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Pharmaceuticals 2017, 10(2), 44; doi:10.3390/ph10020044

Pathogenesis and Inhibition of Flaviviruses from a Carbohydrate Perspective

1
,
2,3,* and 1,4,5,6,7,*
1
Biochemistry and Biophysics Graduate Program, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USA
2
Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety, Guangzhou 510640, China
3
School of Food Science and Technology, South China University of Technology, Guangzhou 510640, China
4
Department of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USA
5
Department of Biological Science, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USA
6
Department of Chemical and Biological Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USA
7
Biomedical Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USA
*
Authors to whom correspondence should be addressed.
Academic Editor: Barbara Mulloy
Received: 3 March 2017 / Revised: 24 April 2017 / Accepted: 26 April 2017 / Published: 4 May 2017
(This article belongs to the Special Issue Glycosaminoglycans and Proteoglycans)
View Full-Text   |   Download PDF [1892 KB, uploaded 4 May 2017]   |  

Abstract

Flaviviruses are enveloped, positive single stranded ribonucleic acid (RNA) viruses with various routes of transmission. While the type and severity of symptoms caused by pathogenic flaviviruses vary from hemorrhagic fever to fetal abnormalities, their general mechanism of host cell entry is similar. All pathogenic flaviviruses, such as dengue virus, yellow fever virus, West Nile virus, Japanese encephalitis virus, and Zika virus, bind to glycosaminglycans (GAGs) through the putative GAG binding sites within their envelope proteins to gain access to the surface of host cells. GAGs are long, linear, anionic polysaccharides with a repeating disaccharide unit and are involved in many biological processes, such as cellular signaling, cell adhesion, and pathogenesis. Flavivirus envelope proteins are N-glycosylated surface proteins, which interact with C-type lectins, dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN) through their glycans. In this review, we discuss both host and viral surface receptors that have the carbohydrate components, focusing on the surface interactions in the early stage of flavivirus entry. GAG-flavivirus envelope protein interactions as well as interactions between flavivirus envelope proteins and DC-SIGN are discussed in detail. This review also examines natural and synthetic inhibitors of flaviviruses that are carbohydrate-based or carbohydrate-targeting. Both advantages and drawbacks of these inhibitors are explored, as are potential strategies to improve their efficacy to ultimately help eradicate flavivirus infections. View Full-Text
Keywords: dengue virus; DC-SIGN; envelope protein; flavivirus; flavivirus inhibitors; glycosaminoglycans; Japanese encephalitis virus; proteoglycans; viral infection; West Nile virus; yellow fever virus; Zika virus dengue virus; DC-SIGN; envelope protein; flavivirus; flavivirus inhibitors; glycosaminoglycans; Japanese encephalitis virus; proteoglycans; viral infection; West Nile virus; yellow fever virus; Zika virus
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Kim, S.Y.; Li, B.; Linhardt, R.J. Pathogenesis and Inhibition of Flaviviruses from a Carbohydrate Perspective. Pharmaceuticals 2017, 10, 44.

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