Isolation and properties of complement-resistant strains of Escherichia coli K-12.
Several strains that were resistant to the bactericidal action of antibody and complement were isolated from Escherichia coli K-12 W3110/SM by selecting them through the medium containing antiserum and complement. They can be agglutinated by antiserum against the parent strain and showed similar immune adherence reactivity to the parent when sensitized with this antiserum. Few differences were found in the compositions of phospholipids and proteins between both inner and outer membranes of these strains and those of the parent. However, there were fewer short-chain and more long-chain fatty acids in these strains than in the parent. It was also found that unsaturated fatty acide decreased and saturated and cyclopropanoic acids increased in phosphatidylethanolamine and phosphatidylglycerol in both inner and outer membranes of one of these strains when compared with those from the parent. Therefore, the resistance of these strains to the complement-mediated bactericidal action was considered to be due to the rigidity of their membrane structures which might repel the insertion of membrane-attack complement complex C5b-9, although they could fix the earlier complement components up to the step of the formation of C4b,2a,3b complex enzyme.
D001426:Bacterial Proteins / Q000032:analysis; D003165:Complement System Proteins; D004926:Escherichia coli / Q000032:analysis / Q000276:immunology / Q000302:isolation & purification*; D007104:Immune Adherence Reaction; D008563:Membrane Lipids / Q000032:analysis; D008565:Membrane Proteins; D010743:Phospholipids / Q000032:analysis
D001426:Bacterial Proteins; D008563:Membrane Lipids; D008565:Membrane Proteins; D010743:Phospholipids; D003165:Complement System Proteins