Human rhinovirus capsid protein VP1 (VP1)

Human rhinovirus capsid protein VP1 is a major structural component of the human rhinovirus (HRV) capsid, forming part of the outer shell that encapsulates the viral RNA genome. The HRV capsid consists of 60 copies each of four proteins—VP1, VP2, VP3, and internal VP4—with VP1 primarily forming the vertices of the icosahedral structure. VP1 mediates initial attachment to host cells by interacting with specific cellular receptors such as intercellular adhesion molecule 1 (ICAM‑1), low-density lipoprotein receptor (LDLR), or cadherin-related family member 3 (CDHR3), depending on HRV species. This interaction is essential for viral entry into host cells. The exposed regions of VP1 are highly variable, contributing significantly to antigenic diversity among HRV strains and influencing immune recognition. Because it plays a central role in both cell entry and immune evasion, VP1 has been targeted for antiviral drug development, particularly with compounds like pleconaril that bind within a hydrophobic pocket in the protein structure to block infection. Overall, human rhinovirus capsid protein VP1 is considered an important therapeutic target for interventions aimed at preventing or treating HRV infections.

Other names

HRV VP1Rhinovirus VP1Capsid protein VP1 (HRV)

Inhibition of viral attachment to host cells by blocking receptor binding site on VP1; Inhibition of virion uncoating or destabilization by binding to hydrophobic pocket in the capsid