Picornavirus capsid protein VP1 (VP1) (VP1)

Picornavirus capsid protein VP1 is the primary surface-exposed structural protein of the Picornaviridae family, which includes pathogens such as Rhinovirus, Poliovirus, and Enterovirus 71 (UniProt: P03300). It plays a pivotal role in the viral life cycle by mediating attachment to host cell receptors, such as ICAM-1 or CD155, and facilitating the delivery of the viral RNA genome into the cytoplasm (PubMed: 11907214). A defining feature of VP1 in many picornaviruses is a hydrophobic "canyon" or pocket that is essential for receptor binding and serves as a major target for antiviral drug development (PubMed: 10482571). Small-molecule inhibitors, known as capsid binders, occupy this pocket to stabilize the virion and prevent the uncoating process necessary for infection (PubChem: CID 104314). These drugs, such as Pleconaril, effectively lock the viral capsid in a rigid state, thereby blocking the release of the viral genome (PubMed: 11907214). Due to its high degree of sequence variability, VP1 is also the standard target for molecular typing and phylogenetic analysis of picornavirus strains (PubMed: 12692194). Furthermore, mutations within the VP1 pocket are the primary mechanism by which viruses develop resistance to these antiviral agents (PubMed: 11907214).

Other names

Viral protein 11D proteinCapsid protein 1DVP1 structural protein

Capsid binders occupy a hydrophobic pocket within the VP1 protein, which stabilizes the viral capsid and prevents the conformational changes required for the release of viral RNA into the host cell (uncoating) (PubMed: 11907214). They may also interfere with viral attachment to host receptors by altering the "canyon" conformation (PubMed: 10482571).