Publications associées à Hémolysine

Functional and structural characterization of Serratia marcescens ExbB: determinants of the interaction with HasB/TonB

ExbBD is part of a cytoplasmic membrane molecular motor driven by the proton-motive force. It belongs to the larger family of motors involved in nutriment import across the outer membrane of Gram-negative bacteria (ExbBD), flagellar rotation (MotAB) or lat ...

2021

The molecular treasure box of environmental Vibrio cholerae strains

Natalia Carolina Drebes Dorr

Cholera pandemics have been affecting humankind for centuries and are still considered a major public health problem, especially in regions around the world with poor access to clean water and sanitation. Cholera pandemics are caused by a specific lineage ...

EPFL2021

The evolution of the type VI secretion system as a disintegration weapon

Julius Hans Bernd Winter

The type VI secretion system (T6SS) is a nanomachine used by many bacteria to drive a toxin-laden needle into other bacterial cells. Although the potential to influence bacterial competition is clear, the fitness impacts of wielding a T6SS are not well und ...

PUBLIC LIBRARY SCIENCE2020

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

Anthrax toxin requires ZDHHC5-mediated palmitoylation of its surface-processing host enzymes

Françoise Gisou van der Goot Grunberg, Oksana Andrei Sergeeva

The protein acyl transferase ZDHHC5 was recently proposed to regulate trafficking in the endocytic pathway. Therefore, we explored the function of this enzyme in controlling the action of bacterial toxins. We found that ZDHHC5 activity is required for two ...

National Academy of Sciences2019

Development of potent and selective S. aureus sortase A inhibitors Based on Peptide Macrocycles

Christian Heinis, Inmaculada Rentero Rebollo, Davide Bertoldo

Sortases are transpeptidase enzymes that anchor surface proteins, including virulence factors, to the cell wall of Gram-positive bacteria, and they are potential targets for the development of anti-infective agents. While several large compound libraries w ...

2016

Quantitative Single-Cell Analysis of Host-Pathogen Interactions

Matthieu Jean-Hubert Delincé

During infection, microbial pathogens encounter phagocytic cells of the host innate immune system, such as macrophages and neutrophils. These encounters typically lead to uptake and killing of the bacteria by the host cell or, conversely, parasitization of ...

EPFL2016

Use of VacA as a Vaccine Antigen

Dominique Velin, Mati André Marie Moyat

One of the major toxins secreted by H. pylori is the Vacuolating cytotoxin A (VacA) named after its ability to induce the formation of "vacuole"-like membrane vesicles in the cytoplasm of gastric cells. VacA has been associated with the disruption of mitoc ...

Mdpi Ag2016

Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process

Françoise Gisou van der Goot Grunberg, Matteo Dal Peraro, Mircea Ioan Iacovache, Nuria Cirauqui Diaz

Owing to their pathogenical role and unique ability to exist both as soluble proteins and transmembrane complexes, pore-forming toxins (PFTs) have been a focus of microbiologists and structural biologists for decades. PFTs are generally secreted as water-s ...

Nature Publishing Group2016

X-ray and Cryo-electron Microscopy Structures of Monalysin Pore-forming Toxin Reveal Multimerization of the Pro-form

Bruno Lemaitre, Onya Opota

beta-Barrel pore-forming toxins (beta-PFT), a large family of bacterial toxins, are generally secreted as water-soluble monomers and can form oligomeric pores in membranes following proteolytic cleavage and interaction with cell surface receptors. Monalysi ...

American Society for Biochemistry and Molecular Biology2015

Molecular Modeling of Bacterial Nanomachineries

Matteo Thomas Degiacomi

Proteins have the ability to assemble in multimeric states to perform their specific biological function. Unfortunately, characterizing experimentally these structures at atomistic resolution is usually difficult. For this reason, in silico methodologies a ...

EPFL2012

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

Extending the aerolysin family: from bacteria to vertebrates

Françoise Gisou van der Goot Grunberg, Mircea Ioan Iacovache

A number of bacterial virulence factors have been observed to adopt structures similar to that of aerolysin, the principal toxin of Aeromonas species. However, a comprehensive description of architecture and structure of the aerolysin-like superfamily has ...

Public Library of Science2011

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

Folding and Structure of the Pore Forming Toxin Aerolysin

Mircea Ioan Iacovache

The first obstacle encountered by a bacterial pathogen once inside the host is the plasma membrane surrounding the target cells. Throughout evolution bacteria has acquired and maintained genes that upon stimulation express proteins capable of damaging the ...

EPFL2011

Assembly Mechanisms and Cellular Effects of Bacterial Pore-Forming Toxins

Mirko Bischofberger

The correct assembly of macromolecular protein complexes such as ribosomes or multisubunit membrane channels is essential for their function. Alterations in the process can lead to disease either by loss of function or by acquisition of toxic function. How ...

EPFL2011

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

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

Bacterial pore-forming toxins: the (w)hole story?

Françoise Gisou van der Goot Grunberg, Mirko Bischofberger, Rodrigo Manuel Gonzalez

Pore-forming toxins (PFTs) are the most common class of bacterial protein toxins and constitute important bacterial virulence factors. The mode of action of PFT is starting to be better understood. In contrast, little is known about the cellular response t ...

Birkhäuser-Verlag, Springer2008