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The Foot-and-mouth disease virus (FMDV) antigens are structural and non-structural proteins that drive the pathogenesis of FMD in cloven-hoofed animals [11, 14]. The viral capsid is composed of four structural proteins—VP1, VP2, VP3, and VP4—which are essential for viral assembly and host cell entry [1, 11]. VP1, in particular, contains an RGD motif that mediates binding to host integrin receptors and serves as the primary target for neutralizing antibodies in infected or vaccinated animals [1, 2, 15]. Beyond their structural roles, these antigens participate in sophisticated immune evasion by antagonizing type I interferon signaling and disrupting host protein synthesis to facilitate viral replication [12, 13, 16]. In disease management, these antigens are the focus of vaccine development, including inactivated virus, recombinant protein, and virus-like particle (VLP) platforms [3, 5, 15]. The extreme antigenic variation among the seven FMDV serotypes (O, A, C, SAT 1-3, and Asia 1) presents a major challenge for therapeutic cross-protection [11, 16, 17]. Non-structural antigens, such as the 3ABC polyprotein, are critically utilized as biomarkers in Differentiating Infected from Vaccinated Animals (DIVA) diagnostic assays [8, 14, 19]. Small molecule inhibitors and monoclonal antibodies targeting these antigens or associated viral proteases are active areas of antiviral research intended to control the rapid spread of this economically devastating disease [3, 15].
Induction of neutralizing antibodies against capsid proteins; inhibition of viral attachment and entry via receptor-binding blocking; inhibition of viral polyprotein processing by protease interference; inhibition of RNA-dependent RNA polymerase; induction of host antiviral state through interferon stimulation.
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