scholarly journals Inflammasome Activation Induced by Perfringolysin O of Clostridium perfringens and Its Involvement in the Progression of Gas Gangrene

2019 ◽  
Vol 10 ◽  
Author(s):  
Kiyonobu Yamamura ◽  
Hiroshi Ashida ◽  
Tokuju Okano ◽  
Ryo Kinoshita-Daitoku ◽  
Shiho Suzuki ◽  
...  
Keyword(s):  
Clostridium Perfringens ◽  
Gas Gangrene ◽  
Inflammasome Activation ◽  
Perfringolysin O

scholarly journals Perfringolysin O Expression in Clostridium perfringens Is Independent of the Upstream pfoR Gene

2002 ◽  
Vol 184 (7) ◽  
pp. 2034-2038 ◽  
Author(s):  
Milena M. Awad ◽  
Julian I. Rood
Keyword(s):  
Escherichia Coli ◽  
Homologous Recombination ◽  
Gene Product ◽  
Structural Gene ◽  
Clostridium Perfringens ◽  
Deletion Mutant ◽  
Gas Gangrene ◽  
Alpha Toxin ◽  
Clostridial Myonecrosis ◽  
Perfringolysin O

ABSTRACT The pathogenesis of Clostridium perfringens-mediated gas gangrene or clostridial myonecrosis involves the extracellular toxins alpha-toxin and perfringolysin O. Previous studies (T. Shimizu, A. Okabe, J. Minami, and H. Hayashi, Infect. Immun. 59:137-142, 1991) carried out with Escherichia coli suggested that the perfringolysin O structural gene, pfoA, was positively regulated by the product of the upstream pfoR gene. In an attempt to confirm this hypothesis in C. perfringens, a pfoR-pfoA deletion mutant was complemented with isogenic pfoA+ shuttle plasmids that varied only in their ability to encode an intact pfoR gene. No difference in the ability to produce perfringolysin O was observed for C. perfringens strains carrying these plasmids. In addition, chromosomal pfoR mutants were constructed by homologous recombination in C. perfringens. Again no difference in perfringolysin O activity was observed. Since it was not possible to alter perfringolysin O expression by mutation of pfoR, it was concluded that the pfoR gene product is unlikely to have a role in the regulation of pfoA expression in C. perfringens.

scholarly journals Amentoflavone Attenuates Clostridium perfringens Gas Gangrene by Targeting Alpha-Toxin and Perfringolysin O

2020 ◽  
Vol 11 ◽  
Author(s):  
Shui Liu ◽  
Xiaofeng Yang ◽  
Hong Zhang ◽  
Jian Zhang ◽  
Yonglin Zhou ◽  
...  
Keyword(s):  
Clostridium Perfringens ◽  
Gas Gangrene ◽  
Alpha Toxin ◽  
Perfringolysin O

scholarly journals Synergistic Effects of Alpha-Toxin and Perfringolysin O in Clostridium perfringens-Mediated Gas Gangrene

2001 ◽  
Vol 69 (12) ◽  
pp. 7904-7910 ◽  
Author(s):  
Milena M. Awad ◽  
Darren M. Ellemor ◽  
Richard L. Boyd ◽  
John J. Emmins ◽  
Julian I. Rood
Keyword(s):  
Structural Gene ◽  
Clostridium Perfringens ◽  
Synergistic Effects ◽  
Gas Gangrene ◽  
Alpha Toxin ◽  
Coagulative Necrosis ◽  
Clostridial Myonecrosis ◽  
Perfringolysin O ◽  
Vascular Disruption ◽  
Rapid Spread

ABSTRACT To examine the synergistic effects of alpha-toxin and perfringolysin O in clostridial myonecrosis, homologous recombination was used to construct an alpha-toxin deficient derivative of a perfringolysin O mutant of Clostridium perfringens. The subsequent strain was complemented with separate plasmids that carried the alpha-toxin structural gene (plc), the perfringolysin O gene (pfoA), or both toxin genes, and the resultant isogenic strains were examined in a mouse myonecrosis model. Synergistic effects were clearly observed in these experiments. Infection with the control strain, which did not produce either toxin, resulted in very minimal gross pathological changes, whereas the isogenic strain that was reconstituted for both toxins produced a pathology that was clearly more severe than when alpha-toxin alone was reconstituted. These changes were most apparent in the rapid spread of the disease, the gross pathology of the footpad and in the rate at which the mice had to be euthanatized for ethical reasons. Elimination of both alpha-toxin and perfringolysin O production removed most of the histopathological features typical of clostridial myonecrosis. These effects were restored when the mutant was complemented with the alpha-toxin structural gene, but reconstituting only perfringolysin O activity produced vastly different results, with regions of coagulative necrosis, apparently enhanced by vascular disruption, being observed. Reconstitution of both alpha-toxin and perfringolysin O activity produced histopathology most similar to that observed with the alpha-toxin reconstituted strain. The spreading of myonecrosis was very rapid in these tissues, and coagulative necrosis appeared to be restricted to the lumen of the blood vessels. The results of these virulence experiments clearly support the hypothesis that alpha-toxin and perfringolysin O have a synergistic effect in the pathology of gas gangrene.

scholarly journals Effects of Clostridium perfringens Alpha-Toxin (PLC) and Perfringolysin O (PFO) on Cytotoxicity to Macrophages, on Escape from the Phagosomes of Macrophages, and on Persistence of C. perfringens in Host Tissues

2004 ◽  
Vol 72 (9) ◽  
pp. 5204-5215 ◽  
Author(s):  
David K. O'Brien ◽  
Stephen B. Melville
Keyword(s):  
Clostridium Perfringens ◽  
Peritoneal Macrophages ◽  
Gas Gangrene ◽  
Polymorphonuclear Cells ◽  
Alpha Toxin ◽  
Phagocytic Cells ◽  
Mouse Muscle ◽  
Perfringolysin O ◽  
Mouse Peritoneal Macrophages ◽  
Host Tissues

ABSTRACT Clostridium perfringens is the most common cause of clostridial myonecrosis (gas gangrene). Polymorphonuclear cells (PMNs) appear to play only a minor role in preventing the onset of myonecrosis in a mouse animal model of the disease (unpublished results). However, the importance of macrophages in the host defense against C. perfringens infections is still unknown. Two membrane-active toxins produced by the anaerobic C. perfringens, alpha-toxin (PLC) and perfringolysin O (PFO), are thought to be important in the pathogenesis of gas gangrene and the lack of phagocytic cells at the site of infection. Therefore, C. perfringens mutants lacking PFO and PLC were examined for their relative cytotoxic effects on macrophages, their ability to escape the phagosome of macrophages, and their persistence in mouse tissues. C. perfringens survival in the presence of mouse peritoneal macrophages was dependent on both PFO and PLC. PFO was shown to be the primary mediator of C. perfringens-dependent cytotoxicity to macrophages. Escape of C. perfringens cells from phagosomes of macrophage-like J774-33 cells and mouse peritoneal macrophages was mediated by either PFO or PLC, although PFO seemed to play a more important role in escape from the phagosome in peritoneal macrophages. At lethal doses (109) of bacteria only PLC was necessary for the onset of myonecrosis, while at sublethal doses (106) both PFO and PLC were necessary for survival of C. perfringens in mouse muscle tissue. These results suggest PFO-mediated cytotoxicity toward macrophages and the ability to escape macrophage phagosomes may be important factors in the ability of C. perfringens to survive in host tissues when bacterial numbers are low relative to those of phagocytic cells, e.g., early in an infection.

Clostridium perfringens intestinal gas gangrene in a preterm newborn

2008 ◽  
Vol 212 (S 1) ◽  
Author(s):  
CA Hanke ◽  
R Hentschel ◽  
R Berner ◽  
A Superti-Furga ◽  
KD Rückauer ◽  
...  
Keyword(s):  
Clostridium Perfringens ◽  
Gas Gangrene ◽  
Preterm Newborn ◽  
Intestinal Gas

scholarly journals Identification of residues critical for toxicity in Clostridium perfringens phospholipase C, the key toxin in gas gangrene

2000 ◽  
Vol 267 (16) ◽  
pp. 5191-5197 ◽  
Author(s):  
Alberto Alape-Girón ◽  
Marietta Flores-Díaz ◽  
Isabelle Guillouard ◽  
Claire E. Naylor ◽  
Richard W. Titball ◽  
...  
Keyword(s):  
Phospholipase C ◽  
Clostridium Perfringens ◽  
Gas Gangrene

scholarly journals Perfringolysin O: The Underrated Clostridium perfringens Toxin?

Toxins ◽  
2015 ◽  
Vol 7 (5) ◽  
pp. 1702-1721 ◽  
Author(s):  
Stefanie Verherstraeten ◽  
Evy Goossens ◽  
Bonnie Valgaeren ◽  
Bart Pardon ◽  
Leen Timbermont ◽  
...  
Keyword(s):  
Clostridium Perfringens ◽  
Perfringolysin O

Crystallization and preliminary X-ray diffraction studies of θ-toxin (perfringolysin O), a pore-forming cytolysin of Clostridium perfringens

1996 ◽  
Vol 168 (1-4) ◽  
pp. 288-291 ◽  
Author(s):  
Mitsuaki Sugahara ◽  
Naoko Sekino-Suzuki ◽  
Yoshiko Ohno-Iwashita ◽  
Kunio Miki
Keyword(s):  
Clostridium Perfringens ◽  
X Ray Diffraction ◽  
X Ray ◽  
Perfringolysin O
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