Perfringolysin O as a useful tool to study human sperm physiology
Fertility 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
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Characterization of Listeria monocytogenes pathogenesis in a strain expressing perfringolysin O in place of listeriolysin O [PDF]
Infection 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
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Inhibition of the mitochondrial pyruvate carrier protects from excitotoxic neuronal death. [PDF]
, 2017 Glutamate is the dominant excitatory neurotransmitter in the brain, but under conditions of metabolic stress it can accumulate to excitotoxic levels.
Andreyev, Alexander Y +12 more
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R468A mutation in perfringolysin O destabilizes toxin structure and induces membrane fusion
Biochimica 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
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Microorganisms, 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
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Regulation of the Membrane Insertion and Conductance Activity of the Metamorphic Chloride Intracellular Channel Protein CLIC1 by Cholesterol [PDF]
, 2013 The Chloride Intracellular ion channel protein CLIC1 has the ability to spontaneously insert into lipid membranes from a soluble, globular state.
Alkhamici, H +8 more
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Listeriolysin O is necessary and sufficient to induce autophagy during Listeria monocytogenes infection. [PDF]
PLoS 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
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Structural basis of complement membrane attack complex formation [PDF]
, 2015 In response to complement activation, the membrane attack complex (MAC) assembles from fluid-phase proteins to form pores in lipid bilayers. MAC directly lyses pathogens by a ‘multi-hit’ mechanism; however, sublytic MAC pores on host cells activate ...
Bubeck, D +3 more
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Mechanisms of Action and Cell Death Associated with Clostridium perfringens Toxins. [PDF]
, 2018 Clostridium perfringens uses its large arsenal of protein toxins to produce histotoxic, neurologic and intestinal infections in humans and animals. The major toxins involved in diseases are alpha (CPA), beta (CPB), epsilon (ETX), iota (ITX), enterotoxin (
McClane, Bruce A +2 more
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Single-Molecule Imaging of Perfringolysin O Binding and Assembly on Model Membranes [PDF]
Biophysical 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
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