Dengue virus serotype 2 envelope protein (DENV-2 E protein)

The Dengue virus serotype 2 envelope protein (E protein) is the major surface glycoprotein on the mature virion, composed of 180 copies arranged as homodimers. It consists of three β-sheet domains (DI central, DII dimerization with fusion loop, DIII), a membrane-proximal stem, amphipathic helix, and transmembrane anchor. At neutral pH, it forms stable prefusion dimers; low pH in endosomes triggers rearrangement to postfusion trimers, driving viral-endosomal membrane fusion for genome release. It contains a hydrophobic ligand-binding pocket at the DI/DII interface that opens via β-hairpin shift, influencing fusion pH threshold. The protein exhibits temperature-dependent morphology (smooth at 29°C, bumpy at 37°C due to loosened dimer interactions) and is targeted by neutralizing antibodies at inter-dimer, intra-dimer, and domain-specific epitopes.

Other names

DENV2 envelope glycoproteinDENV-2 E glycoproteinsE protein (soluble ectodomain)

Neutralization by binding quaternary epitopes across E dimers to prevent conformational reorganization and membrane fusion, Binding domain III or fusion loop to disrupt virion architecture and induce premature fusion loop exposure