Dengue Virus Envelope Protein (E protein)

The dengue virus envelope (E) protein is a membrane-spanning glycoprotein that plays a central role in the viral life cycle. It is the principal determinant of virion assembly and acts as the fusion catalyst for merging viral and host cell membranes. The E protein mediates viral attachment to host cells, entry via membrane fusion, and is also the primary target for neutralizing antibodies. On mature virions, E proteins are arranged as antiparallel homodimers on the surface, forming a herringbone pattern within lipid rafts. Upon exposure to low pH during endocytosis, these dimers rearrange into trimers to drive membrane fusion. Glycosylation sites on E are critical for interaction with cell-surface lectins such as DC-SIGN; both N-linked glycosylation sites at Asn-67 (unique to dengue) and Asn-153 (conserved among flaviviruses) are required for efficient recognition by DC-SIGN-expressing dendritic cells. A hydrophobic pocket within domain II influences pH threshold for triggering fusion; this site can accept small ligands or inhibitors that may block conformational changes necessary for entry—a potential antiviral drug target.

Other names

DENV E proteinDengue virus envelope glycoprotein

Inhibition of viral entry by blocking conformational changes required for membrane fusion; antibody-mediated neutralization of the virus.