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The dengue virus envelope glycoprotein (commonly referred to as "E protein") is the principal surface protein of the dengue virus and plays a central role in viral attachment, entry, and membrane fusion during infection. It is also the main target for neutralizing antibodies and vaccine development efforts. The E protein is organized into three distinct domains: Domain I (EDI), Domain II (EDII), and Domain III (EDIII). It mediates initial binding of dengue virus to host cell receptors and triggers fusion between viral and cellular membranes. There are two N-linked glycosylation sites: Asn-67 and Asn-153. The E protein contains major antigenic determinants recognized by neutralizing antibodies. Knowledge of the E protein structure has enabled rational design strategies targeting either receptor-binding or fusogenic functions.
Small-molecule inhibitors targeting receptor-binding or fusogenic functions, vaccines eliciting neutralizing antibodies.
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