Search results
Results from the WOW.Com Content Network
The type A toxin of C. perfringens, also known as the CPA is responsible for food poisoning. [44] Clostridium perfringens is the most common bacterial agent for gas gangrene. [45] Gas gangrene is induced by α-toxin that embeds itself into the plasma membrane of cells and disrupts normal cellular function by altering membrane structure. [8]
The C terminal domain shows similarity with non-bacterial enzymes such as pancreatic lipase, soybean lipoxygenase, and synaptotagmin I. [4] The alpha toxin is a zinc metallophospholipase, requiring zinc for activation. First, the toxin binds to a binding site on the cell surface.
Clostridium perfringens alpha toxin (α-toxin) C. perfringens alpha toxin is widely associated with gas gangrene as it is its main virulence factor whilst invading its host. Alpha-toxin causes excessive platelet aggregation which blocks blood vessels and deprives the vital organs of oxygen supply. This creates an acidic, oxygen-deficient ...
Roughly 10 million cases of foodborne illness each year in the U.S. are caused by six pathogens — salmonella, listeria monocytogenes, campylobacter, clostridium perfringens, shiga toxin ...
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]
Clostridium perfringens is an anaerobic, gram-positive bacteria that is often found in the large and small intestines of humans and other animals. Clostridium perfringens has the ability to reproduce quickly producing toxins relating to the cause of diseases.
It can be produced by Clostridium perfringens, Staphylococcus aureus, Pseudomonas aeruginosa or Listeria monocytogenes. C. perfringens alpha toxin (lecithinase) causes myonecrosis and hemolysis. The lecithinase of S. aureus is used in detection of coagulase-positive strains, because of high link between lecithinase activity and coagulase activity.
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.