Enterovirus capsid proteins VP1–VP4 (VP1–VP4)

Enterovirus capsid proteins VP1, VP2, VP3, and VP4 are the structural components that form the icosahedral shell of viruses within the Enterovirus genus, including poliovirus, coxsackievirus, and rhinovirus. VP1, VP2, and VP3 are located on the external surface of the virion and are responsible for host cell receptor recognition and antigenic properties, while VP4 is situated internally and plays a critical role in genome release. These proteins are essential for the viral life cycle, mediating attachment to host cells and the subsequent uncoating of the viral RNA genome. In clinical medicine, these proteins are the primary targets for 'capsid binders,' small molecules that lodge in a hydrophobic pocket of VP1 to stabilize the capsid and inhibit infection. Despite their potential, the high rate of mutation in enteroviruses often leads to the development of resistance, posing a significant challenge for therapeutic development.

Other names

Enterovirus structural proteinsPicornavirus capsid proteinsVP1VP2VP3VP4Capsid protein VP1Capsid protein VP2Capsid protein VP3Capsid protein VP4

Capsid binders occupy a hydrophobic pocket (the 'canyon' or 'pocket') within the VP1 protein, which increases the rigidity of the viral capsid. This stabilization prevents the conformational changes necessary for the virus to attach to host cell receptors or prevents the uncoating process required to release the viral RNA into the host cytoplasm.