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Coxsackievirus A10 (CVA10) capsid proteins VP1, VP2, VP3, and VP4 are the structural components that form the icosahedral shell of the virus, protecting its RNA genome. These proteins are derived from the cleavage of the P1 precursor polyprotein by viral proteases. VP1, VP2, and VP3 are located on the external surface and are primarily responsible for host cell receptor recognition—specifically binding to KREMEN1—and initiating the infection process, while VP4 is positioned internally. As the primary targets for the host immune system, these proteins are the focus of vaccine development, including inactivated and virus-like particle (VLP) candidates designed to elicit neutralizing antibodies. Additionally, the 'canyon' structure on the capsid surface serves as a potential site for small-molecule antiviral drugs, such as capsid binders, which inhibit viral uncoating and entry into the host cell.
Vaccines targeting these proteins induce neutralizing antibodies that block viral attachment to host receptors like KREMEN1. Small molecule capsid binders typically stabilize the viral capsid to prevent the release of viral RNA (uncoating) into the host cytoplasm.
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