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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.
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 key Clostridium septicum virulence factor is a pore-forming toxin called alpha-toxin, though it is unrelated to the Clostridium perfringens alpha-toxin. Clostridium sordellii can also produce two major toxins: all known virulent strains produce the essential virulence factor lethal toxin (TcsL), and a number also produce haemorrhagic toxin ...
Currently, new methods of detecting bacterial toxins are being developed to better isolate and understand these toxins. Potential applications of toxin research include combating microbial virulence, the development of novel anticancer drugs and other medicines, and the use of toxins as tools in neurobiology and cellular biology .
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]
The reverse CAMP test is a method to identify Clostridium perfringens using β-hemolytic streptococci. The CAMP factor produced by S. agalactiae and the alpha toxin produced by C. perfringens act synergistically to produce enhanced hemolysis. Streaking these two organisms perpendicular to each other on a blood agar plate will yield a “bow tie ...
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.
This method, which is commonly used with Mueller–Hinton agar, is used by evenly seeding bacteria over a petri dish and applying an antibiotic treated disk to the top of the agar. By observing the ring formed around the disk formed due to the lack of bacterial growth, the zone of inhibition can be found, which is used to find the ...