Rhinovirus capsid protein VP3 (VP3)

Rhinovirus capsid protein VP3 is a key structural component of the Human Rhinovirus (HRV) icosahedral shell, which is responsible for the majority of common cold cases (UniProt: P03303). The capsid is composed of 60 copies each of four proteins (VP1-VP4), with VP3 being one of the three surface-exposed proteins that facilitate host cell recognition and entry. VP3 contributes to the formation of the "canyon," a surface depression that acts as the binding site for cellular receptors such as Intercellular Adhesion Molecule 1 (ICAM-1) (Rossmann et al., Nature 1985). In addition to its role in receptor binding, VP3 is essential for the assembly and stability of the viral particle. Therapeutic strategies targeting the capsid, such as the use of "WIN compounds" like Pleconaril, involve binding to a hydrophobic pocket that spans the capsid proteins, effectively locking the virus in a stable state to prevent the uncoating process (Pevear et al., Antimicrob Agents Chemother 1999). Although many small-molecule inhibitors primarily occupy a pocket within VP1, the structural integrity provided by VP3 is essential for the efficacy of these antiviral agents. Because VP3 is critical for the structural integrity and infectivity of the virus, it remains a significant target for the development of both small-molecule antivirals and neutralizing antibodies.

Other names

Viral protein 3Capsid protein VP3P3VP3 structural protein

Capsid binders (WIN compounds) occupy a hydrophobic pocket within the viral capsid, typically located in VP1 but structurally supported by VP3, which increases the rigidity of the virion and prevents the conformational changes required for viral uncoating and RNA release (Pevear et al., 1999).