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research article

Mechanism of Shiga Toxin Clustering on Membranes

Pezeshkian, Weria
•
Gao, Haifei
•
Arumugam, Senthil
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2017
ACS Nano

The bacterial Shiga toxin interacts with its cellular receptor, the glycosphingolipid globotriaosylceramide (Gb3 or CD77), as a first step to entering target cells. Previous studies have shown that toxin molecules cluster on the plasma membrane, despite the apparent lack of direct interactions between them. The precise mechanism by which this clustering occurs remains poorly defined. Here, we used vesicle and cell systems and computer simulations to show that line tension due to curvature, height or compositional mismatch, and lipid or solvent depletion cannot drive the clustering of Shiga toxin molecules. By contrast, in coarse-grained computer simulations a correlation was found between clustering and toxin nanoparticle-driven suppression of membrane fluctuations, and experimentally we observed that clustering required the toxin molecules to be tightly bound to the membrane surface. The most likely interpretation of these findings is that a membrane fluctuation-induced force generates an effective attraction between toxin molecules. Such force would be of similar strength to the electrostatic force at separations around 1 nm, remain strong at distances up to the size of toxin molecules (several nm), and persist even beyond. This force is predicted to operate between manufactured nanoparticles providing they are sufficiently rigid and tightly bound to the plasma membrane, thereby suggesting a route for the targeting of nanoparticles to cells for biomedical applications.

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Type
research article
DOI
10.1021/acsnano.6b05706
Web of Science ID

WOS:000392886500032

Author(s)
Pezeshkian, Weria
•
Gao, Haifei
•
Arumugam, Senthil
•
Becken, Ulrike
•
Bassereau, Patricia
•
Florent, Jean-Claude
•
Ipsen, John Hjort
•
Johannes, Ludger
•
Shillcock, Julian Charles  
Date Issued

2017

Published in
ACS Nano
Volume

11

Issue

1

Start page

314

End page

324

Subjects

Casimir force

•

Fluctuation-induced force

•

Endocytosis

•

Invagination

•

Membrane clustering

•

Glyocsphingolipid

Editorial or Peer reviewed

REVIEWED

Written at

EPFL

EPFL units
BBP-CORE  
RelationRelated workURL/DOI

IsContinuedBy

https://infoscience.epfl.ch/record/259353
Available on Infoscience
December 17, 2016
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/132050
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