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Clostridium perfringens (formerly known as C. welchii, or Bacillus welchii) is a Gram-positive, bacillus (rod-shaped), anaerobic, spore-forming pathogenic bacterium of the genus Clostridium. [1] [2] C. perfringens is ever-present in nature and can be found as a normal component of decaying vegetation, marine sediment, the intestinal tract of ...
Clostridium perfringens alpha toxin is a toxin produced by the bacterium Clostridium perfringens (C. perfringens) and is responsible for gas gangrene and myonecrosis in infected tissues. The toxin also possesses hemolytic activity.
Because C. perfringens beta toxin shares homology with S. aureus pore-forming alpha toxin, it was hypothesized that beta toxin acts in a similar way. Upon investigation, it was found that C. perfringens beta toxin forms cation-selective pores in cell membranes [4] of 1.6–1.8 nm [5] and results in swelling and lysis in HL60 cells. [6]
Species of the class Clostridia are often but not always Gram-positive (see Halanaerobium) and have the ability to form spores. [1] Studies show they are not a monophyletic group, and their relationships are not entirely certain. Currently, most are placed in a single order called Clostridiales, but this is not a natural group and is likely to ...
Clostridium is a genus of anaerobic, Gram-positive bacteria.Species of Clostridium inhabit soils and the intestinal tracts of animals, including humans. [1] This genus includes several significant human pathogens, including the causative agents of botulism and tetanus.
The Clostridiaceae are a family of the bacterial class Clostridia, and contain the genus Clostridium.. The family Clostridiaceae (scientific name) defined by the taxonomic outline of Bergey's Manual of Systematic Bacteriology contains as its core the genus Clostridium (sensu stricto), as well as Acetivibrio, Acidaminobacter, Alkaliphilus, Anaerobacter, Caloramator, Caloranaerobacter ...
Clostridium enterotoxin is a nine-stranded beta sheet sandwich in shape. It has been determined that it is very similar to other spore-forming bacteria. [1] The binding site is between beta sheets eight and nine. This allows the human claudin-3,4,6,7,8 and 14 to bind but not 1,2,5, and 10.
Tetanolysin belongs to a family of protein toxins known as thiol-activated cytolysins, which bind to cholesterol. [1] It is related to streptolysin O and the θ-toxin of Clostridium perfringens. [2] Cytolysins form pores in the cytoplasmic membrane that allows for the passage of ions and other molecules into the cell.