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Release of Phospholipids from Bacterial Surface Structure and Liposomes by the Action of Complement

Osaka University Medical School, Osaka, Japan

Abstract

When an antibody-sensitized Escherichia coli B (parent strain) is treated with complement in the absence of lysozyme, free fatty acids (FFA) and lysophosphatidylethanolamine (LPE) are liberated into the lipid fraction of the surrounding medium in addition to a little amount of phosphatidylethanolamine (PE). However, when a phospholipase A-deficient mutant isolated from the parent strain is similarly treated, PE appears in the lipid fraction, but only traces of its degradation products are found. Therefore, most of the degradation of bacterial PE to FFA and LPE observed in the usual immune bactericidal reaction must be the result of the action of bacterial phospholipase A.

When liposomes which were made from a mixture of lipid fractions of sheep erythrocytes and of ¹⁴C-labeled E. coli are treated with complement, ¹⁴C-phospholipids are also liberated into the surrounding medium, but the degradation products (FFA and LPE) are not observed. Some of the liberated lipids seem to bind with some components of complement, giving a positive IA reaction, and are lighter than liposome particles on isopyenic sucrose density gradient centrifugation.