Structural highlights
Function
CAPSD_ADVG Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 25 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 (10% abundance) and VP2 (90% abundance), which differ by the presence of an N-terminal extension in the minor protein VP1. Capsid proteins are responsible for the attachment to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. VP1 binds DNA and may therefore play a role in viral DNA encapsidation.[1] [2] [3]
References
- ↑ Bloom ME, Best SM, Hayes SF, Wells RD, Wolfinbarger JB, McKenna R, Agbandje-McKenna M. Identification of aleutian mink disease parvovirus capsid sequences mediating antibody-dependent enhancement of infection, virus neutralization, and immune complex formation. J Virol. 2001 Nov;75(22):11116-27. doi: 10.1128/JVI.75.22.11116-11127.2001. PMID:11602751 doi:https://dx.doi.org/10.1128/JVI.75.22.11116-11127.2001
- ↑ Willwand K, Kaaden OR. Capsid protein VP1 (p85) of Aleutian disease virus is a major DNA-binding protein. Virology. 1988 Sep;166(1):52-7. doi: 10.1016/0042-6822(88)90145-6. PMID:2842956 doi:https://dx.doi.org/10.1016/0042-6822(88)90145-6
- ↑ Christensen J, Storgaard T, Bloch B, Alexandersen S, Aasted B. Expression of Aleutian mink disease parvovirus proteins in a baculovirus vector system. J Virol. 1993 Jan;67(1):229-38. doi: 10.1128/JVI.67.1.229-238.1993. PMID:8380073 doi:https://dx.doi.org/10.1128/JVI.67.1.229-238.1993
