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Chikungunya virus (CHIKV) viral antigens comprise a suite of structural and non-structural proteins essential for the viral life cycle and pathogenesis. The structural proteins, specifically the E1 and E2 envelope glycoproteins, are the primary targets for the host immune response and vaccine development; E2 facilitates binding to host cell receptors like Mxra8, while E1 mediates pH-dependent membrane fusion (Silva & Dermody, 2017). The non-structural proteins (nsP1, nsP2, nsP3, and nsP4) form the viral replicase complex, with nsP2 acting as a protease and helicase and nsP4 serving as the RNA-dependent RNA polymerase (Ahola & Merits, 2016). These antigens are the causative agents of Chikungunya fever, a disease characterized by acute febrile illness and severe, often debilitating, polyarthralgia that can persist for months or years (Burt et al., 2017). Therapeutic interventions targeting these antigens include the FDA-approved live-attenuated vaccine Ixchiq, which elicits protective neutralizing antibodies, and various experimental monoclonal antibodies and small-molecule inhibitors designed to disrupt viral entry or replication machinery (FDA, 2023).
Vaccines (e.g., VLA1553) induce neutralizing antibodies that target the E2 and E1 envelope glycoproteins to block viral attachment and membrane fusion (FDA, 2023; Silva & Dermody, 2017). Antiviral small molecules target non-structural proteins, such as nsP2 to inhibit protease/helicase activity or nsP4 to inhibit RNA-dependent RNA polymerase (RdRp) activity, thereby halting viral genome replication (Ahola & Merits, 2016).
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