How do anti toxins work?
10323278#2
The antitoxin is generally less stable than the toxin due to its degradation by proteases already present in the cell. For example, in the ccdAB proteic addiction module, the "Lon" protease  degrades the antitoxin, but also serves many unrelated proteolytic roles, such as degrading oxidated mitochondrial products. This may indicate that the development of these addiction molecules "co-opted" existing cell utilities.
The antitoxin in proteic addiction modules functions by binding directly to the toxin and preventing its mode of action. Once the antitoxin has bound to the toxin, the toxin prevents the proteases normally responsible for degrading antitoxin to do so, maintaining the neutralization of that individual toxin molecule.
Addiction module
729694#0
An antitoxin is an antibody with the ability to neutralize a specific toxin. Antitoxins are produced by certain animals, plants, and bacteria. Although they are most effective in neutralizing toxins, they can kill bacteria and other microorganisms. Antitoxins are made within organisms, but can be injected into other organisms, including humans. This procedure involves injecting an animal with a safe amount of a particular toxin. Then, the animal’s body makes the antitoxin needed to neutralize the toxin. Later, the blood is withdrawn from the animal. When the antitoxin is obtained from the blood, it is purified and injected into a human or other animal, inducing passive immunity. To prevent serum sickness, it is often best to use antitoxin generated from the same species (e.g. use human antitoxin to treat humans).
Antitoxin
28335087#7
It has been proposed that chromosomal homologues of plasmid toxin-antitoxin systems may serve as anti-addiction modules, which would allow progeny to lose a plasmid without suffering the effects of the toxin it encodes. For example, a chromosomal copy of "the ccdA" antitoxin encoded in the chromosome of "Erwinia chrysanthemi" is able to neutralize the "ccdB" toxin encoded on the F plasmid and thus, prevent toxin activation when such a plasmid is lost. Similarly, the "ataR" antitoxin encoded on the chromosome of is able neutralize the "ataT" toxin encoded on plasmids found in other enterohemorragic "E. coli".
Toxin-antitoxin system
10021492#7
Anti-venoms are commercially prepared antibodies to toxins in animal bites. They are specific for each bite. There are several anti-venoms commercially available in Brazil, which have been shown to be effective in controlling the spread of necrosis in rabbits. When administered immediately, they can almost entirely neutralize any ill effects. If too much time is allowed to pass, the treatment becomes ineffective. Most victims do not seek medical attention within the first twelve hours of being bitten, and these anti-venoms are largely ineffective after this point. Because of this, anti-venoms are not being developed more widely. They have, however, been proven to be very effective if administered in a timely manner and could be utilized in Brazil as a legitimate technique.
Loxoscelism
28335087#1
Toxin-antitoxin systems are typically classified according to how the antitoxin neutralises the toxin. In a type I toxin-antitoxin system, the translation of messenger RNA (mRNA) that encodes the toxin is inhibited by the binding of a small non-coding RNA antitoxin that binds the toxin mRNA. The toxic protein in a type II system is inhibited post-translationally by the binding of an antitoxin protein. Type III toxin-antitoxin systems consist of a small RNA that binds directly to the toxin protein and inhibits its activity. There are also types IV-VI, which are less common. Toxin-antitoxin genes are often inherited through horizontal gene transfer and are associated with pathogenic bacteria, having been found on plasmids conferring antibiotic resistance and virulence.
Toxin-antitoxin system
635170#12
While resistance to tetrodotoxin is beneficial in acquiring newt prey, there are also costs associated with it as well. Consuming the toxin can lead to reduced speed and sometimes no movement for extended periods of time, along with impaired thermoregulation. The anti-predator display that this species uses demonstrates the idea of an "arms race" between different species and their anti-predator displays. Along the entire geographical interaction of "T. granulosa" and "T. sirtalis", there are patches that correspond to strong coevolution as well as weak or absent coevolution. Populations of "T. sirtalis" that do not live in areas that contain "T. granulosa" contain the lowest amount of tetrodotoxin resistance, while those that do live in the same area contain the highest levels of tetrodotoxin resistance. In populations where tetrodotoxin is absent in "T. granulosa", resistance in "T. sirtalis" is selected against because the mutation causes lower average population fitness. This helps maintain polymorphism within garter snake populations.
Common garter snake
28335087#6
Another theory states that chromosomal toxin-antitoxin systems are designed to be bacteriostatic rather than bactericidal. RelE, for example, is a global inhibitor of translation, is induced during nutrient stress. By shutting down translation under stress, it could reduce the chance of starvation by lowering the cell's nutrient requirements. However, it was shown that several toxin-antitoxin systems, including "relBE", do not give any competitive advantage under any stress condition.
Toxin-antitoxin system
1260420#30
Many prey animals, and to defend against seed predation also seeds of plants, make use of poisonous chemicals for self-defence. These may be concentrated in surface structures such as spines or glands, giving an attacker a taste of the chemicals before it actually bites or swallows the prey animal: many toxins are bitter-tasting. A last-ditch defence is for the animal's flesh itself to be toxic, as in the puffer fish, danaid butterflies and burnet moths. Many insects acquire toxins from their food plants; "Danaus" caterpillars accumulate toxic cardenolides from milkweeds (Asclepiadaceae).
Anti-predator adaptation
37411479#1
ParD is a plasmid anti-toxin that forms a ribbon-helix-helix DNA binding structure. It stabilises plasmids by inhibiting ParE toxicity in cells that express ParD and ParE. ParD forms a dimer and also regulates its own promoter (parDE). As with CcdB the toxin target is DNA gyrase. Induction of ParE toxin results in inhibition of cell division but not cell growth.
ParDE type II toxin-antitoxin system
28335087#5
"mazEF", a toxin-antitoxin locus found in "E. coli" and other bacteria, was proposed to induce programmed cell death in response to starvation, specifically a lack of amino acids. This would release the cell's contents for absorption by neighbouring cells, potentially preventing the death of close relatives, and thereby increasing the inclusive fitness of the cell that perished. This would be an example of altruism and how bacterial colonies could resemble multicellular organisms. However, the ""mazEF"-mediated PCD" has largely been refuted by several studies.
Toxin-antitoxin system
6948252#5
Several drugs are used to treat DES, including nitroglycerin, hyoscine butylbromide, calcium channel blockers, hydralazine, and anti-anxiety medications. Acid suppression therapy, such as proton pump inhibitors, are often the first line therapy. Botulinum toxin, which inhibits acetylcholine release from nerve endings, injected above the lower esophageal sphincter may also be used in the treatment of DES. Small studies have suggested benefit from endoscopic balloon dilation in certain patients, but all of the above have a low percentage of success in treating the condition; whilst the treatments work in some sufferers, it does not work for everyone. In extremely rare cases, surgery may be considered.
Diffuse esophageal spasm