Studies on the interaction of C1q,a subcomponent of the first component of complement, with porins from Salmonella minnesota incorporated into artificial membranes

Abstract

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.