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

Logan, Derek LU orcid ; Abu-Ghazaleh, Robin ; Blakemore, Wendy ; Curry, Stephen ; Jackson, Terry ; King, Andrew ; Lea, Susan ; Lewis, Richard ; Newman, John and Parry, Nigel , et al. (1993) In Nature 362(6420). p.566-568
Abstract

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 processes1-7. In our original crystal structure of FMDV the Arg-Gly-Asp-containing loop ('the loop'), located between β-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 (ref. 8). We report here the crystal structure of the virus in which this disulphide is reduced. Reduced virus retains infectivity and serological... (More)

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 processes1-7. In our original crystal structure of FMDV the Arg-Gly-Asp-containing loop ('the loop'), located between β-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 (ref. 8). 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 conserved8. 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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publishing date
type
Contribution to journal
publication status
published
subject
in
Nature
volume
362
issue
6420
pages
3 pages
publisher
Nature Publishing Group
external identifiers
  • scopus:0027417816
  • pmid:8385272
ISSN
0028-0836
DOI
10.1038/362566a0
language
English
LU publication?
no
id
d19ff9fb-97fb-4dda-847e-5ebe531d9c14
date added to LUP
2022-04-08 09:03:00
date last changed
2024-06-24 08:16:19
@article{d19ff9fb-97fb-4dda-847e-5ebe531d9c14,
  abstract     = {{<p>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<sup>1-7</sup>. In our original crystal structure of FMDV the Arg-Gly-Asp-containing loop ('the loop'), located between β-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 (ref. 8). 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<sup>8</sup>. 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.</p>}},
  author       = {{Logan, Derek and Abu-Ghazaleh, Robin and Blakemore, Wendy and Curry, Stephen and Jackson, Terry and King, Andrew and Lea, Susan and Lewis, Richard and Newman, John and Parry, Nigel and Rowlands, David and Stuart, David and Fry, Elizabeth}},
  issn         = {{0028-0836}},
  language     = {{eng}},
  number       = {{6420}},
  pages        = {{566--568}},
  publisher    = {{Nature Publishing Group}},
  series       = {{Nature}},
  title        = {{Structure of a major immunogenic site on foot-and-mouth disease virus}},
  url          = {{http://dx.doi.org/10.1038/362566a0}},
  doi          = {{10.1038/362566a0}},
  volume       = {{362}},
  year         = {{1993}},
}