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| | <StructureSection load='1s58' size='340' side='right'caption='[[1s58]], [[Resolution|resolution]] 3.50Å' scene=''> | | <StructureSection load='1s58' size='340' side='right'caption='[[1s58]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1s58]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/B19_virus B19 virus]. The May 2010 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Parvoviruses'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2010_5 10.2210/rcsb_pdb/mom_2010_5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S58 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1S58 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1s58]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_parvovirus_B19 Human parvovirus B19]. The May 2010 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Parvoviruses'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2010_5 10.2210/rcsb_pdb/mom_2010_5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S58 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1k3v|1k3v]], [[1lp3|1lp3]], [[1fpv|1fpv]], [[1mvm|1mvm]], [[4dpv|4dpv]], [[1dnv|1dnv]]</div></td></tr> | + | </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=1s58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s58 OCA], [https://pdbe.org/1s58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s58 RCSB], [https://www.ebi.ac.uk/pdbsum/1s58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s58 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">vp2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10798 B19 virus])</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=1s58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s58 OCA], [http://pdbe.org/1s58 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s58 RCSB], [http://www.ebi.ac.uk/pdbsum/1s58 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s58 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CAPSD_PAVHV CAPSD_PAVHV] Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 20 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1 (PubMed:15289612). The capsid encapsulates the genomic ssDNA (Probable). Binds to erythroid progenitor cells expressing high levels of P antigen and uses host ITGA5-ITGB1 and XRCC5/Ku80 autoantigen as coreceptors on the cell surface to provide virion attachment to target cell (PubMed:12907437, PubMed:8211117, PubMed:16076874). This attachment induces virion internalization predominantly through clathrin-dependent endocytosis (PubMed:22718826). Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region (PubMed:17020940). The additional N-terminal region of isoform Minor capsid protein VP1, called VP1u, may serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell and might contribute to virus transport to the nucleus (PubMed:11702787).<ref>PMID:11702787</ref> <ref>PMID:12907437</ref> <ref>PMID:15289612</ref> <ref>PMID:16076874</ref> <ref>PMID:17020940</ref> <ref>PMID:22718826</ref> <ref>PMID:8211117</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Canine parvovirus|Canine parvovirus]] | |
| | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] |
| | == References == | | == References == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: B19 virus]] | + | [[Category: Human parvovirus B19]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Parvoviruses]] | | [[Category: Parvoviruses]] |
| | [[Category: RCSB PDB Molecule of the Month]] | | [[Category: RCSB PDB Molecule of the Month]] |
| - | [[Category: Kaufmann, B]] | + | [[Category: Kaufmann B]] |
| - | [[Category: Rossmann, M G]] | + | [[Category: Rossmann MG]] |
| - | [[Category: Simpson, A A]] | + | [[Category: Simpson AA]] |
| - | [[Category: Beta-barrel]]
| + | |
| - | [[Category: Icosahedral capsid]]
| + | |
| - | [[Category: Icosahedral virus]]
| + | |
| - | [[Category: Virus]]
| + | |
| Structural highlights
Function
CAPSD_PAVHV Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 20 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1 (PubMed:15289612). The capsid encapsulates the genomic ssDNA (Probable). Binds to erythroid progenitor cells expressing high levels of P antigen and uses host ITGA5-ITGB1 and XRCC5/Ku80 autoantigen as coreceptors on the cell surface to provide virion attachment to target cell (PubMed:12907437, PubMed:8211117, PubMed:16076874). This attachment induces virion internalization predominantly through clathrin-dependent endocytosis (PubMed:22718826). Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region (PubMed:17020940). The additional N-terminal region of isoform Minor capsid protein VP1, called VP1u, may serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell and might contribute to virus transport to the nucleus (PubMed:11702787).[1] [2] [3] [4] [5] [6] [7]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Human parvovirus B19 is the only parvovirus known to be a human pathogen. The structure of recombinant B19-like particles has been determined to approximately 3.5-A resolution by x-ray crystallography and, to our knowledge, represents the first near-atomic structure of an Erythrovirus. The polypeptide fold of the major capsid protein VP2 is a "jelly roll" with a beta-barrel motif similar to that found in many icosahedral viruses. The large loops connecting the strands of the beta-barrel form surface features that differentiate B19 from other parvoviruses. Although B19 VP2 has only 26% sequence identity to VP3 of adeno-associated virus, 72% of the C(alpha) atoms can be aligned structurally with a rms deviation of 1.8 A. Both viruses require an integrin as a coreceptor, and conserved surface features suggest a common receptor-binding region.
The structure of human parvovirus B19.,Kaufmann B, Simpson AA, Rossmann MG Proc Natl Acad Sci U S A. 2004 Aug 10;101(32):11628-33. Epub 2004 Aug 2. PMID:15289612[8]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zádori Z, Szelei J, Lacoste MC, Li Y, Gariépy S, Raymond P, Allaire M, Nabi IR, Tijssen P. A viral phospholipase A2 is required for parvovirus infectivity. Dev Cell. 2001 Aug;1(2):291-302. PMID:11702787 doi:10.1016/s1534-5807(01)00031-4
- ↑ Weigel-Kelley KA, Yoder MC, Srivastava A. Alpha5beta1 integrin as a cellular coreceptor for human parvovirus B19: requirement of functional activation of beta1 integrin for viral entry. Blood. 2003 Dec 1;102(12):3927-33. PMID:12907437 doi:10.1182/blood-2003-05-1522
- ↑ Kaufmann B, Simpson AA, Rossmann MG. The structure of human parvovirus B19. Proc Natl Acad Sci U S A. 2004 Aug 10;101(32):11628-33. Epub 2004 Aug 2. PMID:15289612 doi:10.1073/pnas.0402992101
- ↑ Munakata Y, Saito-Ito T, Kumura-Ishii K, Huang J, Kodera T, Ishii T, Hirabayashi Y, Koyanagi Y, Sasaki T. Ku80 autoantigen as a cellular coreceptor for human parvovirus B19 infection. Blood. 2005 Nov 15;106(10):3449-56. PMID:16076874 doi:10.1182/blood-2005-02-0536
- ↑ Ros C, Gerber M, Kempf C. Conformational changes in the VP1-unique region of native human parvovirus B19 lead to exposure of internal sequences that play a role in virus neutralization and infectivity. J Virol. 2006 Dec;80(24):12017-24. PMID:17020940 doi:10.1128/JVI.01435-06
- ↑ Quattrocchi S, Ruprecht N, Bönsch C, Bieli S, Zürcher C, Boller K, Kempf C, Ros C. Characterization of the early steps of human parvovirus B19 infection. J Virol. 2012 Sep;86(17):9274-84. PMID:22718826 doi:10.1128/JVI.01004-12
- ↑ Brown KE, Anderson SM, Young NS. Erythrocyte P antigen: cellular receptor for B19 parvovirus. Science. 1993 Oct 1;262(5130):114-7. PMID:8211117 doi:10.1126/science.8211117
- ↑ Kaufmann B, Simpson AA, Rossmann MG. The structure of human parvovirus B19. Proc Natl Acad Sci U S A. 2004 Aug 10;101(32):11628-33. Epub 2004 Aug 2. PMID:15289612 doi:10.1073/pnas.0402992101
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