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Heparan sulfate has an important role in cell entry by foot-and-mouth disease virus (FMDV). We find that subtype O1 FMDV binds this glycosaminoglycan with a high affinity by immobilizing a specific highly abundant motif of sulfated sugars. The binding site is a shallow depression on the virion surface, located at the junction of the three major capsid proteins, VP1, VP2 and VP3. Two pre-formed sulfate-binding sites control receptor specificity. Residue 56 of VP3, an arginine in this virus, is critical to this recognition, forming a key component of both sites. This residue is a histidine in field isolates of the virus, switching to an arginine in adaptation to tissue culture, forming the high affinity heparan sulfate-binding site. We postulate that this site is a conserved feature of FMDVs, such that in the infected animal there is a biological advantage to low affinity, or more selective, interactions with glycosaminoglycan receptors.

Original publication

DOI

10.1093/emboj/18.3.543

Type

Journal article

Journal

EMBO J

Publication Date

01/02/1999

Volume

18

Pages

543 - 554

Keywords

Adaptation, Physiological, Animals, Aphthovirus, Binding Sites, Biological Evolution, CHO Cells, Capsid, Cricetinae, Crystallography, X-Ray, Heparitin Sulfate, Integrins, Macromolecular Substances, Models, Molecular, Molecular Sequence Data, Oligosaccharides, Protein Conformation, Receptors, Cell Surface, Receptors, Virus