Human Rhinovirus capsid protein VP1 and VP2 epitopes (HRV VP1/VP2)

Human Rhinovirus (HRV) capsid proteins VP1 and VP2 are essential structural components of the virus, which is the primary cause of the common cold and a major trigger for asthma and COPD exacerbations (Jacobs et al., 2013; Kennedy et al., 2012). These proteins form the icosahedral shell of the virus, with VP1 containing a deep surface depression known as the 'canyon' that facilitates binding to host cell receptors such as ICAM-1 (Rossmann et al., 1985). The epitopes on the surface of VP1 and VP2 are the primary targets for the host's neutralizing antibody response, making them critical for vaccine development and monoclonal antibody therapies (Edlmayr et al., 2011). Antiviral drugs like pleconaril and vapendavir interact with a hydrophobic pocket beneath the VP1 canyon, stabilizing the capsid to inhibit viral uncoating and the subsequent release of the viral genome (Pevear et al., 1999). However, the high degree of antigenic variation across more than 160 HRV serotypes presents a significant challenge for creating broad-spectrum treatments targeting these epitopes (Palmenberg et al., 2009). Ongoing research aims to identify highly conserved epitopes across different HRV species to develop more effective, universal vaccines (Niespodziana et al., 2012).

Other names

HRV VP1HRV VP2Human Rhinovirus capsid proteinsHRV antigenic sitesRhinovirus surface proteins

Binding to the hydrophobic pocket of the VP1 capsid protein to prevent viral uncoating and attachment to host cell receptors.