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The envelope (E) protein of dengue virus type 1 (DENV-1) is the major structural glycoprotein on the surface of the virion. It plays a central role in viral attachment, entry, and membrane fusion during infection. The E protein mediates binding to host cell receptors and undergoes significant conformational changes to facilitate fusion between the viral and host membranes, allowing delivery of the viral genome into the cytosol. The E protein is organized as a homodimer on mature virions and consists of three distinct domains: Domain I (EDI), Domain II (EDII), and Domain III (EDIII). It contains two N-linked glycosylation sites: Asn-67 and Asn-153. EDIII contains epitopes recognized by potent neutralizing antibodies. A hydrophobic pocket at an interdomain interface modulates pH sensitivity required for triggering fusion and represents a potential site for small-molecule inhibitors.
Inhibition of viral entry by blocking receptor binding or membrane fusion. Stabilization of pre-fusion conformation.
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