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The Pseudomonas exotoxin (or exotoxin A) is an exotoxin produced by Pseudomonas aeruginosa. [1] Vibrio cholerae produces a similar protein called the Cholix toxin 2] It inhibits elongation factor-2. It does so by ADP-ribosylation of EF2 using NAD+. This then causes the elongation of polypeptides to cease.
An exotoxin is a toxin secreted by bacteria. [1] An exotoxin can cause damage to the host by destroying cells or disrupting normal cellular metabolism. They are highly potent and can cause major damage to the host. Exotoxins may be secreted, or, similar to endotoxins, may be released during lysis of the cell.
The exotoxin A of Pseudomonas aeruginosa is another example of an AB toxin that targets the eEF2. The "A" part is structually similar to the DT "A" part; the "B" part is located to the N-terminal direction to the "A" part, unlike DT.
Pseudomonas aeruginosa in Petri dish. Pseudomonas aeruginosa is a common encapsulated, Gram-negative, aerobic–facultatively anaerobic, rod-shaped bacterium that can cause disease in plants and animals, including humans.
The tcdA and tcdB genes are situated on the Clostridioides difficile chromosome in a 19.6-kb pathogenicity locus (PaLoc) found only in toxigenic strains of C. difficile.Non toxigenic strains contain a 127 base pair fragment replacing the PaLoc. [8]
This toxin is a 38 kDa fragment of Pseudomonas exotoxin A. Hairy cell leukemia (HCL) is a rare, slow-growing cancer of the blood in which the bone marrow makes too many B cells (lymphocytes), a type of white blood cell that fights infection. [4] HCL is named after these extra B cells which look “hairy” when viewed under a microscope. [4]
Listeriolysin O toxin is an exotoxin produced by Listeria monocytogenes and is associated with foodborne systemic illness and meningitis. [7] Listeriolysin O toxin is classified as a pore-forming toxin that targets host cholesterol cells, inserting a pore into the host cell plasma membrane and permanently disabling cellular functioning. [3]
SpeB was identified in 1919 as an ectoenzyme secreted by certain strains of streptococci. [11] It was originally studied as two separate toxins, streptococcal pyrogenic exotoxin B and streptococcal cysteine proteinase, until it was shown that both proteins were encoded by the speB gene and that the attributed pyrogenic activities were due to contamination by SpeA and SpeC.