Role of caseinase from Aeromonas salmonicida in activation of hemolysin.
Mutants of the bacterial fish pathogen Aeromonas salmonicida selected for inability to digest casein concomitantly lost hemolytic activity against horse erythrocytes under certain conditions. Mixtures of wild-type with mutant culture supernatants indicated that mutants produce an inactive precursor of a hemolysin which was activated by autogenous caseinase and, with less efficiency, by other serine proteases. Selective inhibition or repression of caseinase production in the wild-type strain also resulted in the production of an inactive precursor of a hemolysin. The precursor of hemolysin was also activated by a serum factor which appeared to exert its maximum effect at the bacterial surface or after entry into the bacterial cell. These results could affect the interpretation of studies evaluating the role of individual extracellular products in the pathogenesis of A. salmonicida infections.
D000333:Aeromonas / Q000201:enzymology* / Q000472:pathogenicity; D000818:Animals; D004794:Enzyme Repression; D005399:Fishes; D006460:Hemolysin Proteins / Q000378:metabolism*; D008666:Metalloendopeptidases; D009154:Mutation; D010447:Peptide Hydrolases / Q000494:pharmacology / Q000502:physiology*
D006460:Hemolysin Proteins; D010447:Peptide Hydrolases; D008666:Metalloendopeptidases; C030895:caseinase