Human rhinovirus 14 capsid protein VP1 (HRV-14 VP1)

Human rhinovirus 14 (HRV-14) capsid protein VP1 is a primary structural component of the viral icosahedral shell, playing a critical role in the viral life cycle. It contains a surface feature known as the "canyon," which serves as the binding site for the host cell receptor, Intercellular Adhesion Molecule 1 (ICAM-1), facilitating viral attachment and entry (Rossmann et al., 1985; Greve et al., 1989). Located beneath the canyon floor is a hydrophobic pocket that typically accommodates a host-derived "pocket factor," which is essential for maintaining the structural integrity and flexibility required for viral uncoating (Oliveira et al., 1993). This pocket is a major therapeutic target for antiviral compounds called capsid binders, such as Pleconaril, which displace the pocket factor to stabilize the capsid and prevent the release of the viral genome (Pevear et al., 1999). By inhibiting the uncoating process, these drugs effectively block viral replication at an early stage. However, the high genetic diversity of rhinovirus serotypes and the rapid development of resistance mutations within the VP1 pocket present significant challenges for the clinical success of these therapies (Rotbart, 2002; Kim et al., 2007).

Other names

Viral protein 1VP1Capsid protein VP1HRV14 VP1

Capsid-binding inhibitors bind to a hydrophobic pocket within the VP1 protein, which stabilizes the viral capsid and prevents the conformational changes necessary for viral uncoating and genome release. Additionally, binding can sterically hinder the interaction between the viral canyon and the host cell receptor ICAM-1.