A5061893236- Vibrio bacteria research studies
- Escherichia coli research studies
- Bacterial biofilms and quorum sensing
- Bacterial Genetics and Biotechnology
- Lipid Membrane Structure and Behavior
- Legionella and Acanthamoeba research
- Caching and Content Delivery
- Cell death mechanisms and regulation
- Cancer Research and Treatments
- Yersinia bacterium, plague, ectoparasites research
- Autophagy in Disease and Therapy
- Advanced Data Storage Technologies
- Endoplasmic Reticulum Stress and Disease
- Child Nutrition and Water Access
- Distributed and Parallel Computing Systems
Umeå University
2021-2025
Significance Vibrio cholerae , responsible for outbreaks of cholera disease, is a highly motile organism by virtue single flagellum. We describe how the flagellum facilitates secretion three V. proteins encoded hitherto-unrecognized genomic island. The MakA/B/E can form tripartite toxin that lyses erythrocytes and cytotoxic to cultured human cells. A structural basis cytolytic activity Mak was obtained X-ray crystallography. Flagellum-facilitated ensuring spatially coordinated delivery...
Vibrio cholerae is a noninvasive intestinal pathogen extensively studied as the causative agent of human disease cholera. Our recent work identified MakA potent virulence factor V . in both Caenorhabditis elegans and zebrafish, prompting us to investigate potential contribution pathogenesis also mammalian hosts. In this study, we demonstrate that protein could induce autophagy cytotoxicity target cells. addition, observed phosphatidic acid (PA)-mediated MakA-binding host cell plasma...
The α-pore-forming toxins (α-PFTs) from pathogenic bacteria damage host cell membranes by pore formation. We demonstrate a remarkable, hitherto unknown mechanism an α-PFT protein Vibrio cholerae. As part of the MakA/B/E tripartite toxin, MakA is involved in membrane formation similar to other α-PFTs. In contrast, isolation induces tube-like structures acidic endosomal compartments epithelial cells vitro. present study unravels dynamics tubular growth, which occurs pH-, lipid-, and...
A prevailing action of the Type VI secretion system (T6SS) in several Gram-negative bacterial species is inter-bacterial competition. In past years, many effectors T6SS were identified different and their involvement interactions described. However, possible defence mechanisms against attack among prey bacteria not well clarified yet. Escherichia coli was assessed for susceptibility to T6SS-mediated killing by Vibrio cholerae. TheT6SS-mediated assays performed absence or presence protease...
Abstract Recently, we demonstrated that a novel bacterial cytotoxin, the protein MakA which is released by Vibrio cholerae , virulence factor, causing killing of Caenorhabditis elegans when worms are grazing on bacteria. Studies with mammalian cell cultures in vitro indicated could affect eukaryotic signalling pathways involved lipid biosynthesis. treatment colon cancer cells caused inhibition growth and loss viability. These findings prompted us to investigate possible be targets...
Pathogenic serotypes of Vibrio cholerae, transmitted through contaminated water and food, are responsible for outbreaks cholera, an acute diarrheal disease. While the cholera toxin is primary virulence factor, V. cholerae also expresses other factors, such as tripartite MakABE that secreted via bacterial flagellum. These three proteins co-expressed with two accessory proteins, MakC MakD, whose functions remain unknown. Here, we present crystal structures revealing they similar in both...
ABSTRACT The protein MakA was discovered as a motility-associated secreted toxin from Vibrio cholerae , Here, we show that is part of gene cluster encoding four additional proteins: MakB, MakC, MakD and MakE. MakA, MakB MakE proteins were readily detected in culture supernatants wild type V. whereas secretion very much reduced flagellum deficient mutant. Crystal structures revealed structural relationship to superfamily bacterial pore-forming proteins. Cloning expression MakA/B/E Escherichia...
Abstract Many pathogenic bacteria produce protein toxins that target and perturb host cell membranes. The secreted α-pore-forming (α-PFTs) cause membrane damage via pore formation. This study demonstrates a remarkable, hitherto unknown mechanism by an α-PFT from Vibrio cholerae . As part of the MakA/B/E tripartite toxin, MakA is involved in formation similar to other α-PFTs. In contrast, alone induces tube-like structures acidic lysosomal compartment. vitro studies unravel dynamics tubular...