Coxsackievirus A16 capsid protein VP1 (VP1)

Coxsackievirus A16 capsid protein VP1 is a major structural component of the icosahedral viral capsid, with 60 copies forming the vertices around the 5-fold symmetry axes. It features a β-barrel core with a hydrophobic pocket at the canyon base that binds pocket factors like sphingosine, stabilizing the capsid; receptor binding expels this factor, initiating uncoating and genome release. VP1 contains surface loops (BC, DE, EF, GH, HI) that form neutralizing epitopes targeted by antibodies and interact with receptors like SCARB2. It is critical for host cell attachment and is a key antiviral target due to its role in early infection steps.

Stabilization of VP1 hydrophobic pocket to prevent pocket factor expulsion and uncoating; Blocking receptor binding site in canyon region