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The Chikungunya virus envelope glycoprotein complex consists primarily of three proteins: **E1, E2, and E3**—derived from a precursor polyprotein that is cleaved during viral maturation[1][2][3]. The E1 glycoprotein is responsible for mediating membrane fusion between the virus and host cell during entry, while the E2 glycoprotein is responsible for binding to host cell receptors, including Mxra8 and glycosaminoglycans[1][3][4]. E3 stabilizes the complex in the immature virus particle and is cleaved off during maturation[1][3]. The envelope glycoprotein spikes, formed as E1-E2 heterodimers (trimeric on the virion surface), are major antigenic determinants and the main targets of neutralizing antibodies generated during infection or vaccination[1][3][5]. These proteins play a central role in **viral attachment, cell entry, and initiation of infection**, making them key targets for vaccines, serological diagnostics, and investigational antiviral therapies[1][3][5].
Inhibition of virus-cell fusion (by blocking E1 protein or its conformational changes)[1][3] Blockade of viral receptor binding (by targeting E2 protein interactions with host factors such as Mxra8)[1][4][5] Neutralization via antibody binding to exposed epitopes on E2 or E1[5]
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