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A novel bicomponent hemolysin from Bacillus cereus.

D J Beecher1, J D MacMillan

  • 1Department of Biochemistry and Microbiology, Cook College, Rutgers University, New Brunswick, New Jersey 08903.

Infection and Immunity
|July 1, 1990
PubMed
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Bacillus cereus enterotoxin exhibits hemolytic activity, mediated by two distinct protein components (B and L). This novel hemolysin displays a unique delayed lysis pattern in blood agar assays.

Area of Science:

  • Microbiology
  • Protein Biochemistry

Background:

  • Bacillus cereus produces a multicomponent diarrheal enterotoxin.
  • Hemolytic activity was previously considered a contaminant of enterotoxin preparations.

Purpose of the Study:

  • To investigate the nature of hemolytic activity associated with Bacillus cereus enterotoxin.
  • To determine if hemolysis is an intrinsic property of the enterotoxin.

Main Methods:

  • Purification using Sephadex isoelectric focusing (IEF) and fast protein liquid chromatography (Superose 12; Mono-Q).
  • Gel diffusion assays in blood agar.
  • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), isoelectric focusing (IEF), and Western blot analysis.

Main Results:

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  • Hemolytic activity was removed by purification but restored upon recombination of fractions, indicating it's an enterotoxin property.
  • A unique delayed hemolysis ring pattern was observed in gel diffusion assays.
  • The hemolysin comprises two distinct proteins: component B (cell alteration) and component L (cell lysis).
  • Hemolysin BL shares properties with the enterotoxin and is distinct from cereolysin and cereolysin AB.

Conclusions:

  • Hemolysis is an intrinsic property of the Bacillus cereus diarrheal enterotoxin.
  • The hemolysin (hemolysin BL) is composed of two synergistic protein components.
  • Hemolysin BL exhibits novel characteristics, including a delayed lysis mechanism.