Publications associées à Shigatoxine

Bactericidal effect of tetracycline in E. coli strain ED1a may be associated with ribosome dysfunction

Camille Véronique Bernadette Goemans, Christian Eugen Zimmerli, Martin Beck

Ribosomes translate the genetic code into proteins. Recent technical advances have facilitated in situ structural analyses of ribosome functional states inside eukaryotic cells and the minimal bacterium Mycoplasma. However, such analyses of Gram-negative b ...

Nature Research2024

Harnessing the Membrane Translocation Properties of AB Toxins for Therapeutic Applications

Françoise Gisou van der Goot Grunberg, Oksana Andrei Sergeeva

Over the last few decades, proteins and peptides have become increasingly more common as FDA-approved drugs, despite their inefficient delivery due to their inability to cross the plasma membrane. In this context, bacterial two-component systems, termed AB ...

2021

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

Henning Paul-Julius Stahlberg

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

Mammalian membrane trafficking as seen through the lens of bacterial toxins

Françoise Gisou van der Goot Grunberg, Francisco De Magalhães Sarmento R De Mesquita, Oksana Andrei Sergeeva

A fundamental question of eukaryotic cell biology is how membrane organelles are organised and interact with each other. Cell biologists address these questions by characterising the structural features of membrane compartments and the mechanisms that coor ...

WILEY2020

Mechanisms protecting host cells against bacterial pore-forming toxins

Francisco De Magalhães Sarmento R De Mesquita

Pore-forming toxins (PFTs) are key virulence determinants produced and secreted by a variety of human bacterial pathogens. They disrupt the plasma membrane (PM) by generating stable protein pores, which allow uncontrolled exchanges between the extracellula ...

SPRINGER BASEL AG2019

Targeted protein degradation through cytosolic delivery of monobody binders using bacterial toxins

Oliver Hantschel, Nadine Eliane Schmit, Katyayanee Neopane

Monobodies are small engineered binding proteins that, upon expression in cells, can inhibit signaling of cytosolic oncoproteins with outstanding selectivity. Efficacy may be further increased by inducing degradation of monobody targets through fusion to t ...

2019

Functional analysis of RIP toxins from the Drosophila endosymbiont Spiroplasma poulsonii

Bruno Lemaitre, Florent François Masson, Juan Camilo Paredes Escobar, Mario Gonzalo Garcia Arraez

BackgroundInsects frequently live in close relationship with symbiotic bacteria that carry out beneficial functions for their host, like protection against parasites and viruses. However, in some cases, the mutualistic nature of such associations is put in ...

2019

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

Association of brain amyloidosis with pro-inflammatory gut bacterial taxa and peripheral inflammation markers in cognitively impaired elderly

Tristan Bolmont, Taoufiq Harach

The pathway leading from amyloid-b deposition to cognitive impairment is believed to be a cornerstone of the pathogenesis of Alzheimer's disease (AD). However, what drives amyloid buildup in sporadic nongenetic cases of AD is still unknown. AD brains featu ...

Elsevier Science Inc2017

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 Ins and Outs of Anthrax Toxin

Françoise Gisou van der Goot Grunberg

Anthrax is a severe, although rather rare, infectious disease that is caused by the Gram-positive, spore-forming bacterium Bacillus anthracis. The infectious form is the spore and the major virulence factors of the bacterium are its poly-gamma-D-glutamic a ...

Mdpi Ag2016

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

Glucose- but Not Rice-Based Oral Rehydration Therapy Enhances the Production of Virulence Determinants in the Human Pathogen Vibrio cholerae

Andrea Rinaldo, Melanie Blokesch, Enrico Bertuzzo, Flavio Finger, Juliane Kühn, Marino Gatto

Despite major attempts to prevent cholera transmission, millions of people worldwide still must address this devastating disease. Cholera research has so far mainly focused on the causative agent, the bacterium Vibrio cholerae, or on disease treatment, but ...

2014

Did Cholera Toxin Finally Get Caught?

Françoise Gisou van der Goot Grunberg

To orchestrate immune responses, pathogen-recognition receptors have evolved sophisticated strategies to monitor pathogenic processes. In this issue of Cell Host & Microbe, a study by Cho et al. reveals a mechanism of immune recognition that relies on the ...

Cell Press2013

Caspase-2 is an initiator caspase responsible for pore-forming toxin-mediated apoptosis

Françoise Gisou van der Goot Grunberg

Bacterial pathogens modulate host cell apoptosis to establish a successful infection. Pore-forming toxins (PFTs) secreted by pathogenic bacteria are major virulence factors and have been shown to induce various forms of cell death in infected cells. Here w ...

Nature Publishing Group2012

Dual Chaperone Role of the C-Terminal Propeptide in Folding and Oligomerization of the Pore-Forming Toxin Aerolysin

Françoise Gisou van der Goot Grunberg, Matteo Dal Peraro, Mircea Ioan Iacovache, Sylvia Ho, Matteo Thomas Degiacomi

Throughout evolution, one of the most ancient forms of aggression between cells or organisms has been the production of proteins or peptides affecting the permeability of the target cell membrane. This class of virulence factors includes the largest family ...

2011

Genetic evidence for a protective role of the peritrophic matrix against intestinal bacterial infection in Drosophila melanogaster

Bruno Lemaitre, Onya Opota, Olivier Binggeli, Takayuki Kuraishi

The peritrophic matrix (PM) forms a layer composed of chitin and glycoproteins that lines the insect intestinal lumen. This physical barrier plays a role analogous to that of mucous secretions of the vertebrate digestive tract and is thought to protect the ...

National Academy of Sciences2011

Cellular Responses to Bacterial Pore-Forming Toxins

Rodrigo Manuel Gonzalez

Pore-forming toxins (PFTs) represent the largest class of bacterial protein toxins and constitute major virulence factors produced by pathogenic bacteria during infection. Pore formation appears to be an ancient form of attack, which is also found in hydro ...

EPFL2011

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