Clostridial toxins. (October 2009)
- Record Type:
- Journal Article
- Title:
- Clostridial toxins. (October 2009)
- Main Title:
- Clostridial toxins
- Authors:
- Popoff, Michel R
Bouvet, Philippe - Abstract:
- Clostridia produce the highest number of toxins of any type of bacteria and are involved in severe diseases in humans and other animals. Most of the clostridial toxins are pore-forming toxins responsible for gangrenes and gastrointestinal diseases. Among them, perfringolysin has been extensively studied and it is the paradigm of the cholesterol-dependent cytolysins, whereas Clostridium perfringens εε-toxin and Clostridium septicum αα-toxin, which are related to aerolysin, are the prototypes of clostridial toxins that form small pores. Other toxins active on the cell surface possess an enzymatic activity, such as phospholipase C and collagenase, and are involved in the degradation of specific cell-membrane or extracellular-matrix components. Three groups of clostridial toxins have the ability to enter cells: large clostridial glucosylating toxins, binary toxins and neurotoxins. The binary and large clostridial glucosylating toxins alter the actin cytoskeleton by enzymatically modifying the actin monomers and the regulatory proteins from the Rho family, respectively. Clostridial neurotoxins proteolyse key components of neuroexocytosis. Botulinum neurotoxins inhibit neurotransmission at neuromuscular junctions, whereas tetanus toxin targets the inhibitory interneurons of the CNS. The high potency of clostridial toxins results from their specific targets, which have an essential cellular function, and from the type of modification that they induce. In addition, clostridialClostridia produce the highest number of toxins of any type of bacteria and are involved in severe diseases in humans and other animals. Most of the clostridial toxins are pore-forming toxins responsible for gangrenes and gastrointestinal diseases. Among them, perfringolysin has been extensively studied and it is the paradigm of the cholesterol-dependent cytolysins, whereas Clostridium perfringens εε-toxin and Clostridium septicum αα-toxin, which are related to aerolysin, are the prototypes of clostridial toxins that form small pores. Other toxins active on the cell surface possess an enzymatic activity, such as phospholipase C and collagenase, and are involved in the degradation of specific cell-membrane or extracellular-matrix components. Three groups of clostridial toxins have the ability to enter cells: large clostridial glucosylating toxins, binary toxins and neurotoxins. The binary and large clostridial glucosylating toxins alter the actin cytoskeleton by enzymatically modifying the actin monomers and the regulatory proteins from the Rho family, respectively. Clostridial neurotoxins proteolyse key components of neuroexocytosis. Botulinum neurotoxins inhibit neurotransmission at neuromuscular junctions, whereas tetanus toxin targets the inhibitory interneurons of the CNS. The high potency of clostridial toxins results from their specific targets, which have an essential cellular function, and from the type of modification that they induce. In addition, clostridial toxins are useful pharmacological and biological tools. … (more)
- Is Part Of:
- Future microbiology. Volume 4:Number 8(2009)
- Journal:
- Future microbiology
- Issue:
- Volume 4:Number 8(2009)
- Issue Display:
- Volume 4, Issue 8 (2009)
- Year:
- 2009
- Volume:
- 4
- Issue:
- 8
- Issue Sort Value:
- 2009-0004-0008-0000
- Page Start:
- 1021
- Page End:
- 1064
- Publication Date:
- 2009-10
- Subjects:
- botulism -- Clostridium -- enteritis -- gangrene -- neurotoxin -- pore-forming toxin -- tetanus -- toxin
Microbiology -- Research -- Periodicals
616.9041 - Journal URLs:
- http://www.futuremedicine.com/loi/fmb ↗
http://www.futuremedicine.com/ ↗ - DOI:
- 10.2217/fmb.09.72 ↗
- Languages:
- English
- ISSNs:
- 1746-0913
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4060.604000
British Library DSC - BLDSS-3PM
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- 16408.xml