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Protection against Shiga Toxins

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 endoplasmi...

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Autores principales: Kavaliauskiene, Simona, Dyve Lingelem, Anne Berit, Skotland, Tore, Sandvig, Kirsten
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5331424/
https://www.ncbi.nlm.nih.gov/pubmed/28165371
http://dx.doi.org/10.3390/toxins9020044
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author Kavaliauskiene, Simona
Dyve Lingelem, Anne Berit
Skotland, Tore
Sandvig, Kirsten
author_facet Kavaliauskiene, Simona
Dyve Lingelem, Anne Berit
Skotland, Tore
Sandvig, Kirsten
author_sort Kavaliauskiene, Simona
collection PubMed
description 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.
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spelling pubmed-53314242017-03-13 Protection against Shiga Toxins Kavaliauskiene, Simona Dyve Lingelem, Anne Berit Skotland, Tore Sandvig, Kirsten Toxins (Basel) Review 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. MDPI 2017-02-03 /pmc/articles/PMC5331424/ /pubmed/28165371 http://dx.doi.org/10.3390/toxins9020044 Text en © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Kavaliauskiene, Simona
Dyve Lingelem, Anne Berit
Skotland, Tore
Sandvig, Kirsten
Protection against Shiga Toxins
title Protection against Shiga Toxins
title_full Protection against Shiga Toxins
title_fullStr Protection against Shiga Toxins
title_full_unstemmed Protection against Shiga Toxins
title_short Protection against Shiga Toxins
title_sort protection against shiga toxins
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5331424/
https://www.ncbi.nlm.nih.gov/pubmed/28165371
http://dx.doi.org/10.3390/toxins9020044
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