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The binding of the exotoxin and antibody forms an antigen-antibody interaction and the exotoxins are targeted for destruction by the immune system. If this interaction does not happen, the exotoxins bind to the exotoxin receptors that are on the cell surface and causes death of the host cell by inhibiting protein synthesis. This figure also ...
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 enterotoxin is a protein exotoxin released by a microorganism that targets the intestines. [1] They can be chromosomally or plasmid encoded. [2] They are heat labile (> 60 °C), of low molecular weight and water-soluble.
It is slightly unusual in that it combines the A and B parts in the same protein chain: the pre-toxin is cleaved into two parts, then the two parts are joined by a disulfide bond. [5] 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 ...
Exotoxin activity can be separated into specific cytotoxic activity or broad cytotoxic activity based on whether the toxin targets specific cell types or various cell types and tissues, respectively. Lethal toxins refers to the group of toxins that are the obvious agents responsible for death associated with the infection.
A potent three-protein virulence factor produced by Bacillus anthracis, called anthrax toxin, plays a key role in anthrax pathogenesis. Exotoxins are extremely immunogenic and trigger the humoral response (antibodies target the toxin). Exotoxins are also produced by some fungi as a competitive resource.
Diphtheria toxin is a single polypeptide chain of 535 amino acids consisting of two subunits linked by disulfide bridges, known as an A-B toxin.Binding to the cell surface of the B subunit (the less stable of the two subunits) allows the A subunit (the more stable part of the protein) to penetrate the host cell.
Pertussis toxin is an exotoxin with six subunits (named S1 through S5—each complex contains two copies of S4). [12] [13] The subunits are arranged in A-B structure: the A component is enzymatically active and is formed from the S1 subunit, while the B component is the receptor-binding portion and is made up of subunits S2–S5. [13]