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      How foot-and-mouth disease virus receptor mediates foot-and-mouth disease virus infection

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          Abstract

          This study reviews the FMDV receptor-binding domain, integrin receptors, and heparan sulfate receptors to provide references for studies regarding the mechanisms underlying FMDV infection.

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          RGD and other recognition sequences for integrins.

          E Ruoslahti (1996)
          Proteins that contain the Arg-Gly-Asp (RGD) attachment site, together with the integrins that serve as receptors for them, constitute a major recognition system for cell adhesion. The RGD sequence is the cell attachment site of a large number of adhesive extracellular matrix, blood, and cell surface proteins, and nearly half of the over 20 known integrins recognize this sequence in their adhesion protein ligands. Some other integrins bind to related sequences in their ligands. The integrin-binding activity of adhesion proteins can be reproduced by short synthetic peptides containing the RGD sequence. Such peptides promote cell adhesion when insolubilized onto a surface, and inhibit it when presented to cells in solution. Reagents that bind selectively to only one or a few of the RGD-directed integrins can be designed by cyclizing peptides with selected sequences around the RGD and by synthesizing RGD mimics. As the integrin-mediated cell attachment influences and regulates cell migration, growth, differentiation, and apoptosis, the RGD peptides and mimics can be used to probe integrin functions in various biological systems. Drug design based on the RGD structure may provide new treatments for diseases such as thrombosis, osteoporosis, and cancer.
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            Protection against foot-and-mouth disease by immunization with a chemically synthesized peptide predicted from the viral nucleotide sequence.

            Thomas Shinnick, Thomas R Lerner, William H. Alexander … (1982)
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              Efficient infection of cells in culture by type O foot-and-mouth disease virus requires binding to cell surface heparan sulfate.

              F M Ellard, W Blakemore, A Corteyn … (1996)
              Foot-and-mouth disease virus (FMDV) enters cells by attaching to cellular receptor molecules of the integrin family, one of which has been identified as the RGD-binding integrin alpha(v)beta3. Here we report that, in addition to an integrin binding site, type O strains of FMDV share with natural ligands of alpha(v)beta3 (i.e., vitronectin and fibronectin) a specific affinity for heparin and that binding to the cellular form of this sulfated glycan, heparan sulfate, is required for efficient infection of cells in culture. Binding of the virus to paraformaldehyde-fixed cells was powerfully inhibited by agents such as heparin, that compete with heparan sulfate or by agents that compete for heparan sulfate (platelet factor 4) or that inactivate it (heparinase). Neither chondroitin sulfate, a structurally related component of the extracellular matrix, nor dextran sulfate appreciably inhibited binding. The functional importance of heparan sulfate binding was demonstrated by the facts that (i) infection of live cells by FMDV could also be blocked specifically by heparin, albeit at a much higher concentration of inhibitor; (ii) pretreatment of cells with heparinase reduced the number of plaques formed compared with that for untreated cells; and (iii) mutant cell lines deficient in heparan sulfate expression were unable to support plaque formation by FMDV, even though they remained equally susceptible to another picornavirus, bovine enterovirus. The results show that entry of type O FMDV into cells is a complex process and suggest that the initial contact with the cell surface is made through heparan sulfate.
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                Author and article information

                Contributors
                Guangxiang Wang: wanggx666@163.com
                Yanhua Wang: wangyh061001@163.com
                Youjun Shang: yjshang71@hotmail.com
                Zhidong Zhang: zhangzhidong@caas.cn
                Xiangtao Liu: hnxiangtao@163.com
                Journal
                Journal ID (nlm-ta): Virol J
                Journal ID (iso-abbrev): Virol. J
                Title: Virology Journal
                Publisher: BioMed Central (London )
                ISSN (Electronic): 1743-422X
                Publication date (Electronic): 3 February 2015
                Publication date PMC-release: 3 February 2015
                Publication date Collection: 2015
                Volume: 12
                Electronic Location Identifier: 9
                Affiliations
                [ ]State Key Laboratory of Veterinary Etiological Biology, Lanzhou, 730046 China
                [ ]National Foot-and-Mouth Disease Reference Laboratory, Lanzhou, 730046 China
                [ ]Key Laboratory of Animal Virology of Ministry of Agriculture, Lanzhou, 730046 China
                [ ]Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, 730046 China
                Article
                Publisher ID: 246
                DOI: 10.1186/s12985-015-0246-z
                PMC ID: 4322448
                PubMed ID: 25645358
                SO-VID: ad06c1fa-1070-49d6-b046-fd843f46728f
                Copyright © © Wang et al.; licensee BioMed Central. 2015
                License:

                This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver ( http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

                History
                Date received : 15 October 2014
                Date accepted : 19 January 2015
                Categories
                Subject: Review
                Custom metadata
                issue-copyright-statement © The Author(s) 2015

                ScienceOpen disciplines: Microbiology & Virology
                Keywords: foot-and-mouth disease virus,receptor,infection
                Data availability:
                ScienceOpen disciplines: Microbiology & Virology
                Keywords: foot-and-mouth disease virus, receptor, infection

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