Enterovirus capsid protein

Enterovirus capsid proteins are the structural proteins that together assemble to form the protective shell (capsid) of enteroviruses, members of the Picornaviridae family[1][2][3]. The capsid consists of 60 copies each of four proteins—VP1, VP2, VP3 (surface-exposed structural proteins), and VP4 (internal)—arranged with icosahedral symmetry[1][2][3][6]. These proteins encapsulate the viral RNA genome, participate in cell attachment by binding to host receptors, mediate genome release during infection, and provide major antigenic determinants for neutralizing antibodies[1][2][3][5][6]. The capsid proteins are key targets for antiviral drug and vaccine development, with small-molecule inhibitors such as pleconaril and WIN51711 shown to bind the hydrophobic pocket in VP1, blocking conformational changes needed for viral uncoating[1][2][5]. Mutation in capsid proteins can lead to antigenic variation and resistance to capsid-binding drugs. Capsid proteins (particularly VP1) are widely used as targets in molecular diagnostics and serologic assays for enteroviral infections[6]. Caveats and limitations: "Enterovirus capsid proteins" refers to a family of homologous proteins across different enteroviruses, not a single, unique human protein or classical receptor/enzyme; specificity for disease or drug interactions may vary by species or strain, and no approved drugs currently target the capsid.

Other names

Enteroviral structural proteinEnterovirus capsid (sometimes used as a shorthand)Enterovirus structural protein

Inhibition of uncoating/release of viral genome by stabilizing the capsid and preventing structural transitions necessary for RNA release[1][2][5]. Prevention of attachment or entry through capsid stabilization (for some inhibitors)