Dengue virus serotype 3 envelope protein (E protein (DENV-3 E protein))

The Dengue virus serotype 3 envelope protein is a 53kDa glycoprotein that forms homodimers on the viral surface, mediating initial attachment and entry into host cells. This protein consists of three domains: DI (central), DII (fusion domain), and DIII (receptor-binding domain)[4][7]. It is responsible for binding to host-cell receptors (such as DC-SIGN and heparan sulfate), facilitating fusion between the viral and endosomal membranes following acidification[4][9]. Domain III, which is immunoglobulin-like, contains serotype-specific epitopes and serves as the primary binding site for neutralizing antibodies and many vaccine candidates[2][5][7]. The protein is a major therapeutic target for dengue, but its high variability across strains and the phenomenon of antibody-dependent enhancement present key challenges for drug and vaccine development[1][4][8]. Genomic differences in the E gene are important for diagnosis and patient stratification, and the E protein is used as an antigen in serological assays and research on viral pathogenesis.

Other names

DENV-3 E proteinEnvelope glycoprotein (serotype 3)E glycoprotein (Dengue serotype 3)Dengue virus type 3 envelope protein

Inhibition of membrane fusion (prevents viral entry into host cells[1]) Blockade of receptor binding (prevents attachment to host cells[4]) Neutralization by binding to specific epitopes (serotype-specific or cross-reactive domains, notably on EDIII[5])