Dengue virus envelope protein domain III (EDIII) F-G loop epitope (DENV EDIII F-G loop)

The Dengue virus envelope protein domain III (EDIII) F-G loop epitope is a critical structural component of the Dengue virus (DENV) surface, specifically involved in the virus's ability to infect host cells (Wahala et al., 2010, PubMed: 20444301). EDIII is an immunoglobulin-like domain that functions as the primary receptor-binding moiety, facilitating the attachment of the virus to host cell surface molecules such as DC-SIGN or heparan sulfate (Crill & Roehrig, 2001, PubMed: 11689846). The F-G loop is a specific peptide sequence within this domain that forms a prominent part of the lateral surface epitope, making it highly accessible to the host's immune system. This epitope is a major target for potent neutralizing antibodies, which can block viral entry and prevent infection (Shrestha et al., 2010, PubMed: 20660191). Consequently, it is a focal point for the design of recombinant subunit vaccines and therapeutic monoclonal antibodies, such as the clinical candidate VIS513 (Visterra Inc.). However, therapeutic intervention must be carefully managed due to the risk of antibody-dependent enhancement (ADE), a phenomenon where non-neutralizing or sub-neutralizing antibodies facilitate viral uptake into myeloid cells, potentially exacerbating the disease (Halstead, 2003, PubMed: 12631894). Understanding the precise molecular interactions at the F-G loop is therefore essential for developing safe and effective pan-serotype treatments for Dengue.

Other names

DENV EDIIIDengue virus E protein domain 3ED3 F-G loopLateral surface epitope of EDIIIDENV E-DIII F-G loop

Neutralization of viral particles by sterically blocking the interaction between the viral envelope protein and host cell receptors, thereby preventing viral attachment and subsequent entry.