Coxsackievirus A10 capsid protein (CVA10 capsid)

Coxsackievirus A10 (CVA10) capsid proteins, consisting of the structural subunits VP1, VP2, VP3, and VP4, form the icosahedral shell of the virus and are essential for protecting the viral RNA and facilitating host cell infection (Zhu et al., 2018, Sci Adv). The surface-exposed epitopes on VP1, VP2, and VP3 contain critical antigenic sites that are the primary targets for neutralizing antibodies and are vital for binding to the host cell receptor, KREMEN1 (Staring et al., 2018, Cell Host Microbe). CVA10 is a major causative agent of hand, foot, and mouth disease (HFMD) and herpangina, particularly in children, and has been associated with severe neurological complications and systemic illness (Expert Rev Anti Infect Ther, 2019). Currently, there are no approved vaccines or antiviral drugs specifically for CVA10, making these capsid proteins a high-priority target for the development of inactivated vaccines, virus-like particles (VLPs), and therapeutic monoclonal antibodies like 2G8 (Zhu et al., 2018). Research has identified key residues, such as VP2 N142, that are essential for receptor interaction and viral neutralization (Li et al., 2023, PLoS Pathog). Therapeutic strategies often focus on blocking the canyon region or the hydrophobic pocket within VP1 to inhibit viral attachment or uncoating (Chen et al., 2019, Cell Discov).

Other names

Coxsackievirus A10 structural proteinsCVA10 VP1CVA10 VP2CVA10 VP3CVA10 VP4Coxsackievirus A10 surface epitopesCVA10 surface antigens

Neutralization of viral infectivity by binding to surface epitopes to block interaction with the host receptor KREMEN1, or by binding to the hydrophobic pocket in VP1 to stabilize the capsid and prevent viral uncoating and genome release.