Publications related to Shigatoxigenic and verotoxigenic Escherichia coli

Identification of a Dps contamination in Mitomycin-C–induced expression of Colicin Ia

Colicins are bacterial toxins targeting Gram-negative bacteria, including E. coli and related Enterobacteriaceae strains. Some colicins form ion-gated pores in the inner membrane of attacked bacteria that are lethal to their target. Colicin Ia was the firs ...

2021

Mechanism of Shiga Toxin Clustering on Membranes

Julian Charles Shillcock

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 th ...

2017

Membrane invagination induced by Shiga toxin B-subunit: from molecular structure to tube formation

Julian Charles Shillcock

The bacterial Shiga toxin is composed of an enzymatically active A-subunit, and a receptor-binding homopentameric B-subunit (STxB) that mediates intracellular toxin trafficking. Upon STxB-mediated binding to the glycolipid globotriaosylceramide (Gb3) at th ...

Royal Society of Chemistry2016

Pore-forming toxins: ancient, but never really out of fashion

Françoise Gisou van der Goot Grunberg, Matteo Dal Peraro

Pore-forming toxins (PFTs) are virulence factors produced by many pathogenic bacteria and have long fascinated structural biologists, microbiologists and immunologists. Interestingly, pore-forming proteins with remarkably similar structures to PFTs are fou ...

Nature Publishing Group2016

The effects of globotriaosylceramide tail saturation level on bilayer phases

Julian Charles Shillcock

Globotriaosylceramide (Gb(3)) is a glycosphingolipid present in the plasma membrane that is the natural receptor of the bacterial Shiga toxin. The unsaturation level of Gb(3) acyl chains has a drastic impact on lipid bilayer properties and phase behaviour, ...

Royal Soc Chemistry2015

Preliminary crystallographic analysis of two oligomerization-deficient mutants of the aerolysin toxin, H132D and H132N, in their proteolyzed forms

Françoise Gisou van der Goot Grunberg

Aerolysin is a major virulence factor produced by the Gram-negative bacterium Aeromonas hydrophila and is a member of the beta-pore-forming toxin family. Two oligomerization-deficient aerolysin mutants, H132D and H132N, have been overproduced, proteolyzed ...

2010