Coxsackievirus A10 capsid conformational epitopes (CVA10 epitopes)

Coxsackievirus A10 (CVA10) capsid conformational epitopes are specific three-dimensional arrangements of amino acids on the viral surface that serve as the primary targets for the host's neutralizing immune response (Zhu et al., 2018, Nature Communications). These epitopes are primarily located on the structural proteins VP1, VP2, and VP3, which assemble to form the icosahedral shell of the virus (Tang et al., 2020, Journal of Virology). They play a critical role in the viral life cycle by mediating attachment to host cell receptors, most notably KREMEN1, and facilitating subsequent viral entry and uncoating (Zhu et al., 2018, Nature Communications). In the context of disease, CVA10 is a significant pathogen responsible for hand, foot, and mouth disease (HFMD), herpangina, and occasionally severe neurological complications (Fan et al., 2020, Vaccine). Therapeutic strategies focusing on these epitopes include the development of inactivated vaccines and monoclonal antibodies designed to block viral infection (Ye et al., 2020, PLOS Pathogens). Neutralizing antibodies typically bind to these conformational sites to sterically hinder receptor interaction or stabilize the capsid to prevent the release of the viral genome (Tang et al., 2020, Journal of Virology). Understanding the precise structure of these epitopes is essential for overcoming challenges such as antigenic drift and ensuring broad protection against diverse CVA10 strains (Zhu et al., 2018, Nature Communications).

Other names

CVA10 antigenic determinantsCoxsackievirus A10 neutralizing sitesCVA10 capsid surface antigensCVA10 VP1-VP2-VP3 conformational epitopes

Neutralization of viral infectivity by sterically hindering binding to the host receptor KREMEN1 or by stabilizing the viral capsid to prevent the release of the viral RNA genome (uncoating).