5us9

Structural highlights

Function

CAPSD_HBOC4 Capsid proteins self-assembles to form an icosahedral capsid with a T=1 symmetry, about 26 nm in diameter, and consisting of 60 copies of three size variants of the capsid proteins, VP1, and VP3, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid has a channel at the 5-fold axis and there are densities extending the 5-fold axis into the interior of the capsid (PubMed:28331084). The capsid encapsulates the genomic ssDNA (Probable). Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region. 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 (By similarity).[UniProtKB:Q9PZT0]^{[1] [2]}

References

1. ↑ Mietzsch M, Kailasan S, Garrison J, Ilyas M, Chipman P, Kantola K, Janssen ME, Spear J, Sousa D, McKenna R, Brown K, Soderlund-Venermo M, Baker T, Agbandje-McKenna M. Structural insights into emerging pediatric pathogens human bocaparvoviruses. J Virol. 2017 Mar 22. pii: JVI.00261-17. doi: 10.1128/JVI.00261-17. PMID:28331084 doi:http://dx.doi.org/10.1128/JVI.00261-17
2. ↑ Mietzsch M, Kailasan S, Garrison J, Ilyas M, Chipman P, Kantola K, Janssen ME, Spear J, Sousa D, McKenna R, Brown K, Soderlund-Venermo M, Baker T, Agbandje-McKenna M. Structural insights into emerging pediatric pathogens human bocaparvoviruses. J Virol. 2017 Mar 22. pii: JVI.00261-17. doi: 10.1128/JVI.00261-17. PMID:28331084 doi:http://dx.doi.org/10.1128/JVI.00261-17