Abstract
CHANGES resulting in altered antigenic properties of viruses nearly always occur on their surface and have been attributed to the substitution of residues directly involved in binding antibody. To investigate the mechanism of antigenic variation in foot-and-mouth disease virus (FMDV), variants that escape neutralization by a monoclonal antibody have been compared crystallographically and serologically with parental virus. FMDVs form one of the four genera of the Picornaviridae. The unenveloped icosahedral shell comprises 60 copies each of four structural proteins VP1–4. Representatives from each of the genera have similar overall structure, but differences in the external features1–4. For example, human rhinovirus has a pronounced 'canyon' that is proposed to contain the cell attachment site1,5–7, whereas elements of the attachment site for FMDV, which involves the G–H loop (residues 134–160) and C-terminus (200–213) of VP18,9, are exposed on the surface. Moreover, this G–H loop, which is a major antigenic site of FMDV, forms a prominent, highly accessible protrusion4, a feature not seen in other picornaviruses. It is this loop that is perturbed in the variant viruses that we have studied. The amino acid mutations characterizing the variants are not at positions directly involved in antibody binding, but result in far-reaching perturbations of the surface structure of the virus. Thus, this virus seems to use a novel escape mechanism whereby an induced confor-mational change in a major antigenic loop destroys the integrity of the epitope.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Rossmann, M. G. et al. Nature 317, 145–153 (1985).
Hogle, J. M., Chow M. & Filman D. J. Science 229, 1358–1365 (1985).
Luo, M. et al. Science 235, 182–191 (1987).
Acharya, R. et al. Nature 337, 709–716 (1989).
Colonno, R. J. et al. Proc. natn. Acad. Sci. U.S.A. 85, 5449–5453 (1988).
Greve, J. M. et al. Cell 56, 839–847 (1989).
Staunton, D. E. et al. Cell 56, 849–853 (1989).
Fox, G. et al. J. gen. Virol. 70, 625–637 (1989).
Surovoi, A. Y., Ivanov, V. T., Chepurkin, A. V., Ivanyushchenkov, V. N. & Dryagalin, N. N. Soviet J. bio-organic Chem. 14, 527–580 (1989).
Barnett, P. V., Ouldridge, E. J., Rowlands, D. J., Brown, F. & Parry, N. R. J. gen. Virol. 70, 1483–1491 (1989).
Parry, N. R., Barnett, P. V., Ouldridge, E. J., Rowlands, D. J. & Brown, F. J. gen. Virol. 70, 1493–1503 (1989).
Strohmaier, K., Franze, R. & Adam, K. H. J. gen. Virol. 59, 295–306 (1982).
Ouldridge, E. J. et al. J. gen. Virol. 65, 203–207 (1984).
McCullough, K. C., Crowther, J. R. & Butcher, R. N. J. immun. Meth. 82, 91–100 (1985).
Fox, G. et al. J. molec. Biol. 196, 591–597 (1987).
Bricogne, G. Acta crystallogr. A32, 832–847 (1976).
Bolwell, C. et al. J. gen. Virol. 70, 59–68 (1989).
Mateu, M. G. et al. Virus Research 8, 261–274 (1987).
Bolwell, C. et al. J. gen. Virol. 70, 45–57 (1989).
Bittle, J. L. et al. Nature 298, 30–33 (1982).
Thomas, A. A. M., Woortmeijer, R. J., Puijk, W. & Barteling, S. J. J. Virol. 62, 2782–2789 (1988).
McCahon, D. et al. J. gen. Virol. 70, 639–645 (1989).
Baxt, B. & Bachrach, H. L. Virology 104, 42–55 (1980).
Monod, J., Wyman, J. & Changeux, J.-P. Biochemistry 5, 365–385 (1965).
Kabsch, W. J. appl. Crystallogr. 21, 67–71 (1988).
Badger J. et al. Proc. natn. Acad. Sci. U.S.A. 85, 3304–3308 (1988).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Parry, N., Fox, G., Rowlands, D. et al. Structural and serological evidence for a novel mechanism of antigenic variation in foot-and-mouth disease virus. Nature 347, 569–572 (1990). https://doi.org/10.1038/347569a0
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1038/347569a0
This article is cited by
-
Production of foot-and-mouth disease virus SAT2 VP1 protein
AMB Express (2020)
-
How foot-and-mouth disease virus receptor mediates foot-and-mouth disease virus infection
Virology Journal (2015)
-
Genetic characterization of the cell-adapted PanAsia strain of foot-and-mouth disease virus O/Fujian/CHA/5/99 isolated from swine
Virology Journal (2010)
-
B cell epitopes within VP1 of type O foot-and-mouth disease virus for detection of viral antibodies
Virologica Sinica (2010)
-
A Novel Mucosal Vaccine Against Foot-and-Mouth Disease Virus Induces Protection in Mice and Swine
Biotechnology Letters (2005)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.