C9-mediated killing of bacterial cells by transferred C5b-8 complexes: transferred C5b-9 complexes are nonbactericidal
نویسندگان
چکیده
منابع مشابه
Bacterial killing by complement. C9-mediated killing in the absence of C5b-8.
The ability of serum complement to kill Gram-negative bacteria requires assembly of the membrane attack complex (MAC) on the cell surface. The molecular events that lead to cell killing after MAC assembly are unknown. We have investigated the effect of C9 on bacterial survival in the presence and absence of its receptor, the C5b-8 complex, on the outer membrane. A fluorescence assay of the memb...
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The binding of C9 at 0 and 37 degrees C to viable Escherichia coli K-12 cells carrying C5b-8 complexes was quantified. At low temperature, limited average binding of only 1 to 1.4 molecules of C9 per C8 molecule occurred, whereas 6 to 8 C9 molecules were bound per C8 molecule at 37 degrees C. Despite incorporation of C9 into C5b-9 complexes at 0 degrees C, these terminal complexes caused no los...
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Rational drug design depends on the knowledge of the three-dimensional (3D) structure of complexes between proteins and lead compounds of low molecular weight. A novel nuclear magnetic resonance (NMR) spectroscopy strategy based on the paramagnetic effects from lanthanide ions allows the rapid determination of the 3D structure of a small ligand molecule bound to its protein target in solution a...
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The membrane attack complex of complement (MAC) can induce reversible changes in cell membrane permeability resulting in significant but transient intracellular ionic changes in the absence of cell lysis. Because ion fluxes and cytosolic ionic changes are integral steps in the signaling cascade initiated when growth factors bind to their receptors, we hypothesized that the MAC-induced reversibl...
متن کاملGlutathione-catalyzed disulfide-linking of C9 in the membrane attack complex of complement.
The membrane attack complex of complement (the dimeric C5b-9 complex) is a multimolecular assemblage of five proteins (C5b, C6, C7, C8, and C9) which are held together by noncovalent forces. We found that C9 molecules in the complex can be covalently crosslinked (disulfide-linked) by glutathione. In this experiment, the tetramolecular C5b-8 complex bound to phospholipid vesicles was first prepa...
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ژورنال
عنوان ژورنال: Infection and Immunity
سال: 1994
ISSN: 0019-9567,1098-5522
DOI: 10.1128/iai.62.10.4101-4106.1994