Dengue Virus Infectivity Depends on Envelope Protein Binding to Target Cell Heparan Sulfate
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Authors
Chen, Yaping
Maguire, Terry
Hileman, Ronald E.
Fromm, Jonathan R.
Esko, Jeffrey D.
Linhardt, Robert J.
Marks, Rory M.
Issue Date
1997-08-01
Type
Article
Language
ENG
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Alternative Title
Abstract
Dengue virus is a human pathogen that has reemerged as an increasingly important public health threat. We found that the cellular receptor utilized by dengue envelope protein to bind to target cells is a highly sulfated type of heparan sulfate. Heparin, highly sulfated heparan sulfate, and the polysulfonate pharmaceutical Suramin effectively prevented dengue virus infection of target cells, indicating that the envelope protein-target cell receptor interaction is a critical determinant of infectivity. The dengue envelope protein sequence includes two putative glycosaminoglycan-binding motifs at the carboxy terminus; the first could be structurally modeled and formed an unusual extended binding surface of basic amino acids. Similar motifs were also identified in the envelope proteins of other flaviviridae. Developing pharmaceuticals that inhibit target cell binding may be an effective strategy for treating flavivirus infections.
Description
Nature Medicine, 3, 866-871
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Full Citation
Dengue Virus Infectivity Depends on Envelope Protein Binding toTarget Cell Heparan Sulfate, Y. Chen, T. Maguire, R. E. Hileman, J. R.Fromm, J. D. Esko, R.J. Linhardt, R. M. Marks, Nature Medicine,3,866-871, 1997.
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Volume
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PubMed ID
DOI
ISSN
10788956