revealed the anti-BK virus antibody repertoire as clonally complex with respect to immunoglobulin sequences and isotypes (both IgM and IgG), including a high frequency of monoclonal antibodies that broadly neutralize BK virus subtypes and the related JC polyomavirus. Cryo-electron microscopy of a broadly neutralizing IgG single-chain variable fragment complexed with BK virus-like particles revealed the quaternary nature of a conserved viral epitope at the junction between capsid pentamers. These features unravel a potent modality for inhibiting polyomavirus infection in kidney transplant recipients and other immunocompromised patients.
Human Memory B Cells Harbor Diverse Cross-Neutralizing Antibodies against BK and JC Polyomaviruses.,Lindner JM, Cornacchione V, Sathe A, Be C, Srinivas H, Riquet E, Leber XC, Hein A, Wrobel MB, Scharenberg M, Pietzonka T, Wiesmann C, Abend J, Traggiai E Immunity. 2019 Feb 16. pii: S1074-7613(19)30048-2. doi:, 10.1016/j.immuni.2019.02.003. PMID:30824324[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Eash S, Querbes W, Atwood WJ. Infection of vero cells by BK virus is dependent on caveolae. J Virol. 2004 Nov;78(21):11583-90. PMID:15479799 doi:http://dx.doi.org/10.1128/JVI.78.21.11583-11590.2004
- ↑ Low JA, Magnuson B, Tsai B, Imperiale MJ. Identification of gangliosides GD1b and GT1b as receptors for BK virus. J Virol. 2006 Feb;80(3):1361-6. PMID:16415013 doi:http://dx.doi.org/80/3/1361
- ↑ Lindner JM, Cornacchione V, Sathe A, Be C, Srinivas H, Riquet E, Leber XC, Hein A, Wrobel MB, Scharenberg M, Pietzonka T, Wiesmann C, Abend J, Traggiai E. Human Memory B Cells Harbor Diverse Cross-Neutralizing Antibodies against BK and JC Polyomaviruses. Immunity. 2019 Feb 16. pii: S1074-7613(19)30048-2. doi:, 10.1016/j.immuni.2019.02.003. PMID:30824324 doi:http://dx.doi.org/10.1016/j.immuni.2019.02.003
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