Results 41 to 50 of about 1,422 (145)

Capacity of listeriolysin O, streptolysin O, and perfringolysin O to mediate growth of Bacillus subtilis within mammalian cells [PDF]

open access: yesInfection and Immunity, 1992
The Listeria monocytogenes hemolysin listeriolysin O (LLO) plays a major role in mediating the escape of L. monocytogenes from a vacuolar compartment. In a previous report, it was shown that Bacillus subtilis expressing LLO could escape from a host vacuolar compartment and grow in the cytoplasm (J. Bielecki, P. Youngman, P. Connelly, and D. A. Portnoy,
D A, Portnoy   +3 more
openaire   +2 more sources

Interaction of Macrophages and Cholesterol-Dependent Cytolysins: The Impact on Immune Response and Cellular Survival

open access: yesToxins, 2020
Cholesterol-dependent cytolysins (CDCs) are key virulence factors involved in many lethal bacterial infections, including pneumonia, necrotizing soft tissue infections, bacterial meningitis, and miscarriage.
Roshan Thapa   +2 more
doaj   +1 more source

Bottom‐Up Coacervate‐Based Artificial Cells: Integrating Cellular Hallmarks into Complex Life‐Like Systems

open access: yesAngewandte Chemie, Volume 138, Issue 22, 25 May 2026.
Current interest in artificial cell research underscores its potential to deepen our understanding of life's fundamental processes. This review highlights advances in bottom‐up coacervate‐based artificial cell engineering via combined integration of cellular hallmarks.
Arjan Hazegh Nikroo   +3 more
wiley   +2 more sources

Contribution of Histidine Residues to Oligomerization of θ-Toxin (Perfringolysin O), a Cholesterol-Binding Cytolysin [PDF]

open access: yesBioscience, Biotechnology, and Biochemistry, 1999
Theta-toxin (perfringolysin O) modified by diethyl pyrocarbonate, a histidine-specific reagent, lost its hemolytic activity. The modified toxin retains the activities of binding to and insertion into cholesterol-containing membranes but lacks the ability to form oligomers.
NAKAMURA, Megumi   +3 more
openaire   +2 more sources

Immunoinformatic analysis of the whole proteome for vaccine design: An application to Clostridium perfringens

open access: yesFrontiers in Immunology, 2022
Clostridium perfringens is a dangerous bacterium and known biological warfare weapon associated with several diseases, whose lethal toxins can produce necrosis in humans. However, there is no safe and fully effective vaccine against C.
Luis F. Soto   +7 more
doaj   +1 more source

Immunoelectron Microscopic Localization of Cholesterol Using Biotinylated and Non-cytolytic Perfringolysin O [PDF]

open access: yesJournal of Histochemistry & Cytochemistry, 2002
We used a proteolytically modified and biotinylated derivative of the cholesterol-binding θ-toxin (perfringolysin O) to localize cholesterol-rich membranes in cryosections of cultured human lymphoblastoid cells (RN) by electron microscopy. We developed a fixation and immunolabeling procedure to improve the preservation of membranes and minimize the ...
Wiebke, Möbius   +8 more
openaire   +2 more sources

Streptococcus pyogenes NAD+-Glycohydrolase Reduces Skeletal Muscle βNAD+ Levels Independently of Streptolysin O

open access: yesMicroorganisms, 2022
Necrotizing soft tissue infections caused by Streptococcus pyogenes (group A streptococcus [GAS]) are characterized by rapid and extensive necrosis of fascia and muscle.
Eric R. McIndoo   +7 more
doaj   +1 more source

Listeriolysin O is necessary and sufficient to induce autophagy during Listeria monocytogenes infection. [PDF]

open access: yesPLoS ONE, 2010
Recent studies have suggested that autophagy is utilized by cells as a protective mechanism against Listeria monocytogenes infection.However we find autophagy has no measurable role in vacuolar escape and intracellular growth in primary cultured bone ...
Nicole Meyer-Morse   +7 more
doaj   +1 more source

An upstream regulatory sequence stimulates expression of the perfringolysin O gene of Clostridium perfringens [PDF]

open access: yesInfection and Immunity, 1991
The structural gene for perfringolysin O (pfoA), a thiol-activated hemolysin of Clostridium perfringens, was cloned into Escherichia coli JM109 on a 4.6-kilobase (kb) EcoRI-NdeI fragment which contained the 1.7-kb pfoA gene and an upstream 2.9-kb region. An E.
T, Shimizu   +3 more
openaire   +2 more sources

The foodborne toxin perfringolysin O targets mitochondrial destabilization for NLRP3 inflammasome activation

open access: yesFood Science and Human Wellness
Foodborne pathogens are the leading causes of human diseases that result in hundreds of thousands of deaths annually. Clostridium perfringens is a notorious foodborne pathogen of global significance that is known to produce a large repertoire of toxic ...
Xinyi Wang   +4 more
doaj   +1 more source

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