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The deactivated exotoxins are called toxoids and they are not harmful to somatic cells. 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.
A toxoid is an inactivated toxin (usually an exotoxin) whose toxicity has been suppressed either by chemical or heat treatment, while other properties, typically immunogenicity, are maintained. [1] Toxins are secreted by bacteria, whereas toxoids are altered form of toxins; toxoids are not secreted by bacteria.
Diphtheria toxin is an exotoxin secreted mainly by Corynebacterium diphtheriae but also by Corynebacterium ulcerans and Corynebacterium pseudotuberculosis, the pathogenic bacterium that causes diphtheria. The toxin gene is encoded by a prophage [annotation 1] called corynephage β.
Since not all mycotoxins can be bound to such agents, the latest approach to mycotoxin control is mycotoxin deactivation. By means of enzymes ( esterase , de-epoxidase ), yeast ( Trichosporon mycotoxinvorans ), or bacterial strains ( Eubacterium BBSH 797 developed by Biomin ), mycotoxins can be reduced during pre-harvesting contamination.
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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.
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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.