Bacillus cereus contains a monomeric phospholipase C (PLC) of 245 amino-acid residues. Although PLC prefers to acton phosphatidylcholine, it also shows weak catalytic activity with sphingomyelin and phosphatidylinositol. Sequence studies have shown the protein to be similar both to alpha toxin fromClostridium perfringens and Clostridium bifermentans, a phospholipase C involved in haemolysis and cell rupture, and to lecithinase from Listeria monocytogenes, which aids cell-to-cell spread by breaking down the 2-membrane vacuoles that surround the bacterium during transfer.
Each of these proteins is a zinc-dependent enzyme, binding 3 zinc ions per molecule. The enzymes catalyse the conversion of phosphatidylcholine and water to 1,2-diacylglycerol and choline phosphate.
In Bacillus cereus, there are nine residues known to be involved in binding the zinc ions: 5 His, 2 Asp, 1 Glu and 1 Trp. These residues are all conserved in the Clostridium alpha-toxin.
Research reports on clostridium therapy from Muroran Institute of Technology, Department of Applied Chemistry provide new insights.
Jul 30, 2008; Data detailed in 'Complete dechlorination of tetrachloroethylene by use of an anaerobic Clostridium bifermentans DPH-1 and...