Abstract
THE Shiga toxin family, a group of cytotoxins associated with diarrhoeal diseases and the haemolytic uraemic syndrome, includes Shiga toxin from Shigella dysenteriae type 1 and verotoxins1 produced by enteropathogenic Escherichia coli. The family belongs to the A–B class of bacterial toxins, which includes the cholera toxin family, pertussis and diphtheria toxins. These toxins all have bipartite structures consisting of an enzymatic A subunit associated with a B oligomer which binds to specific cell-surface receptors, but their amino-acid sequences and pathogenic mechanisms differ. We have determined the crystal structure of the B oligomer of verotoxin-1 from E. coll. The structure unexpectedly resembles that of the B oligomer of the cholera toxin-like heat-labile enterotoxin fromE. coli2, despite the absence of detectable sequence similarity between these two proteins. This result implies a distant evolutionary relationship between the Shiga toxin and cholera toxin families. We suggest that the cell surface receptor-binding site lies in a cleft between adjacent subunits of the B pentamer, providing a potential target for drugs and vaccines to prevent toxin binding and effect.
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
Rent or buy this article
Prices vary by article type
from$1.95
to$39.95
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Brunton, J. L. in The Bacteria Vol. 11, Molecular Basis of Bacterial Pathogenesis (eds Iglewski, B. & Clark, V) 377–398 (Academic, New York, 1990).
Sixma, T. K. et al. Nature 351, 371–377 (1991).
Seidah, N. G. et al. J. biol. Chem. 261, 13928–13931 (1986).
Jacewicz, M., Clausen, H., Nudelman, E., Donohue-Rolfe, A. & Keusch, G. T. J. exp. Med. 163, 1391–1404 (1986).
Lingwood, C. A. et al. J. biol. Chem. 262, 8834–8839 (1987).
Waddell, T., Head, S., Petric, M., Cohen, A. & Lingwood, C. Biochem. biophys. Res. Commun. 152, 674–679 (1988).
DeGrandis, S., Law, H., Brunton, J., Gyles, C. & Lingwood, C. A. J. biol. Chem. 264, 12520–12525 (1989).
Lindberg, A. A. et al. J. biol. Chem. 262, 1779–1785 (1987).
Quiocho, F. A. Pure appl. Chem. 61, 1293–1306 (1989).
Jackson, M. P., Wadolkowski, E. A., Weinstein, D. L., Holmes, R. K. & O'Brien, A. D. Bacteriology 172, 653–658 (1990).
Perera, L. P., Samuel, J. E., Holmes, R. K. & O'Brien, D. J. Bact. 173, 1151–1160 (1991).
Tyrrell, G. J. et al. Proc. natn. Acad. Sci. U.S.A. (in the press).
Sixma, T. K. et al. Nature 355, 561–564 (1992).
Bernstein, F. C. et al. J. molec. Biol. 112, 535–542 (1977).
Boodhoo, A., Read, R. J. & Brunton, J. J. molec. Biol. 221, 729–731 (1991).
Hart, P. J. et al. J. molec. Biol. 218, 691–694 (1991).
Otwinowski, Z. Am. crystallogr. Ass. 1990 Annual Meeting. New Orleans Abstr. C04 (1990).
Jones, T. A. J. appl. Crystallogr. 11, 268–272 (1978).
Jones, T. A. & Thirup, S. EMBO J. 5, 819–822 (1986).
Brünger, A. T., Kuriyan, J. & Karplus, M. Science. 235, 458–460 (1987).
Hendrickson, W. A. & Konnert, J. H. In Computing in Crystallography (eds Diamond, R., Ramaseshan, S. & Venkatesan, K.) 13.01–13.23 (Indian Institute of Sciences, Bangalore, 1980).
Read, R. J. Acta crystallogr. A42, 140–149 (1986).
Kabsch, W. & Sander, C. Biopolymers, 22, 2577–2637 (1983).
Ramotar, K. et al. Biochem. J. 273, 805–811 (1990).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Stein, P., Boodhoo, A., Tyrrell, G. et al. Crystal structure of the cell-binding B oligomer of verotoxin-1 from E. coli. Nature 355, 748–750 (1992). https://doi.org/10.1038/355748a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/355748a0
This article is cited by
-
The Fatal Role of Enterohaemorrhagic Escherichia coli Shiga Toxin-associated Extracellular Vesicles in Host Cells
Journal of Microbiology (2023)
-
Degradation and inactivation of Shiga toxins by nitrogen gas plasma
AMB Express (2017)
-
Localizing Carbohydrate Binding Sites in Proteins Using Hydrogen/Deuterium Exchange Mass Spectrometry
Journal of the American Society for Mass Spectrometry (2016)
-
Comparison of Xenorhabdus bovienii bacterial strain genomes reveals diversity in symbiotic functions
BMC Genomics (2015)
-
Shiga toxins — from cell biology to biomedical applications
Nature Reviews Microbiology (2010)
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.