Dengue virus serotype 1 envelope glycoprotein (DENV-1 E)

The Dengue virus serotype 1 envelope glycoprotein (DENV-1 E) is the primary structural protein on the surface of the DENV-1 virion and is essential for viral infectivity. It is a class II viral fusion protein that exists as a homodimer on the mature virus surface and undergoes a dramatic structural rearrangement into a trimer during the fusion process. The protein is organized into three distinct domains: Domain I (DI) serves as the central structural core, Domain II (DII) contains the highly conserved fusion loop required for membrane insertion, and Domain III (DIII) is primarily responsible for binding to host cell receptors such as DC-SIGN and heparan sulfate. DENV-1 E is the principal target for neutralizing antibodies and is the central component of current tetravalent vaccines, including Dengvaxia and Qdenga, as well as therapeutic monoclonal antibodies like VIS513. However, the E protein is also the primary driver of antibody-dependent enhancement (ADE), a phenomenon where sub-neutralizing or cross-reactive antibodies from a previous infection with a different serotype facilitate viral entry into Fc-receptor-bearing immune cells, significantly increasing the risk of severe clinical manifestations like dengue hemorrhagic fever.

Other names

DENV-1 E proteinDengue virus type 1 envelope proteinEnvelope glycoprotein EDENV1-EDengue virus 1 E protein

Neutralization of viral particles, inhibition of viral attachment to host cell receptors, and blockade of pH-dependent membrane fusion within the endosome.