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==The structure of B19 parvovirus capsid==
==The structure of B19 parvovirus capsid==
<StructureSection load='1s58' size='340' side='right' caption='[[1s58]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
<StructureSection load='1s58' size='340' side='right'caption='[[1s58]], [[Resolution|resolution]] 3.50&Aring;' 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://oca.weizmann.ac.il/oca-docs/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">[[1k3v|1k3v]], [[1lp3|1lp3]], [[1fpv|1fpv]], [[1mvm|1mvm]], [[4dpv|4dpv]], [[1dnv|1dnv]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</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'>[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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/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]</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]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s5/1s58_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s5/1s58_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1s58 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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<ref>PMID:15289612</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1s58" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Canine parvovirus|Canine parvovirus]]
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
*[[Virus coat protein|Virus coat protein]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: B19 virus]]
[[Category: Human parvovirus B19]]
[[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]]

Latest revision as of 09:13, 3 April 2024

The structure of B19 parvovirus capsidThe structure of B19 parvovirus capsid

Structural highlights

1s58 is a 1 chain structure with sequence from Human parvovirus B19. The May 2010 RCSB PDB Molecule of the Month feature on Parvoviruses by David Goodsell is 10.2210/rcsb_pdb/mom_2010_5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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
  6. ↑ 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
  7. ↑ 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

1s58, resolution 3.50Å

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