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J Gen Virol. 2012 Jan;93(Pt 1):72-82. doi: 10.1099/vir.0.037317-0. Epub 2011 Sep 28.

Residues in domain III of the dengue virus envelope glycoprotein involved in cell-surface glycosaminoglycan binding.

Author information

1
Australian Infectious Diseases Research Centre, School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, Queensland 4072, Australia.

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.

PMID:
21957126
DOI:
10.1099/vir.0.037317-0
[Indexed for MEDLINE]

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