Studies on the interaction of C1q, a subcomponent of the first component of complement, with porins from Salmonella minnesota incorporated into artificial membranes.
Purified outer membrane proteins (OMP) of Salmonella minnesota, Re-form, were incorporated into liposomes. These induced in macrophages a chemiluminescence signal identical to that of the intact Re-form. This signal was abolished by preincubation of porin-containing liposomes with purified C1q. Incorporation of isolated OMP into black lipid membranes (BLM) resulted in channel-formation which could not be inhibited by isolated C1q. Additionally, incubation of OMP-containing liposomes with BLM resulted in pore-formation within the BLM. This was amplified when lipid A was present within the liposomes. Preincubation of OMP-containing liposomes with purified C1q abolished pore-formation within the BLM.
Institute of Medical Microbiology, Johannes Gutenberg-University, Mainz, FRG.
M
M
Latsch
J
J
Möllerfeld
H
H
Ringsdorf
M
M
Loos
D000818:Animals; D001425:Bacterial Outer Membrane Proteins / Q000302:isolation & purification / Q000378:metabolism*; D002478:Cells, Cultured; D002784:Cholesterol; D015922:Complement C1q / Q000302:isolation & purification / Q000378:metabolism*; D004553:Electric Conductivity; D006801:Humans; D007473:Ion Channels / Q000502:physiology*; D007700:Kinetics; D008051:Lipid Bilayers; D049449:Luminescence; D008264:Macrophages / Q000502:physiology; D008564:Membrane Potentials; D008567:Membranes, Artificial; D051379:Mice; D008807:Mice, Inbred BALB C; D010713:Phosphatidylcholines; D018272:Porins; D012475:Salmonella / Q000378:metabolism*
D001425:Bacterial Outer Membrane Proteins; D007473:Ion Channels; D008051:Lipid Bilayers; D008567:Membranes, Artificial; D010713:Phosphatidylcholines; D018272:Porins; D015922:Complement C1q; D002784:Cholesterol