Coxsackievirus A16 viral capsid proteins (CVA16 capsid proteins)

Coxsackievirus A16 (CVA16) is a major pathogen responsible for hand, foot, and mouth disease (HFMD), particularly in children, and belongs to the Enterovirus A species (PMID: 25122778). The viral capsid is an icosahedral structure composed of 60 protomers, each containing four structural proteins: VP1, VP2, VP3, and VP4 (UniProt: P04544). These proteins play a vital role in the viral life cycle by recognizing and binding to host cell receptors, such as scavenger receptor class B member 2 (SCARB2) and P-selectin glycoprotein ligand-1 (PSGL-1), and facilitating the delivery of the viral RNA into the host cell (PMID: 26158719). Because they are the most exposed parts of the virion, these proteins are the primary targets for neutralizing antibodies and are central to the development of vaccines and antiviral therapies. Therapeutic strategies include the use of inactivated virus vaccines and small-molecule capsid binders that occupy the hydrophobic pocket of the VP1 protein, thereby stabilizing the capsid and preventing the uncoating process required for infection (PMID: 11850502, PMID: 30253155).

Other names

CVA16 structural proteinsVP1-VP4 proteinsCoxsackievirus A16 capsidCVA16 VP1CVA16 VP2CVA16 VP3CVA16 VP4

Capsid binders (e.g., Pleconaril) occupy a hydrophobic pocket in the VP1 protein, stabilizing the capsid and preventing the uncoating and release of viral RNA into the host cell (PMID: 11850502). Vaccines induce the production of neutralizing antibodies that bind to the capsid surface, blocking viral attachment to host receptors (PMID: 30253155).