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PMID:21704605
| Citation |
Urbina, P, Collado, MI, Alonso, A, Goñi, FM, Flores-Díaz, M, Alape-Girón, A, Ruysschaert, JM and Lensink, MF (2011) Unexpected wide substrate specificity of C. perfringens α-toxin phospholipase C. Biochim. Biophys. Acta 1808:2618-27 |
|---|---|
| Abstract |
Clostridium perfringens phospholipase C (CpPLC), also called α-toxin, is the main virulence factor for gas gangrene in humans. The lipase activity serves the bacterium to generate lipid signals in the host eukaryotic cell, and ultimately to degrade the host cell membranes. Several previous reports indicated that CpPLC was specific for phosphatidylcholine and sphingomyelin. Molecular docking studies described in this paper predict favorable interactions of the CpPLC active site with other phospholipids, e.g. phosphatidylethanolamine, phosphatidylinositol and, to a lesser extent, phosphatidylglycerol. On the basis of these predictions, we have performed experimental studies showing α-toxin to degrade all the phospholipids mentioned above. The molecular docking data also provide an explanation for the observed lower activity of CpPCL on sphingomyelin as compared to the glycerophospholipids. |
| Links |
PubMed Online version:10.1016/j.bbamem.2011.06.008 |
| Keywords |
Bacterial Toxins/metabolism; Clostridium perfringens/enzymology; Substrate Specificity; Type C Phospholipases/metabolism |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0016787: hydrolase activity |
ECO:0000314: |
F |
See figure 3 of paper. |
complete | ||||
|
enables |
GO:0016787: hydrolase activity |
ECO:0000314: direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
See also
References
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