Clostridium perfringens α-Toxin

Phospholipase C
Phospholipase C
nach PDB 1CA1
Andere Namen

Alpha-toxin, Hämolysin, Lecithinase, Phosphatidylcholin-Cholinphosphohydrolase

Vorhandene Strukturdaten: PDB 1KHO

Masse/Länge Primärstruktur 398 Aminosäuren, 45.598 Da
Bezeichner
Externe IDs
Enzymklassifikation
EC, Kategorie 3.1.4.3
Orthologe (Clostridium perfringens)
Entrez 29569865
UniProt Q9RF12


PubMed-Suche 29569865

Clostridium perfringens α-Toxin ist ein Enzym aus der Gruppe der Phospholipasen von Clostridium perfringens und ein mikrobielles Exotoxin.

Eigenschaften

Das α-Toxin von C. perfringens ist eine Phospholipase C und bindet Zinkionen. Es ist der Haupt-Virulenzfaktor von C. perfringens.[1] Es wirkt bei Eukaryoten als Hämolysin. Als Phospholipase C hydrolysiert es Phosphatidylcholin und Sphingomyelin, wodurch es zur Lyse der Zellmembran kommt. Das freigesetzte Diacylglycerol wirkt als sekundärer Botenstoff und aktiviert den Arachidonsäure-Signalweg und die Proteinkinase C, wodurch in Folge weitere Phospholipasen aktiviert werden und die Zellmembran weiter abgebaut wird. Der N-terminale Bereich der Aminosäuren 1–250 enthält die Enzymaktivität, während der C-terminale Bereich der Aminosäuren 251–370 die Bindung an die Zellmembran vermittelt.[2] α-Toxin ist strukturell mit den Phospholipasen aus Bacillus cereus, Clostridium bifermentans und Listeria monocytogenes verwandt.[3] Der C-terminale Bereich ist zudem entfernter mit der pankreatischen Lipase, der Sojabohnen-Lipoxygenase und Synaptotagmin I verwandt.[4]

Die Phospholipase C katalysiert folgende Reaktion:

Phosphatidylcholin + H2O → 1,2-Diacyl-sn-glycerol + Phosphocholin

Anwendungen

Clostridium perfringens α-Toxin wird als Antigen in Impfstoffen gegen Infektionen mit C. perfringens untersucht.[5]

Einzelnachweise

  1. ↑ M. M. Awad, A. E. Bryant, D. L. Stevens, J. I. 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. Band 15, Nummer 2, Januar 1995, S. 191–202, PMID 7746141.
  2. ↑ M. Oda, Y. Terao, J. Sakurai, M. Nagahama: Membrane-Binding Mechanism of Clostridium perfringens Alpha-Toxin. In: Toxins. Band 7, Nummer 12, Dezember 2015, S. 5268–5275, doi:10.3390/toxins7124880, PMID 26633512, PMC 4690130 (freier Volltext).
  3. ↑ J. Sakurai, M. Nagahama, M. Oda: Clostridium perfringens alpha-toxin: characterization and mode of action. In: Journal of biochemistry. Band 136, Nummer 5, November 2004, S. 569–574, doi:10.1093/jb/mvh161, PMID 15632295.
  4. ↑ C. E. Naylor, J. T. Eaton, A. Howells, N. Justin, D. S. Moss, R. W. Titball, A. K. Basak: Structure of the key toxin in gas gangrene. In: Nature structural biology. Band 5, Nummer 8, August 1998, S. 738–746, doi:10.1038/1447, PMID 9699639.
  5. ↑ M. Nagahama: Vaccines against Clostridium perfringens alpha-toxin. In: Current pharmaceutical biotechnology. Band 14, Nummer 10, 2013, S. 913–917, PMID 24372250.

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