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Coxsackievirus A16 (CVA16) is a major pathogen responsible for hand, foot, and mouth disease (HFMD), a common infectious illness that primarily affects infants and young children worldwide [1]. The CVA16 virion is a non-enveloped, positive-sense single-stranded RNA virus with a capsid composed of 60 copies of four structural proteins: VP1, VP2, VP3, and VP4 [2]. These proteins, particularly VP1, contain critical antigenic epitopes that are recognized by the host immune system and are essential for viral attachment to host receptors like scavenger receptor class B member 2 (SCARB2) and P-selectin glycoprotein ligand-1 (PSGL-1) [3]. Therapeutic and preventive strategies focus on these capsid epitopes to elicit neutralizing antibodies that prevent viral entry and uncoating [4]. Inactivated CVA16 vaccines and recombinant subunit vaccines targeting these epitopes are the primary focus of clinical development to mitigate the public health burden of HFMD outbreaks [5]. Understanding the structural biology of these epitopes is crucial for the design of broad-spectrum vaccines and potent monoclonal antibody therapies [6].
Neutralization of viral entry and uncoating; Induction of neutralizing antibodies and T-cell responses
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