Biochemical and immunological properties of the C-terminal domain of the alpha-toxin of Clostridium perfringens.
The C-terminal domain of the alpha-toxin (cpa247-370) of Clostridium perfringens has been expressed in Escherichia coli and purified. Antiserum raised against cpa247-370 reacted in an identical manner to anti-alpha-toxin serum when used to map epitopes in the C-terminal domain, suggesting that cpa247-370 was immunologically and structurally identical to this region in the alpha-toxin. The isolated cpa247-370 was devoid of sphingomyelinase activity or haemolytic activity and was not cytotoxic for mouse lymphocytes. Haemolytic activity was detected when cpa247-370 was tested with the N-terminal domain of the alpha-toxin (cpa1-249), confirming that cpa247-370 confers haemolytic properties on the phospholipase C activity of the alpha-toxin. Haemolytic activity was not detected if cpa247-370 was tested with the Bacillus cereus phosphatidylcholine phospholipase C, nor if cpa1-249 and cpa247-370 were incubated sequentially with erythrocytes.
Titball
R W
RW
Chemical and Biological Defence Establishment, Porton Down, Salisbury, Wiltshire, UK.
Fearn
A M
AM
Williamson
E D
ED
D000818:Animals; D001427:Bacterial Toxins / Q000737:chemistry* / Q000276:immunology*; D002135:Calcium-Binding Proteins; D003001:Cloning, Molecular; D003016:Clostridium perfringens / Q000201:enzymology*; D003601:Cytotoxicity Tests, Immunologic; D004269:DNA, Bacterial / Q000032:analysis*; D006461:Hemolysis; D051379:Mice; D011993:Recombinant Fusion Proteins; D010738:Type C Phospholipases / Q000737:chemistry / Q000276:immunology
D001427:Bacterial Toxins; D002135:Calcium-Binding Proteins; D004269:DNA, Bacterial; D011993:Recombinant Fusion Proteins; D010738:Type C Phospholipases; C040649:alpha toxin, Clostridium perfringens