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Coxsackievirus A16 utilizes cell surface heparan sulfate glycosaminoglycans as its attachment receptor
Coxsackievirus A16 (CVA16) is one of the major pathogens responsible for hand, foot and mouth disease, which affects more than two million children in the Asian-Pacific region annually. Previous studies have shown that scavenger receptor B2 is a functional receptor for CVA16 that facilitates the unc...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5567171/ https://www.ncbi.nlm.nih.gov/pubmed/28745308 http://dx.doi.org/10.1038/emi.2017.55 |
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author | Zhang, Xueyang Shi, Jinping Ye, Xiaohua Ku, Zhiqiang Zhang, Chao Liu, Qingwei Huang, Zhong |
author_facet | Zhang, Xueyang Shi, Jinping Ye, Xiaohua Ku, Zhiqiang Zhang, Chao Liu, Qingwei Huang, Zhong |
author_sort | Zhang, Xueyang |
collection | PubMed |
description | Coxsackievirus A16 (CVA16) is one of the major pathogens responsible for hand, foot and mouth disease, which affects more than two million children in the Asian-Pacific region annually. Previous studies have shown that scavenger receptor B2 is a functional receptor for CVA16 that facilitates the uncoating process. However, it remains unclear whether other receptors are required for efficient CVA16 infection. In this study, by using a variety of assays we demonstrated that CVA16 utilizes surface heparan sulfate glycosaminoglycans as its attachment receptor. We further showed that five surface-exposed positively charged residues located in a cluster at the five-fold vertex of the virion are critical to heparan sulfate binding and cellular attachment of CVA16. Among the five residues, the arginine at position 166 (R166) of VP1 capsid protein appeared to be the most important for the interaction between CVA16 and heparan sulfate. Alanine substitution at this site (R166A) almost completely abolished heparan sulfate binding and cellular attachment of the virus. Our work achieves insight into the early events of CVA16 infection, thereby providing information that may facilitate the rational design of antiviral drugs and vaccines against CVA16 infection. |
format | Online Article Text |
id | pubmed-5567171 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-55671712017-08-30 Coxsackievirus A16 utilizes cell surface heparan sulfate glycosaminoglycans as its attachment receptor Zhang, Xueyang Shi, Jinping Ye, Xiaohua Ku, Zhiqiang Zhang, Chao Liu, Qingwei Huang, Zhong Emerg Microbes Infect Original Article Coxsackievirus A16 (CVA16) is one of the major pathogens responsible for hand, foot and mouth disease, which affects more than two million children in the Asian-Pacific region annually. Previous studies have shown that scavenger receptor B2 is a functional receptor for CVA16 that facilitates the uncoating process. However, it remains unclear whether other receptors are required for efficient CVA16 infection. In this study, by using a variety of assays we demonstrated that CVA16 utilizes surface heparan sulfate glycosaminoglycans as its attachment receptor. We further showed that five surface-exposed positively charged residues located in a cluster at the five-fold vertex of the virion are critical to heparan sulfate binding and cellular attachment of CVA16. Among the five residues, the arginine at position 166 (R166) of VP1 capsid protein appeared to be the most important for the interaction between CVA16 and heparan sulfate. Alanine substitution at this site (R166A) almost completely abolished heparan sulfate binding and cellular attachment of the virus. Our work achieves insight into the early events of CVA16 infection, thereby providing information that may facilitate the rational design of antiviral drugs and vaccines against CVA16 infection. Nature Publishing Group 2017-07 2017-07-26 /pmc/articles/PMC5567171/ /pubmed/28745308 http://dx.doi.org/10.1038/emi.2017.55 Text en Copyright © 2017 The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Original Article Zhang, Xueyang Shi, Jinping Ye, Xiaohua Ku, Zhiqiang Zhang, Chao Liu, Qingwei Huang, Zhong Coxsackievirus A16 utilizes cell surface heparan sulfate glycosaminoglycans as its attachment receptor |
title | Coxsackievirus A16 utilizes cell surface heparan sulfate glycosaminoglycans as its attachment receptor |
title_full | Coxsackievirus A16 utilizes cell surface heparan sulfate glycosaminoglycans as its attachment receptor |
title_fullStr | Coxsackievirus A16 utilizes cell surface heparan sulfate glycosaminoglycans as its attachment receptor |
title_full_unstemmed | Coxsackievirus A16 utilizes cell surface heparan sulfate glycosaminoglycans as its attachment receptor |
title_short | Coxsackievirus A16 utilizes cell surface heparan sulfate glycosaminoglycans as its attachment receptor |
title_sort | coxsackievirus a16 utilizes cell surface heparan sulfate glycosaminoglycans as its attachment receptor |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5567171/ https://www.ncbi.nlm.nih.gov/pubmed/28745308 http://dx.doi.org/10.1038/emi.2017.55 |
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