Chemical studies on damages of Escherichea coli by the immune bactericidal reaction. II. Release of phosphatidylethanolamine from a phospholipase A-deficient mutant of E. coli during the immune bactericidal reaction.
When an antibody-sensitized, phospholipase A-deficient mutant of Escherichia coli B/SM was treated with complement in the absence of lysozyme, bacterial phosphatidylethanolamine (PE) was liberated into the lipid fraction of the surrounding medium, but only traces of its degradation products were found in this fraction. Therefore, most of the degradation of bacterial PE to FFA and LPE observed in the usual immune bactericidal reaction (Inoue et al., 1974) must be the result of the action of bacterial phospholipase A which is activated or becomes accessible to its substrate on formation of lesions by complement. The mechanism of complement-mediated formation of membrane lesions is discussed on the basis of these results.
D002250:Carbon Radioisotopes; D005591:Chemical Fractionation; D002855:Chromatography, Thin Layer; D003165:Complement System Proteins; D004926:Escherichia coli / Q000032:analysis / Q000201:enzymology / Q000276:immunology*; D005230:Fatty Acids, Nonesterified / Q000032:analysis; D009154:Mutation; D010714:Phosphatidylethanolamines / Q000032:analysis*; D010740:Phospholipases / Q000302:isolation & purification / Q000378:metabolism
D002250:Carbon Radioisotopes; D005230:Fatty Acids, Nonesterified; D010714:Phosphatidylethanolamines; D003165:Complement System Proteins; D010740:Phospholipases