Dengue virus infectivity depends on envelope protein binding to target cell heparan sulfate
| Autor: | Jonathan R. Fromm, Robert J. Linhardt, Terry Maguire, Ronald E. Hileman, Jeffrey D. Esko, Rory M. Marks, Yaping Chen |
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| Rok vydání: | 1997 |
| Předmět: |
Molecular Sequence Data
CHO Cells Suramin Plasma protein binding Dengue virus medicine.disease_cause General Biochemistry Genetics and Molecular Biology Dengue fever chemistry.chemical_compound Viral Envelope Proteins Cricetinae Chlorocebus aethiops medicine Animals Antibody-dependent enhancement Amino Acid Sequence Vero Cells Peptide sequence Glycosaminoglycans Infectivity Virulence Heparin Chemistry General Medicine Heparan sulfate Dengue Virus medicine.disease Immunohistochemistry Virology Vero cell Receptors Virus Heparitin Sulfate Protein Binding |
| Zdroj: | Nature Medicine. 3:866-871 |
| ISSN: | 1546-170X 1078-8956 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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