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

The Dengue virus serotype 2 envelope glycoprotein (E protein) is the primary structural component of the viral surface, organized as 90 head-to-tail homodimers in the mature virion (UniProt: P07564). It is responsible for the initial stages of infection, including binding to host cell receptors such as DC-SIGN and mediating pH-dependent membrane fusion within the endosome (PubMed: 15105493). Structurally, the E protein consists of three distinct domains (DI, DII, and DIII), with DIII being the primary site for receptor binding and a major target for neutralizing antibodies (PubMed: 12191471). In the context of disease, DENV-2 is often associated with more severe clinical outcomes, and the E protein's variability among the four serotypes complicates vaccine design. Therapeutic strategies focus on using the E protein as an antigen in vaccines like Qdenga or developing monoclonal antibodies that block its fusion loop or receptor-binding domain (PubMed: 25762141). A significant challenge in targeting this protein is antibody-dependent enhancement (ADE), where non-neutralizing or sub-neutralizing antibodies facilitate viral entry into Fc-gamma receptor-expressing cells, potentially exacerbating the infection (PubMed: 20445044).

Other names

Envelope protein EDENV2 E proteinDengue virus type 2 E proteinViral envelope protein

Neutralization of viral entry by blocking receptor binding or preventing pH-dependent membrane fusion (PubMed: 25762141, PubMed: 15105493).