The synergistic necrohemorrhagic action of Clostridium perfringens perfringolysin and alpha toxin in the bovine intestine and against bovine endothelial cells [PDF]
, 2013 Bovine necrohemorrhagic enteritis is a major cause of mortality in veal calves. Clostridium perfringens is considered as the causative agent, but there has been controversy on the toxins responsible for the disease.
Deprez, Piet +10 more
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Clostridium perfringens α-toxin action facilitates the Perfringolysin O-cholesterol interaction [PDF]
Biophysical Journal, 2009 Clostridium perfringens is a Gram-positive bacterium that causes gangrene and gastrointestinal disease in humans. These pathologies are mediated by potent extracellular protein toxins, particularly alpha-toxin (phospholipase C or PLC) and theta-toxin (perfringolysin O or PFO).
Moe, Paul C., Heuck, Alejandro P.
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Immunoelectron Microscopic Localization of Cholesterol Using Biotinylated and Non-cytolytic Perfringolysin O [PDF]
Journal 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
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Structural insights into Clostridium perfringens delta toxin pore formation [PDF]
, 2013 Clostridium perfringens Delta toxin is one of the three hemolysin-like proteins produced by C. perfringens type C and possibly type B strains. One of the others, NetB, has been shown to be the major cause of Avian Nectrotic Enteritis, which following the
AGW Leslie +57 more
core +5 more sources
The membrane attack complex, perforin and cholesterol-dependent cytolysin superfamily of pore-forming proteins [PDF]
, 2016 The membrane attack complex and perforin proteins (MACPFs) and bacterial cholesterol-dependent cytolysins (CDCs) are two branches of a large and diverse superfamily of pore-forming proteins that function in immunity and pathogenesis.
Blackman +75 more
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Toxins, 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
Stepwise visualization of membrane pore formation by suilysin, a bacterial cholesterol-dependent cytolysin [PDF]
, 2014 Membrane attack complex/perforin/cholesterol-dependent cytolysin (MACPF/CDC) proteins constitute a major superfamily of pore-forming proteins that act as bacterial virulence factors and effectors in immune defence.
Baker +42 more
core +3 more sources
Repurposing rabeprazole sodium as an anti-Clostridium perfringensdrug by inhibiting perfringolysin O
Journal of Applied Microbiology, 2023 AbstractAimsClostridium perfringens infections affect food safety, human health, and the development of the poultry feed industry. Anti-virulence is an alternative strategy to develop new drug. Perfringolysin O (PFO) is an exotoxin of C. perfringens that has been demonstrated to play critical roles in the pathogenesis of this organism, promising it an ...
Guizhen, Wang +8 more
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Capacity of listeriolysin O, streptolysin O, and perfringolysin O to mediate growth of Bacillus subtilis within mammalian cells [PDF]
Infection 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
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Frontiers 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