Binding of Bacterial Lipopolysaccharide to Histocompatibility-2-CompIex Proteins of Mouse Lymphocytes

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Abstract
The membrane binding sites for lipopolysaccharide (LPS) were isolated by affinity chromatography of the solubilized membranes prepared from 125I-labeled mouse B[bone marrow-derived]-cells and T[thymus-derived]-cells on an affinity adsorbent prepared by coupling Salmonella minnesota R595 LPS to activated Sepharose 4B. The membrane proteins bound to the affinity adsorbent and eluted with 1.0% Triton X-100 were analyzed according to their mobility on polyacrylamide gel electrophoresis in sodium dodecylsulfate. These membrane proteins were further identified by immunoprecipitation with specific antisera. Immunoglobulins [Ig], possibly IgM and IgD, were identified in the eluate from the B-cell membranes. The histocompatibility-2-complex proteins (H-2D, H-2K and Ia [immune response associated] antigens) were also binding sites for LPS on B-cells and T-cells.