Results 31 to 40 of about 1,422 (145)

Pathogenic Characterization of Clostridium perfringens Strains Isolated From Patients With Massive Intravascular Hemolysis

open access: yesFrontiers in Microbiology, 2021
Sepsis caused by Clostridium perfringens infection is rare but often fatal. The most serious complication leading to poor prognosis is massive intravascular hemolysis (MIH).
Ai Suzaki   +7 more
doaj   +1 more source

Lethal effects of Clostridium perfringens epsilon toxin are potentiated by alpha and perfringolysin-O toxins in a mouse model [PDF]

open access: yesVeterinary Microbiology, 2008
Mariano Enrique Fernández-Miyakawa   +2 more
exaly   +2 more sources

The projection structure of Perfringolysin O (Clostridium perfringens θ‐toxin) [PDF]

open access: yesFEBS Letters, 1993
The cytolysin Perfringolysin O was applied to lipid layers and the obtained ring‐shaped oligomers analyzed by electron microscopy and image processing. The final result shows the periodic repeat of 2.4 nm along the outer rim of the ring. The asymmetric protein unit, corresponding to one monomer, spans the ring from the convex to the concave surface. It
Olofsson, Anders   +2 more
openaire   +2 more sources

Eukaryotic Cell Permeabilisation to Identify New Putative Chlamydial Type III Secretion System Effectors Secreted within Host Cell Cytoplasm

open access: yesMicroorganisms, 2020
Chlamydia trachomatis and Waddlia chondrophila are strict intracellular bacteria belonging to the Chlamydiales order. C. trachomatis is the most frequent bacterial cause of genital and ocular infections whereas W.
Carole Kebbi-Beghdadi   +3 more
doaj   +1 more source

Characterization of Listeria monocytogenes pathogenesis in a strain expressing perfringolysin O in place of listeriolysin O [PDF]

open access: yesInfection and Immunity, 1994
Listeriolysin O (LLO) is a pore-forming cytolysin that enables Listeria monocytogenes to escape from a host cell vacuole. The structural gene for the related cytolysin perfringolysin O (pfo) was cloned downstream from the promoter for hly, the gene encoding LLO, both on a plasmid and on the L. monocytogenes chromosome. Both strains secreted active PFO,
S, Jones, D A, Portnoy
openaire   +2 more sources

Use of an EZ-Tn5-based random mutagenesis system to identify a novel toxin regulatory locus in Clostridium perfringens strain 13. [PDF]

open access: yesPLoS ONE, 2009
BACKGROUND:Although useful for probing bacterial pathogenesis and physiology, current random mutagenesis systems suffer limitations for studying the toxin-producing bacterium Clostridium perfringens.
Jorge E Vidal   +3 more
doaj   +1 more source

Molecular and cellular basis of microvascular perfusion deficits induced by Clostridium perfringens and Clostridium septicum.

open access: yesPLoS Pathogens, 2008
Reduced tissue perfusion leading to tissue ischemia is a central component of the pathogenesis of myonecrosis caused by Clostridium perfringens. The C.
Michael J Hickey   +9 more
doaj   +1 more source

Selective binding of perfringolysin O derivative to cholesterol-rich membrane microdomains (rafts) [PDF]

open access: yesProceedings of the National Academy of Sciences, 2001
There is increasing evidence that sphingolipid- and cholesterol-rich microdomains (rafts) exist in the plasma membrane. Specific proteins assemble in these membrane domains and play a role in signal transduction and many other cellular events.
A A, Waheed   +8 more
openaire   +2 more sources

Decreasing Transmembrane Segment Length Greatly Decreases Perfringolysin O Pore Size [PDF]

open access: yesThe Journal of Membrane Biology, 2015
Perfringolysin O (PFO) is a transmembrane (TM) β-barrel protein that inserts into mammalian cell membranes. Once inserted into membranes, PFO assembles into pore-forming oligomers containing 30-50 PFO monomers. These form a pore of up to 300 Å, far exceeding the size of most other proteinaceous pores.
Qingqing, Lin   +3 more
openaire   +2 more sources

Single molecule tracking the uncoupling of assembly and membrane insertion in Perfringolysin O [PDF]

open access: yes, 2021
Abstract We exploit single-molecule tracking and optical single channel recording in droplet interface bilayers to resolve the assembly pathway and pore-formation of the archetypical cholesterol-dependent cytolysin nanopore, Perfringolysin O. We follow the stoichiometry and diffusion of Perfringolysin O complexes during assembly with 60
Michael J T Senior   +5 more
openaire   +1 more source

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