Foot-and-mouth disease virus capsid protein VP1 (VP1)

The Foot-and-mouth disease virus capsid protein VP1 is a key structural component of the viral capsid in Foot-and-mouth disease virus (FMDV), an Aphthovirus in the Picornaviridae family, forming the outer shell alongside VP2, VP3, and VP4 from a single-stranded positive-sense RNA genome. VP1 contributes to virion stability and cell entry, featuring a binding site at the junction of VP1, VP2, and VP3 that interacts with host receptors like heparan sulfate, triggering conformational changes and VP4 release. Beyond structure, VP1 interacts with host proteins such as ribosomal protein SA (RPSA) to repress its inhibition of the MAPK pathway, promoting FMDV replication, and antagonizes TPL2 to block IRF3/IFN-β signaling, enabling immune escape. These interactions highlight VP1's role in reprogramming host signaling for viral benefit during infection in susceptible cells like PK-15 and BHK-21. As the main immunogenic component, VP1 drives serotype-specific antibody responses due to sequence variation, complicating cross-protection. Targeting VP1 is relevant for antiviral strategies against FMD, a highly contagious livestock disease, though no approved small-molecule drugs are noted.

Other names

FMDV VP1structural protein VP1