Enterovirus C viral capsid

The **Enterovirus C viral capsid** is a protein shell enclosing the single-stranded positive-sense RNA genome of Enterovirus C species, which encompasses polioviruses and several coxsackieviruses. The capsid adopts an icosahedral symmetry, composed of 60 protomers; each protomer is made up of four structural proteins: VP1, VP2, VP3 (all surface-exposed), and VP4 (internal). The major surface-exposed VP1 forms the 'canyon' and contains a hydrophobic 'pocket factor' site that is critical for capsid stability and the process of viral uncoating during infection[1][3]. Key features of the capsid, such as the antigenic loops of VP1, are targets for neutralizing antibodies and small-molecule inhibitors. The capsid is central to disease progression as it enables both persistence in harsh extracellular environments and the recognition and entry into susceptible host cells by interacting with specific cellular receptors. Variability in capsid proteins underlies serotype diversity, immune escape, and impacts the effectiveness of potential capsid-targeting antivirals or vaccines[1][3][9].

Other names

Enterovirus C capsidPoliovirus capsid (for poliovirus strains in Enterovirus C)Coxsackievirus A capsid (for Coxsackie A viral strains in Enterovirus C)EV-C capsid

Inhibitor binds to the hydrophobic “pocket factor” site in capsid (notably in the VP1 subunit), stabilizing the capsid, thus preventing “pocket factor” expulsion and subsequent uncoating/genome release necessary for infection[1][9]. Antibody-mediated neutralization, especially against external capsid loops and N-terminal region of VP1, blocking receptor binding or triggering uncoating[3].