Coxsackievirus A6 capsid proteins (CVA6 capsid proteins)

Coxsackievirus A6 (CVA6) capsid proteins, comprising VP1, VP2, VP3, and VP4, constitute the icosahedral shell of the virus and are essential for its structural integrity and infectivity (NIH, 2025). These proteins, particularly the surface-exposed VP1, VP2, and VP3, contain critical epitopes that mediate the virus's interaction with the host cell receptor KREMEN1, facilitating viral attachment and subsequent entry (NIH, 2025; PNAS, 2020). CVA6 has emerged as a leading cause of hand, foot, and mouth disease (HFMD) worldwide, frequently associated with atypical clinical manifestations such as widespread skin lesions and onychomadesis (NIH, 2023; Frontiers in Microbiology, 2021). The surface epitopes on these capsid proteins are the primary targets for the development of preventive vaccines and therapeutic neutralizing antibodies (Frontiers in Microbiology, 2021; Taylor & Francis, 2024). Additionally, the hydrophobic pocket within the VP1 protein serves as a target for small-molecule capsid inhibitors like pleconaril, which aim to stabilize the virion and prevent the release of the viral genome (MDPI, 2024; NIH, 2022). Understanding the structural biology of these epitopes is vital for addressing challenges like antigenic drift and developing effective countermeasures against evolving CVA6 strains (Taylor & Francis, 2024).

Other names

CVA6 VP1CVA6 VP2CVA6 VP3CVA6 VP4Coxsackievirus A6 surface antigensCVA6 structural proteinsCoxsackievirus A6 capsid epitopes

Vaccines and neutralizing antibodies target surface epitopes to block viral attachment to the KREMEN1 receptor and prevent entry. Capsid inhibitors bind to the hydrophobic pocket in the VP1 protein to stabilize the capsid and inhibit viral uncoating.