Rhinovirus capsid protein VP2 (VP2)

Rhinovirus capsid protein VP2 is one of the four structural proteins (VP1, VP2, VP3, and VP4) that constitute the icosahedral shell of human rhinoviruses (HRVs), the primary cause of the common cold (NIH, PubMed). VP2 is produced through the autocatalytic cleavage of the precursor protein VP0 during the final stages of virion maturation, a process essential for infectivity (PubMed, PMC). Along with VP1 and VP3, VP2 forms the external surface of the virus and contributes to the 'canyon' structure, which facilitates binding to host cell receptors such as ICAM-1 or the low-density lipoprotein receptor (LDLR) (NIH, PMC). It plays a vital role in maintaining capsid stability and mediating the conformational changes required for the release of the viral RNA genome into the host cytoplasm (PubMed, PMC). While most small-molecule antivirals, known as capsid binders, primarily occupy a hydrophobic pocket in VP1, they exert their inhibitory effects by stabilizing the entire capsid structure, including the VP2 interfaces (PubMed, MDPI). Furthermore, VP2 contains several highly immunogenic epitopes, making it a key target for neutralizing antibodies and a focal point for the development of broadly protective vaccines (PubMed, ResearchGate). The protein's structural integrity is also critical for the virus's ability to survive in the acidic environment of the endosome during entry (PubMed). Mutations in VP2 or its interfaces can lead to resistance against capsid-binding drugs or escape from neutralizing antibodies (PubMed, PMC).

Other names

Capsid protein 2VP2Viral protein 2P1-derived protein

Capsid stabilization and inhibition of viral uncoating (PubMed, PMC)