Viral protein 1 of picornavirus capsid (VP1)

Viral protein 1 (VP1) is one of four major structural proteins that compose the capsid shell of picornaviruses, a large family of non-enveloped, positive-sense single-stranded RNA viruses. The mature virion contains 60 copies each of four proteins—VP4, VP2, VP3, and VP1, with VP1 forming prominent features on the external surface at five-fold axes known as "canyons", which often serve as sites for cellular receptor binding. The "jelly-roll" β-barrel fold is characteristic for this class. During infection, conformational changes in the capsid—often involving release or rearrangement around VP4/VP1 regions—enable delivery of viral RNA into host cells through membrane penetration mechanisms. The external loops on VP1 are key antigenic determinants targeted by neutralizing antibodies but also display high sequence variability among strains. Some antivirals act by occupying a hydrophobic cavity within VP1 ("pocket factor"), thereby blocking necessary structural transitions during cell entry. Picornaviruses cause diverse human diseases ranging from mild respiratory illness (rhinoviruses) to severe neurological disease (poliovirus), with their pathogenicity closely linked to efficient assembly/disassembly cycles mediated by their structural proteins including VP1.

Other names

VP1Capsid protein VP1Picornavirus capsid protein 1Viral capsid protein 1

Drugs targeting this molecule typically: - Bind to a hydrophobic pocket within VP1 ("pocket factor"), stabilizing the capsid and preventing conformational changes required for uncoating and genome release into host cells