Next Article in Journal
Can Inhibitors of Snake Venom Phospholipases A2 Lead to New Insights into Anti-Inflammatory Therapy in Humans? A Theoretical Study
Next Article in Special Issue
The Use of Plant-Derived Ribosome Inactivating Proteins in Immunotoxin Development: Past, Present and Future Generations
Previous Article in Journal
Investigation of Non-Covalent Interactions of Aflatoxins (B1, B2, G1, G2, and M1) with Serum Albumin
Previous Article in Special Issue
A Monoclonal–Monoclonal Antibody Based Capture ELISA for Abrin
Article Menu
Issue 11 (November) cover image

Export Article

Open AccessFeature PaperReview
Toxins 2017, 9(11), 340; https://doi.org/10.3390/toxins9110340

Shiga Toxin—A Model for Glycolipid-Dependent and Lectin-Driven Endocytosis

Cellular and Chemical Biology Department, Institut Curie, PSL Research University, U1143 INSERM, UMR3666 CNRS, 26 rue d’Ulm, 75248 Paris CEDEX 05, France
Academic Editors: Julien Barbier and Daniel Gillet
Received: 28 September 2017 / Revised: 15 October 2017 / Accepted: 20 October 2017 / Published: 25 October 2017
(This article belongs to the Special Issue Ribosome Inactivating Toxins)
View Full-Text   |   Download PDF [1417 KB, uploaded 21 November 2017]   |  

Abstract

The cellular entry of the bacterial Shiga toxin and the related verotoxins has been scrutinized in quite some detail. This is due to their importance as a threat to human health. At the same time, the study of Shiga toxin has allowed the discovery of novel molecular mechanisms that also apply to the intracellular trafficking of endogenous proteins at the plasma membrane and in the endosomal system. In this review, the individual steps that lead to Shiga toxin uptake into cells will first be presented from a purely mechanistic perspective. Membrane-biological concepts will be highlighted that are often still poorly explored, such as fluctuation force-driven clustering, clathrin-independent membrane curvature generation, friction-driven scission, and retrograde sorting on early endosomes. It will then be explored whether and how these also apply to other pathogens, pathogenic factors, and cellular proteins. The molecular nature of Shiga toxin as a carbohydrate-binding protein and that of its cellular receptor as a glycosylated raft lipid will be an underlying theme in this discussion. It will thereby be illustrated how the study of Shiga toxin has led to the proposal of the GlycoLipid-Lectin (GL-Lect) hypothesis on the generation of endocytic pits in processes of clathrin-independent endocytosis. View Full-Text
Keywords: glycosphingolipid; globotriaosylceramide; Gb3; raft; galectin; integrin; CD44; cholera toxin; thermal Casimir-like force; spontaneous curvature glycosphingolipid; globotriaosylceramide; Gb3; raft; galectin; integrin; CD44; cholera toxin; thermal Casimir-like force; spontaneous curvature
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
SciFeed

Share & Cite This Article

MDPI and ACS Style

Johannes, L. Shiga Toxin—A Model for Glycolipid-Dependent and Lectin-Driven Endocytosis. Toxins 2017, 9, 340.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Toxins EISSN 2072-6651 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top