Human Rhinovirus 16 capsid protein VP1 hydrophobic pocket (HRV16 VP1 pocket)

The VP1 hydrophobic pocket of Human Rhinovirus 16 (HRV16) is a specialized cavity located within the VP1 protein of the viral capsid, situated beneath the floor of the “canyon” which serves as the binding site for the host cell receptor ICAM-1 [1][2]. In its native state, this pocket is often occupied by a host-derived “pocket factor,” typically a fatty acid-like molecule, which maintains the structural stability of the virion [2]. During the infection process, the displacement of this pocket factor is a prerequisite for the conformational changes required for viral uncoating and the subsequent release of the viral RNA into the host cytoplasm [1][4]. Therapeutic agents known as capsid binders, such as Pleconaril, target this pocket by binding with higher affinity than the natural pocket factor, thereby over-stabilizing the capsid and preventing the uncoating process [3][5]. This mechanism effectively halts viral replication at the early entry stage, making the VP1 pocket a focal point for antiviral strategies against HRV-mediated respiratory illnesses, including the common cold and exacerbations of asthma or COPD [3][5]. Citations: [1] Rossmann MG, et al. Nature. 1985;317(6033):145-153. [2] Oliveira MA, et al. Structure. 1993;1(1):51-68. [3] Pevear DC, et al. Antimicrob Agents Chemother. 1999;43(9):2109-2115. [4] Ledford RM, et al. J Virol. 2004;78(7):3663-3674. [5] Rotbart HA. Antiviral Res. 2002;53(2):83-98.

Other names

HRV16 VP1 canyonVP1 hydrophobic cavityCapsid binding pocketWIN-binding pocket

Capsid stabilization and inhibition of viral uncoating