Virus coat protein
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. VP4 is an outer capsid protein of non-enveloped viruses. VP4 attaches to sialic acid or to integrin heterodimers[2]. 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 (PDB entry 3gv2). For details on Zika virus capsid protein see Hugo Heringer de Almeida/5YGH. For adeno-associated virus 9 Vp1 see Adeno-Associated Virus. See also Viral capsids 3D structures of virus coat proteins |
|
ReferencesReferences
- ↑ Djabatey EA, Barclay PM. Difficult and failed intubation in 3430 obstetric general anaesthetics. Anaesthesia. 2009 Nov;64(11):1168-71. doi: 10.1111/j.1365-2044.2009.06060.x. PMID:19825049 doi:http://dx.doi.org/10.1111/j.1365-2044.2009.06060.x
- ↑ 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