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The structure and function of a foot‐and‐mouth disease virus–oligosaccharide receptor complex
Author(s) -
Fry Elizabeth E.,
Lea Susan M.,
Jackson Terry,
Newman John W.I.,
Ellard Fiona M.,
Blakemore Wendy E.,
AbuGhazaleh Robin,
Samuel Alan,
King Andrew M.Q.,
Stuart David I.
Publication year - 1999
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/18.3.543
Subject(s) - library science , biology , management , art history , history , computer science , economics
Heparan sulfate has an important role in cell entry by foot‐and‐mouth disease virus (FMDV). We find that subtype O 1 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.