VP1 capsid protein of human rhinovirus 14 (VP1)

The **VP1 capsid protein of human rhinovirus 14** is the largest and most surface-exposed component of the icosahedral viral capsid, forming, along with VP2 and VP3, the outer shell of the virion, while VP4 lines the inner surface[2][3][8]. Each human rhinovirus virion contains 60 copies of VP1, which adopts an eight-stranded β-barrel fold[3][6]. VP1 is central to viral infection: it mediates host cell attachment via binding to cellular receptors, primarily **intercellular adhesion molecule 1 (ICAM-1)** in HRV14, triggering a cascade of conformational changes that prime the virus for genome release upon cell entry[1][2][5]. Its surface-exposed loops are highly variable and antigenic, making VP1 the dominant neutralizing epitope and a focus for antiviral antibody responses[7]. Drugs targeting VP1, such as pleconaril, act by binding hydrophobic pockets within the protein, stabilizing the capsid and blocking the uncoating process necessary for viral replication[8]. Due to its essential roles in the viral life cycle and infection, VP1 is a validated antiviral **therapeutic target**, but its substantial antigenic diversity and rapid evolution present significant challenges for vaccine and drug design[2][7].

Other names

VP1Viral protein 1 of human rhinovirus 14Major capsid protein VP1 (HRV14)

Inhibition of viral uncoating by stabilizing the capsid (e.g., pleconaril and related capsid-binding antivirals) Blockade of receptor attachment by antibody (neutralizing antibodies target exposed VP1 loops[2][7]) Inhibition of capsid assembly or conformational change needed for genome release