Coxsackievirus A16 viral proteins (CVA16 proteins)

Coxsackievirus A16 (CVA16) viral proteins are the functional components of the CVA16 proteome, synthesized as a single large polyprotein that is subsequently cleaved into structural (VP1-VP4) and non-structural (2A-3D) proteins. The structural proteins assemble to form the icosahedral capsid, with VP1 playing a critical role in host cell receptor attachment, specifically to Scavenger Receptor Class B Member 2 (SCARB2) and heparan sulfate. Non-structural proteins, such as the 3C protease and 3D RNA-dependent RNA polymerase, are essential for processing the viral polyprotein and replicating the RNA genome, respectively. These proteins also facilitate immune evasion by cleaving host factors involved in the innate immune response and cellular translation machinery. CVA16 is a primary etiologic agent of Hand, Foot, and Mouth Disease (HFMD), a contagious illness prevalent among infants and children. While often self-limiting, CVA16 infection can lead to severe complications including aseptic meningitis, myocarditis, and fatal pulmonary edema. Because of the clinical significance of HFMD, CVA16 viral proteins are major targets for therapeutic intervention. Current research focuses on the development of bivalent vaccines targeting the capsid proteins and small-molecule inhibitors of the 3C protease (e.g., Rupintrivir) or 3D polymerase to block viral replication and prevent severe disease progression.

Other names

CVA16 polyproteinCV-A16 proteinsCoxsackievirus A16 structural and non-structural proteinsCVA16 proteome

3C protease inhibition, RNA-dependent RNA polymerase (RdRp) inhibition, Capsid binding and entry inhibition, 2C helicase inhibition