Structure of a major immunogenic site on foot-and-mouth disease virus

Attachment of foot-and-mouth disease virus (FMDV) to its cellular receptor involves a long and highly antigenic loop containing the conserved sequence, Arg-Gly-Asp, a motif known to be a recognition element in many integrin-dependent cell adhesion processes. In our original crystal structure of FMDV...

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Bibliographic Details
Published inNature (London) Vol. 362; no. 6420; pp. 566 - 568
Main Authors Logan, D, Abu-Ghazaleh, R, Blakemore, W, Curry, S, Jackson, T, King, A, Lea, S, Lewis, R, Newman, J
Format Journal Article
LanguageEnglish
Published London Nature Publishing 08.04.1993
Nature Publishing Group
Subjects
antigens
Aphthovirus
Aphthovirus - chemistry
Biological and medical sciences
Biological properties
Capsid - chemistry
Capsid Proteins
Crystallography
Foot-and-mouth disease virus
Fundamental and applied biological sciences. Psychology
Medical research
Microbiology
Molecular Conformation
Molecular Structure
Morphology, structure, chemical composition, physicochemical properties
Oligopeptides
Picornaviridae
receptors
structure
Virology
Viruses
Virus
Proteins
Aphthovirus
Conserved sequence
Picornaviridae
Infectivity
Property structure relationship
Capsid
Immunodominance
Conformation
Crystalline structure
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Summary:Attachment of foot-and-mouth disease virus (FMDV) to its cellular receptor involves a long and highly antigenic loop containing the conserved sequence, Arg-Gly-Asp, a motif known to be a recognition element in many integrin-dependent cell adhesion processes. In our original crystal structure of FMDV the Arg-Gly-Asp-containing loop ('the loop'), located between beta-strands G and H of capsid protein VP1, was disordered and hence essentially invisible. We previously surmised that its disorder is enhanced by a disulphide bond linking the base of the loop (Cys 134) to Cys 130 of VP2. We report here the crystal structure of the virus in which this disulphide is reduced. Reduced virus retains infectivity and serological experiments suggest that some of the loop's internal structure is conserved. But here its structure has become sufficiently ordered to allow us to describe an unambiguous conformation, which we relate to some key biological properties of the virus.
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ISSN:0028-0836
1476-4687
DOI:10.1038/362566a0