Interaction between lipopolysaccharide (LPS), LPS-binding protein (LBP), and planar membranes |
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Authors: | Gutsmann T Haberer N Carroll S F Seydel U Wiese A |
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Affiliation: | Research Center Borstel, Center for Medicine and Biosciences, Division of Biophysics, Germany. |
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Abstract: | The mechanism of interaction of the lipopolysaccharide (LPS)-binding protein, LBP, with differently composed symmetric and asymmetric planar lipid bilayers was investigated in electrical measurements (membrane current, potential, capacitance). From a change of the inner membrane potential difference, binding of LBP to membranes was deduced. After addition of LBP to one side of the membrane, binding of anti-LBP antibodies and LPS to LBP on both sides of the bilayer was observed. Effects resulting from an interaction of anti-LBP antiserum with membrane-bound LBP depend on the side of addition of the antiserum, indicating a directed intercalation of LBP into the membrane. Addition of LPS to the same side as LBP may induce a change of the conformation of LBP or its orientation in the membrane. Based on these observations, we propose that LBP intercalates in a directed orientation into negatively-charged membranes and assumes a transmembrane configuration. Moreover, pre-incubated complexes of LPS and LBP do not interact with membranes. These experiments show that reconstituted planar membranes are a suitable tool for investigations of the interaction of non pore-forming proteins that are involved in signal transduction. |
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