Results 41 to 50 of about 1,388 (159)

Repurposing rabeprazole sodium as an anti-Clostridium perfringensdrug by inhibiting perfringolysin O

open access: yesJournal 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
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

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

Perfringolysin O as a useful tool to study human sperm physiology

open access: yesFertility and Sterility, 2013
To evaluate perfringolysin O, a cholesterol-dependent pore-forming cytolysin, as a tool to study several aspects of human sperm physiology.Prospective study.Basic research laboratory.Human semen samples with normal parameters obtained from healthy donors.Interaction of recombinant perfringolysin O with human spermatozoa.Assessment of perfringolysin O ...
Pocognoni, Cristián Adrián   +4 more
openaire   +3 more sources

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

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

R468A mutation in perfringolysin O destabilizes toxin structure and induces membrane fusion

open access: yesBiochimica et Biophysica Acta (BBA) - Biomembranes, 2017
Perfringolysin O (PFO) belongs to the family of cholesterol-dependent cytolysins. Upon binding to a cholesterol-containing membrane, PFO undergoes a series of structural changes that result in the formation of a β-barrel pore and cell lysis. Recognition and binding to cholesterol are mediated by the D4 domain, one of four domains of PFO.
Magdalena, Kulma   +5 more
openaire   +2 more sources

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

Single-Molecule Imaging of Perfringolysin O Binding and Assembly on Model Membranes [PDF]

open access: yesBiophysical Journal, 2016
Perfringolysin O (PFO) is the archetypical pore-forming toxin in the cholesterol-dependent cytolysin (CDC) family, which is implicated in major infections ranging from food poisoning to pneumonia and meningitis. Like other CDCs, transmembrane pores are formed when PFO monomers bind to cholesterol-containing membranes and oligomerize into larger (30-50 ...
Senior, Michael J.   +4 more
openaire   +1 more source

Single molecule compression reveals intra-protein forces drive cytotoxin pore formation

open access: yeseLife, 2015
Perfringolysin O (PFO) is a prototypical member of a large family of pore-forming proteins that undergo a significant reduction in height during the transition from the membrane-assembled prepore to the membrane-inserted pore. Here, we show that targeted
Daniel M Czajkowsky   +3 more
doaj   +1 more source

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