Foot-and-mouth disease virus capsid protein (FMDV capsid protein) (FMDV capsid protein)

The Foot-and-mouth disease virus (FMDV) capsid protein is a complex structural assembly composed of four distinct polypeptides: VP1, VP2, VP3, and VP4, which together form a pseudo-T=3 icosahedral shell (UniProt: P03305). This capsid serves the dual purpose of protecting the viral RNA genome from environmental degradation and facilitating the infection of host cells by recognizing specific cell surface receptors (PMID: 28634238). The primary mechanism of entry involves the binding of a highly conserved Arg-Gly-Asp (RGD) motif, located within the flexible G-H loop of the VP1 protein, to host cell integrins such as αvβ6 (PMID: 15731258). As the most exposed component of the virion, the capsid is the principal target for the host's immune system and the primary focus of vaccine development, including traditional chemically inactivated vaccines and modern virus-like particles (PMID: 31405115). However, the high mutation rate of the FMDV genome leads to significant antigenic variation across seven major serotypes, which complicates the development of universal therapeutics (PMID: 25100862). Current drug discovery efforts target the capsid to develop entry inhibitors or stabilizers that prevent the pH-dependent uncoating of the virus within host endosomes. These structural proteins are also utilized as diagnostic markers to distinguish between infected and vaccinated animals in disease surveillance programs.

Other names

FMDV structural proteinVP1VP2VP3VP4P1 polyproteinFMDV coat protein

Neutralization of viral particles and inhibition of host cell entry by blocking receptor binding sites or inducing protective immune responses.