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The structure and function of a foot-and-mouth disease virus-oligosaccharide receptor complex.

Abstract:

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...

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Publication status:
Published

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Publisher copy:
10.1093/emboj/18.3.543

Authors


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Institution:
University of Oxford
Department:
Oxford, MSD, Pathology Dunn School
Jackson, T More by this author
Newman, JW More by this author
Ellard, FM More by this author
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Journal:
The EMBO journal
Volume:
18
Issue:
3
Pages:
543-554
Publication date:
1999-02-05
DOI:
EISSN:
1460-2075
ISSN:
0261-4189
URN:
uuid:be777de6-60b5-40d9-90b4-790e3c6726c9
Source identifiers:
27785
Local pid:
pubs:27785

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