| Literature DB >> 10377104 |
M Jepson1, A Howells, H L Bullifent, B Bolgiano, D Crane, J Miller, J Holley, P Jayasekera, R W Titball.
Abstract
The phospholipases C of C. perfringens (alpha-toxin) and C. bifermentans (Cbp) show >50% amino acid homology but differ in their hemolytic and toxic properties. We report here the purification and characterisation of alpha-toxin and Cbp. The phospholipase C activity of alpha-toxin and Cbp was similar when tested with phosphatidylcholine in egg yolk or in liposomes. However, the hemolytic activity of alpha-toxin was more than 100-fold that of Cbp. To investigate whether differences in the carboxy-terminal domains of these proteins were responsible for differences in the hemolytic and toxic properties, a hybrid protein (NbiCalpha) was constructed comprising the N domain of Cbp and the C domain of alpha-toxin. The hemolytic activity of NbiCalpha was 10-fold that of Cbp, and the hybrid enzyme was toxic. These results confirm that the C-terminal domain of these proteins confers different properties on the enzymatically active N-terminal domain of these proteins.Entities:
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Year: 1999 PMID： 10377104 PMCID： PMC116509
Source DB: PubMed Journal: Infect Immun ISSN： 0019-9567 Impact factor: 3.441