Rhinovirus coat protein (capsid proteins VP1, VP2, VP3, VP4) (VP1, VP2, VP3, VP4)

The Rhinovirus coat protein forms the icosahedral capsid of human rhinoviruses (HRV), composed of 60 copies each of four proteins: VP1, VP2, VP3 (~30 kDa β-barrels on the surface), and VP4 (~7 kDa internal polypeptide interfacing with RNA). VP1 hosts a hydrophobic pocket beneath the canyon receptor-binding site and protrusions with immunogenic epitopes; VP2 and VP3 contribute to surface loops and stability around symmetry axes; VP4 aids RNA packaging and internal dynamics. These proteins enable cell attachment via ICAM-1 (major group) or LDL-receptor family (minor group) at the canyon or star domain, triggering uncoating in endosomes. In disease, HRV causes common colds and exacerbates asthma/COPD through airway infection, with >160 serotypes evading immunity via VP1-3 surface variation. Drugs target the VP1 pocket, displacing natural 'pocket factors' to lock the capsid and block replication, though few reached market due to resistance and specificity issues. Capsid dynamics, including flexible loops and N-termini, influence assembly, disassembly, and antiviral susceptibility.

Other names

HRV capsid proteinRhinovirus capsidViral coat proteinVP1-VP4

Bind hydrophobic pocket in VP1 to inhibit uncoating and replication; Block receptor attachment; Stabilize capsid against disassembly