Clostridium perfringens α toxin

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Phospholipase C
Phospholipase C
according to PDB  1CA1
other names

Alpha toxin, hemolysin, lecithinase, phosphatidylcholine choline phosphohydrolase

Available structural data : PDB  1KHO

Mass / length primary structure 398 amino acids , 45,598 Da
Identifier
External IDs
Enzyme classification
EC, category 3.1.4.3
Orthologue ( Clostridium perfringens )
Entrez 29569865
UniProt Q9RF12


PubMed search 29569865

Clostridium perfringens α-toxin is an enzyme from the group of phospholipases from Clostridium perfringens and a microbial exotoxin .

properties

The C. perfringens α toxin is a phospholipase C and binds zinc ions . It is the main virulence factor of C. perfringens . It acts as a hemolysin in eukaryotes . As phospholipase C , it hydrolyzes phosphatidylcholine and sphingomyelin , which lyses the cell membrane . The released diacylglycerol acts as a second messenger and activates the arachidonic acid - the signal and protein kinase C , thereby more phospholipases are activated in sequence and the cell membrane is further degraded. The N -terminal region of amino acids 1-250 contains the enzyme activity , while the C -terminal region of amino acids 251-370 mediates binding to the cell membrane. α-toxin is structurally related to the phospholipases from Bacillus cereus , Clostridium bifermentans and Listeria monocytogenes . The C -terminal region is also distantly related to the pancreatic lipase , the soybean lipoxygenase and synaptotagmin I related.

Phospholipase C catalyzes the following reaction:

Phosphatidylcholine + H 2 O → 1,2-diacyl-sn-glycerol + phosphocholine

Applications

Clostridium perfringens α-toxin is being studied as an antigen in vaccines against C. perfringens infections .

Web links

Individual evidence

  1. ↑ MM Awad, AE Bryant, DL Stevens, JI Rood: Virulence studies on chromosomal alpha-toxin and theta-toxin mutants constructed by allelic exchange provide genetic evidence for the essential role of alpha-toxin in Clostridium perfringens-mediated gas gangrene. In: Molecular microbiology. Volume 15, Number 2, January 1995, pp. 191-202, PMID 7746141 .
  2. ↑ M. Oda, Y. Terao, J. Sakurai, M. Nagahama: Membrane-Binding Mechanism of Clostridium perfringens Alpha-Toxin. In: Toxins. Volume 7, number 12, December 2015, pp. 5268-5275, doi : 10.3390 / toxins7124880 , PMID 26633512 , PMC 4690130 (free full text).
  3. ↑ J. Sakurai, M. Nagahama, M. Oda: Clostridium perfringens alpha-toxin: characterization and mode of action. In: Journal of biochemistry. Volume 136, Number 5, November 2004, pp. 569-574, doi : 10.1093 / jb / mvh161 , PMID 15632295 .
  4. ↑ CE Naylor, JT Eaton, A. Howells, N. Justin, DS Moss, RW Titball, AK Basak: Structure of the key toxin in gas gangrene. In: Nature structural biology. Volume 5, Number 8, August 1998, pp. 738-746, doi : 10.1038 / 1447 , PMID 9699639 .
  5. ↑ M. Nagahama: Vaccines against Clostridium perfringens alpha-toxin. In: Current pharmaceutical biotechnology. Volume 14, Number 10, 2013, pp. 913-917, PMID 24372250 .