Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/28069
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Type: Journal article
Title: Neutralization of shiga toxins Stx1, Stx2c, and Stx2e by recombinant bacteria expressing mimics of globotriose and globotetraose
Author: Paton, A.
Morona, R.
Paton, J.
Citation: Infection and Immunity, 2001; 69(3):1967-1970
Publisher: Amer Soc Microbiology
Issue Date: 2001
ISSN: 0019-9567
1098-5522
Statement of
Responsibility: 
Adrienne W. Paton, Renato Morona, and James C. Paton
Abstract: Strains of Escherichia coli producing Shiga toxins Stx1, Stx2, Stx2c, and Stx2d cause gastrointestinal disease and the hemolytic-uremic syndrome in humans. We have recently constructed a recombinant bacterium which displays globotriose (the receptor for these toxins) on its surface and adsorbs and neutralizes these Shiga toxins with very high efficiency. This agent has great potential for the treatment of humans with such infections. E. coli strains which cause edema disease in pigs produce a variant toxin, Stx2e, which has a different receptor specificity from that for the other members of the Stx family. We have now modified the globotriose-expressing bacterium such that it expresses globotetraose (the preferred receptor for Stx2e) by introducing additional genes encoding a N-acetylgalactosamine transferase and a UDP-N-acetylgalactosamine-4-epimerase. This bacterium had a reduced capacity to neutralize Stx1 and Stx2c in vitro, but remarkably, its capacity to bind Stx2e was similar to that of the globotriose-expressing construct; both constructs neutralized 98.4% of the cytotoxicity in lysates of E. coli JM109 expressing cloned stx2e. These data suggest that either globotriose- or globotetraose-expressing constructs may be suitable for treatment and/or prevention of edema disease in pigs.
Keywords: Glycolipids; Globosides; Oligosaccharides; Receptors, Cell Surface; Genetic Engineering; Molecular Mimicry; Carbohydrate Sequence; Molecular Sequence Data; Shiga Toxin 1; Shiga Toxin 2
Description: Copyright © 2001, American Society for Microbiology. All rights reserved.
RMID: 0020010645
DOI: 10.1128/IAI.69.3.1967-1970.2001
Appears in Collections:Molecular and Biomedical Science publications

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