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CRYSTAL-STRUCTURE OF THE CELL-BINDING B-OLIGOMER OF VEROTOXIN-1 FROM ESCHERICHIA-COLI
Author(s): STEIN PE, BOODHOO A, TYRRELL GJ, BRUNTON JL, READ RJ
Source: NATURE    Volume: 355    Issue: 6362    Pages: 748-750    Published: FEB 20 1992  
Times Cited: 204     References: 24     
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 I and verotoxins 1 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. coli. The structure unexpectedly resembles that of the B oligomer of the cholera toxin-like heat-labile enterotoxin from E. coli 2, 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.
Document Type: Article
Language: English
Addresses:
1. UNIV ALBERTA, DEPT MED MICROBIOL & INFECT DIS, EDMONTON T6G 2H7, ALBERTA CANADA
2. MT SINAI HOSP, SAMUEL LUNENFELD RES INST, TORONTO M5G 1X5, ONTARIO CANADA
3. UNIV TORONTO, DEPT MICROBIOL, TORONTO M5S 1A1, ONTARIO CANADA
4. UNIV TORONTO, DEPT MED, TORONTO M5S 1A1, ONTARIO CANADA
Publisher: MACMILLAN MAGAZINES LTD, PORTERS SOUTH, 4 CRINAN ST, LONDON, ENGLAND N1 9XW
Subject Category: Multidisciplinary Sciences
IDS Number: HE604
ISSN: 0028-0836
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