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Toxins 2017, 9(2), 44;

Protection against Shiga Toxins

Department of Molecular Cell Biology, Institute for Cancer Research, Oslo University Hospital, N-0379 Oslo, Norway
Center for Cancer Biomedicine, Faculty of Medicine, Oslo University Hospital, N-0379 Oslo, Norway
Department of Biosciences, University of Oslo, N-0316 Oslo, Norway
Author to whom correspondence should be addressed.
Academic Editor: Holger Barth
Received: 29 December 2016 / Revised: 18 January 2017 / Accepted: 19 January 2017 / Published: 3 February 2017
(This article belongs to the Special Issue Novel Pharmacological Inhibitors for Bacterial Protein Toxins)
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Shiga toxins consist of an A-moiety and five B-moieties able to bind the neutral glycosphingolipid globotriaosylceramide (Gb3) on the cell surface. To intoxicate cells efficiently, the toxin A-moiety has to be cleaved by furin and transported retrogradely to the Golgi apparatus and to the endoplasmic reticulum. The enzymatically active part of the A-moiety is then translocated to the cytosol, where it inhibits protein synthesis and in some cell types induces apoptosis. Protection of cells can be provided either by inhibiting binding of the toxin to cells or by interfering with any of the subsequent steps required for its toxic effect. In this article we provide a brief overview of the interaction of Shiga toxins with cells, describe some compounds and conditions found to protect cells against Shiga toxins, and discuss whether they might also provide protection in animals and humans. View Full-Text
Keywords: Shiga toxin; Stx1; Stx2; hemolytic uremic syndrome; inhibitors; chloroquine; fluorodeoxyglucose; Mn2+ Shiga toxin; Stx1; Stx2; hemolytic uremic syndrome; inhibitors; chloroquine; fluorodeoxyglucose; Mn2+

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Kavaliauskiene, S.; Dyve Lingelem, A.B.; Skotland, T.; Sandvig, K. Protection against Shiga Toxins. Toxins 2017, 9, 44.

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