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Dengue virus serotype 2 envelope protein domain III (DENV2 EDIII) is a critical structural component of the DENV2 virion surface, functioning primarily as the receptor-binding domain that facilitates viral attachment to host cells (UniProt P07564). It is a ~100-amino acid immunoglobulin-like fold located at the C-terminus of the envelope (E) protein, which is the major protein involved in receptor recognition and membrane fusion (PubMed: 15956572). Because EDIII contains many serotype-specific neutralizing epitopes, it is a primary target for the development of subunit vaccines and therapeutic monoclonal antibodies aimed at preventing DENV2 infection (PubMed: 26109513). However, targeting this domain requires careful design to avoid inducing sub-neutralizing antibodies that could lead to antibody-dependent enhancement (ADE), a phenomenon where non-neutralizing antibodies facilitate viral entry into immune cells via Fc receptors, potentially worsening the disease (PubMed: 20539737). Current research focuses on utilizing EDIII in recombinant protein vaccines and identifying potent neutralizing antibodies like 2D22 that specifically bind this domain to block infection (PubMed: 26109513).
Neutralization of viral infection by blocking host cell receptor binding and preventing viral entry into the target cell.
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