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.
↑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
