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Human rhinovirus capsid protein VP2 (VP2) is a primary structural protein of the Human Rhinovirus (HRV), the most common cause of the common cold and a significant trigger for respiratory complications like asthma and COPD (Jacobs et al., 2013, Clinical Microbiology Reviews). It assembles with VP1, VP3, and VP4 to form the icosahedral viral capsid, which protects the viral RNA and facilitates infection of host cells (Rossmann et al., 1985, Nature). VP2 is located on the virion surface and is involved in the formation of the canyon and surface ridges that interact with host receptors and the immune system (UniProt, P03303). Although most small-molecule capsid inhibitors, such as Pleconaril and Vapendavir, bind to a hydrophobic pocket within the VP1 protein, they function by stabilizing the entire capsid assembly, including VP2, to prevent the uncoating process (Kim et al., 2005, Journal of Molecular Biology). VP2 is also a major target for the host's neutralizing antibody response, making it a focus for vaccine development and the engineering of therapeutic antibodies (Ledford et al., 2004, Journal of Virology). Understanding the structural role of VP2 is essential for overcoming the challenges posed by the high genetic diversity of the over 160 known HRV serotypes.
Capsid stabilization to prevent viral uncoating and blocking of receptor binding
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