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The structure of an immunodominant loop on foot and mouth disease virus, serotype O1, determined under reducing conditions

Rowlands, D. ; Logan, D. LU orcid ; Abu-Ghazaleh, R. ; Blakemore, W. ; Curry, S. ; Jackson, T. ; King, A. ; Lea, S. ; Lewis, R. and Newman, J. , et al. (1994) In Archives of virology. Supplementum 9. p.51-58
Abstract

Residues 136-159 of VPI of foot and mouth disease virus (FMDV) comprise the G-H loop of the protein and form a prominent feature on the surface of virus particles. This sequence contains an immunodominant neutralizing epitope, which can be mimicked with synthetic peptides, and includes an Arg, Gly, Asp motif which has been implicated in the binding of the virus to cellular receptors. Crystallographic analysis of native virus particles failed to resolve the structure of this region due to its disordered state. However, reduction of a disulphide bond between cysteine residues 134 of VP1 and 130 of VP2 caused the G-H loop to collapse onto the surface of the virus particle and allowed its conformation to be determined.

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publishing date
type
Contribution to journal
publication status
published
subject
in
Archives of virology. Supplementum
volume
9
pages
8 pages
publisher
Springer
external identifiers
  • scopus:0028249435
  • pmid:8032279
ISSN
0939-1983
DOI
10.1007/978-3-7091-9326-6_6
language
English
LU publication?
no
id
fffa8528-45b6-4389-8e75-3c546d4bb123
date added to LUP
2022-06-03 09:03:01
date last changed
2024-01-03 14:59:26
@article{fffa8528-45b6-4389-8e75-3c546d4bb123,
  abstract     = {{<p>Residues 136-159 of VPI of foot and mouth disease virus (FMDV) comprise the G-H loop of the protein and form a prominent feature on the surface of virus particles. This sequence contains an immunodominant neutralizing epitope, which can be mimicked with synthetic peptides, and includes an Arg, Gly, Asp motif which has been implicated in the binding of the virus to cellular receptors. Crystallographic analysis of native virus particles failed to resolve the structure of this region due to its disordered state. However, reduction of a disulphide bond between cysteine residues 134 of VP1 and 130 of VP2 caused the G-H loop to collapse onto the surface of the virus particle and allowed its conformation to be determined.</p>}},
  author       = {{Rowlands, D. and Logan, D. and Abu-Ghazaleh, R. and Blakemore, W. and Curry, S. and Jackson, T. and King, A. and Lea, S. and Lewis, R. and Newman, J. and Parry, Nigel and Stuart, D. and Fry, E.}},
  issn         = {{0939-1983}},
  language     = {{eng}},
  pages        = {{51--58}},
  publisher    = {{Springer}},
  series       = {{Archives of virology. Supplementum}},
  title        = {{The structure of an immunodominant loop on foot and mouth disease virus, serotype O1, determined under reducing conditions}},
  url          = {{http://dx.doi.org/10.1007/978-3-7091-9326-6_6}},
  doi          = {{10.1007/978-3-7091-9326-6_6}},
  volume       = {{9}},
  year         = {{1994}},
}