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The envelope (E) protein of dengue virus type 2 (DENV-2) is the principal structural glycoprotein on the viral surface. It plays a central role in mediating viral attachment to host cells and facilitating membrane fusion, which is essential for viral entry and infection. The E protein is also the primary target for neutralizing antibodies, making it a key focus for vaccine and therapeutic development. The E protein monomer consists of three distinct ectodomains: Domain I (EDI), Domain II (EDII), and Domain III (EDIII). EDI organizes the overall fold, EDII contains the fusion peptide, and EDIII is involved in receptor binding and is targeted by neutralizing antibodies. Ninety E protein homodimers form an icosahedral shell covering the virion surface. The E protein also contains two conserved N-linked glycosylation sites: Asn-67 and Asn-153.
Inhibition of viral entry
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