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  • Title: Residues in domain III of the dengue virus envelope glycoprotein involved in cell-surface glycosaminoglycan binding.
    Author: Watterson D, Kobe B, Young PR.
    Journal: J Gen Virol; 2012 Jan; 93(Pt 1):72-82. PubMed ID: 21957126.
    Abstract:
    The dengue virus (DENV) envelope (E) protein mediates virus entry into cells via interaction with a range of cell-surface receptor molecules. Cell-surface glycosaminoglycans (GAGs) have been shown to play an early role in this interaction, and charged oligosaccharides such as heparin bind to the E protein. We have examined this interaction using site-directed mutagenesis of a recombinant form of the putative receptor-binding domain III of the DENV-2E protein expressed as an MBP (maltose-binding protein)-fusion protein. Using an ELISA-based GAG-binding assay, cell-based binding analysis and antiviral-activity assays, we have identified two critical residues, K291 and K295, that are involved in GAG interactions. These studies have also demonstrated differential binding between mosquito and human cells.
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