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

FEBS Letters

Loos, Michael¹  Latsch, Maria¹  Möllerfeld, Jörg²  Ringsdorf, Helmut² 

[1] Institute of Medical Microbiology, Johannes Gutenberg-University, Augustusplatz/Hochhaus, D-6500 Mainz, FRG;Institute of Organic Chemistry, Johannes Gutenberg-University, Becherweg 18, D-6500 Mainz, FRG

关键词: C1q;    Macrophage;    Outer membrane protein;    Liposome;    Black lipid membrane;   

DOI  :  10.1016/0014-5793(90)80542-Q

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown