Virus coat protein

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Virus coat proteins (VCP) or capsid proteins coat the virus[1]. The various VCPs are designated as Vp1, Vp2, etc. The VCP P domain (protruding domain) in noroviruses binds histo blood group antigen receptors. The outer capsid protein VP4 is a virus spike-forming protein which mediates the virial attachment to the host epithelial cell receptors. The distal portion of Vp4 - Vp8* - is implicated in binding the cellular receptor[2]. VP4 is an outer capsid protein of non-enveloped viruses. VP4 attaches to sialic acid or to integrin heterodimers[3]. VP4 domains include: VP5* which forms the foot of the spike and acts in the permeabilization of the cell membrane and VP8* which forms the head of the spike and binds to sialic acid.

The biological assembly of HIV-I coat protein is homohexamer (PDB entry 3gv2).

3D structures of virus coat proteins

Virus coat proteins 3D structures

Structure of HIV-I coat protein hexamer (PDB entry 3gv2)

Drag the structure with the mouse to rotate

References

  1. CASPAR DL, KLUG A. Physical principles in the construction of regular viruses. Cold Spring Harb Symp Quant Biol. 1962;27:1-24. doi:, 10.1101/sqb.1962.027.001.005. PMID:14019094 doi:http://dx.doi.org/10.1101/sqb.1962.027.001.005
  2. Liu Y, Huang P, Tan M, Liu Y, Biesiada J, Meller J, Castello AA, Jiang B, Jiang X. Rotavirus VP8*: phylogeny, host range, and interaction with histo-blood group antigens. J Virol. 2012 Sep;86(18):9899-910. doi: 10.1128/JVI.00979-12. Epub 2012 Jul 3. PMID:22761376 doi:http://dx.doi.org/10.1128/JVI.00979-12
  3. Mackow ER, Barnett JW, Chan H, Greenberg HB. The rhesus rotavirus outer capsid protein VP4 functions as a hemagglutinin and is antigenically conserved when expressed by a baculovirus recombinant. J Virol. 1989 Apr;63(4):1661-8. PMID:2538649

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