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The Chikungunya virus (CHIKV) envelope consists of two major glycoproteins, E1 and E2, which form heterodimers that assemble into trimeric spikes on the viral surface. E2 is primarily responsible for receptor binding, specifically interacting with host cell receptors such as Mxra8 to facilitate viral attachment. E1 is a class II fusion protein that mediates the fusion of the viral envelope with the host endosomal membrane following a pH-dependent conformational change. Together, these proteins are the primary targets for the host immune response and are the focus of vaccine and therapeutic development. Neutralizing antibodies typically target the E2 protein to block entry or the E1 protein to prevent membrane fusion. The first FDA-approved vaccine for Chikungunya, Ixchiq (VLA1553), utilizes a live-attenuated virus that expresses these structural proteins to elicit a protective immune response.
Neutralization of viral entry by blocking receptor binding (E2) or inhibiting pH-dependent membrane fusion (E1).
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