Enterovirus 71 viral capsid proteins (EV71 capsid proteins)

Enterovirus 71 (EV71) is a significant human pathogen within the Picornaviridae family, primarily known as a major causative agent of hand, foot, and mouth disease (HFMD) and severe neurological complications in young children (PubMed: 29434377). The viral capsid is an icosahedral shell composed of 60 protomers, each containing four structural proteins: VP1, VP2, VP3, and VP4, which serve to protect the viral RNA and facilitate host cell entry (UniProt: P03300). VP1 is the most surface-exposed protein and plays a critical role in binding to host receptors such as SCARB2 and PSGL-1 (PubMed: 22437571). Because these capsid proteins are essential for the initial stages of the viral life cycle, they are primary targets for antiviral drug development and vaccine design. Small-molecule inhibitors, known as capsid binders, typically lodge in a hydrophobic pocket in VP1 to prevent viral uncoating, while inactivated and recombinant vaccines utilize these proteins to elicit protective neutralizing antibodies (PubMed: 25108375, PubMed: 24581533).

Other names

EV-A71 capsid proteinsVP1VP2VP3VP4P1 precursor proteinEnterovirus A71 structural proteins

Capsid binders interact with a hydrophobic pocket (often referred to as the canyon) located within the VP1 protein; this interaction stabilizes the viral capsid and prevents the conformational changes required for viral uncoating and the subsequent release of the viral RNA genome into the host cell (PubMed: 25108375, PubMed: 22437571).