Microbial toxin

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Microbial toxins are toxins produced by micro-organisms, including bacteria and fungi. Microbial toxins promote infection and disease by directly damaging host tissues and by disabling the immune system. Some bacterial toxins, such as Botulinum neurotoxins, are the most potent natural toxins known. However, microbial toxins also have important uses in medical science and research. 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.[1]

Bacterial toxin[edit]

Bacteria generate toxins[2] which can be classified as either exotoxins or endotoxins. Exotoxins are generated and actively secreted; endotoxins remain part of the bacteria. Usually, an endotoxin is part of the bacterial outer membrane, and it is not released until the bacterium is killed by the immune system. The body's response to an endotoxin can involve severe inflammation. In general, the inflammation process is usually considered beneficial to the infected host, but if the reaction is severe enough, it can lead to sepsis.

Some bacterial toxins can be used in the treatment of tumors.[3]

Toxinosis is pathogenesis caused by the bacterial toxin alone, not necessarily involving bacterial infection (e.g. when the bacteria have died, but have already produced toxin, which are ingested). It can be caused by Staphylococcus aureus toxins, for example.[4]

Botulinum neurotoxin[edit]

Botulinum neurotoxins (BoNTs) are the causative agents of the deadly food poisoning disease botulism, and could pose a major biological warfare threat due to their extreme toxicity and ease of production. They also serve as powerful tools to treat an ever expanding list of medical conditions.[5]

Tetanus toxin[edit]

Clostridium tetani produces tetanus toxin (TeNT protein), which leads to a fatal condition known as tetanus in many vertebrates (including humans) and invertebrates.

Staphylococcal toxins[edit]

Immune evasion proteins from Staphylococcus aureus have a significant conservation of protein structures and a range of activities that are all directed at the two key elements of host immunity, complement and neutrophils. These secreted virulence factors assist the bacterium in surviving immune response mechanisms.[6]

Viral toxin[edit]

There is only one viral toxin that has been described so far: NSP4 from rotavirus. It inhibits the microtubule-mediated secretory pathway and alters cytoskeleton organization in polarized epithelial cells. It has been identified as the viral enterotoxin based on the observation that the protein caused diarrhea when administered intraperitoneally or intra-ileally in infant mice in an age-dependent manner.[7] NSP4 can induce aqueous secretion in the gastrointestinal tract of neonatal mice through activation of an age- and Ca2+-dependent plasma membrane anion permeability.[8]

See also[edit]

References[edit]

  1. ^ Proft T, ed. (2009). Microbial Toxins: Current Research and Future Trends. Caister Academic Press. ISBN 978-1-904455-44-8.[page needed]
  2. ^ "bacterial toxins" at Dorland's Medical Dictionary
  3. ^ "Definition of bacterial toxin". NCI Dictionary of Cancer Terms. Retrieved 2008-12-13.
  4. ^ Bruce F, Harvey RP, Champe PC (2007). Lippincott's Illustrated Reviews: Microbiology (Lippincott's Illustrated Reviews Series). Hagerstown, MD: Lippincott Williams & Wilkins. p. 348. ISBN 978-0-7817-8215-9.
  5. ^ Kukreja R, Singh BR (2009). "Botulinum Neurotoxins: Structure and Mechanism of Action". Microbial Toxins: Current Research and Future Trends. Caister Academic Press. ISBN 978-1-904455-44-8.[page needed]
  6. ^ Langley RJ, Thomas Proft T, Fraser JD (2009). "Staphylococcal Immune Evasion Toxins". In Proft T. Microbial Toxins: Current Research and Future Trends. Caister Academic Press. pp. 147–66. ISBN 978-1-904455-44-8.
  7. ^ Jagannath MR, Kesavulu MM, Deepa R, Sastri PN, Kumar SS, Suguna K, Rao CD (January 2006). "N- and C-terminal cooperation in rotavirus enterotoxin: novel mechanism of modulation of the properties of a multifunctional protein by a structurally and functionally overlapping conformational domain". Journal of Virology. 80 (1): 412–25. doi:10.1128/JVI.80.1.412-425.2006. PMC 1317517. PMID 16352566.
  8. ^ Borghan MA, Mori Y, El-Mahmoudy AB, Ito N, Sugiyama M, Takewaki T, Minamoto N (July 2007). "Induction of nitric oxide synthase by rotavirus enterotoxin NSP4: implication for rotavirus pathogenicity". The Journal of General Virology. 88 (Pt 7): 2064–72. doi:10.1099/vir.0.82618-0. PMID 17554041.