Interaction of human complement proteins with serum-sensitive and serum-resistant strains of Escherichia coli.
Exposure of serum-susceptible Escherichia coli strains to lethal concns of lysozyme-free human serum resulted in stable binding of complement components to the outer membrane (OM), but not to the cytoplasmic membrane (CM). The short prekilling phase of the reaction was accompanied by binding of C3b; loss of viability was immediately preceeded by stable deposition onto the OM of the component proteins of the membrane attack complex. During the early stages of the active killing phase, bound monomeric C9 could be resolved into two distinct bands on SDS-polyacrylamide gels. Serum exposure lead to a progressive loss of CM recoverability, which appeared to result from partial degradation of CM phospholipids. In contrast, exposure of a resistant E, coli strain to human serum resulted in little change in the membrane profile and very little stable deposition of terminal complement components onto the OM.
D001770:Blood Bactericidal Activity; D002458:Cell Fractionation; D002462:Cell Membrane / Q000276:immunology / Q000378:metabolism; D002499:Centrifugation, Density Gradient; D015938:Complement Membrane Attack Complex; D003165:Complement System Proteins / Q000378:metabolism*; D003593:Cytoplasm / Q000276:immunology; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000276:immunology*; D006801:Humans; D010743:Phospholipids / Q000378:metabolism
D015938:Complement Membrane Attack Complex; D010743:Phospholipids; D003165:Complement System Proteins