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      Lipopolysaccharide interactions with lysozyme differentially affect lipopolysaccharide immunostimulatory activity.

      European journal of biochemistry / FEBS
      Adjuvants, Immunologic, Animals, B-Lymphocytes, cytology, immunology, Cell Differentiation, Cell Line, Escherichia coli, Kinetics, Lipopolysaccharides, isolation & purification, metabolism, Lymphocyte Activation, Mice, Mice, Inbred C3H, Muramidase, Protein Binding, Spleen

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          Abstract

          The effect of complex formation between lysozyme and lipopolysaccharide (LPS) on the immunostimulatory activities of LPS have been investigated in vitro. Three prototype immunostimulatory activities were examined: B-lymphocyte proliferation, B-lymphocyte differentiation and macrophage production of lymphocyte-activating factor activity. Different effects of lysozyme were noted, depending upon the structure of the LPS, even though previous studies have established that all LPS preparations readily bind lysozyme. Both Re-LPS- and lipid-A-dependent immunostimulatory activities were readily inhibited by lysozyme in a dose-dependent fashion. In contrast, S-LPS and Ra-LPS were unaffected in their immunostimulatory activities by lysozyme. These differences were not the result of quantitative differences in LPS binding of lysozyme, or effects of lysozyme on overall binding of LPS to target cells. These data suggest that the factors which dictate the initial interactions between LPS and lymphoreticular cells may not be identical for all LPS preparations and/or purified lipid A.

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