title: Binding of bacterial endotoxin (LPS) to encephalitogenic myelin basic protein and modulation of characteristic biologic activities of LPS.
abstract: Myelin basic protein, isolated from central nervous system tissue and an inducer of experimental allergic encephalomyelitis in animals, has been demonstrated to form a stable molecular complex with the lipid A region of gram-negative bacterial lipopolysaccharides (endotoxins). This binding of endotoxin with myelin basic protein results in generation of lower m.w. aggregates with decreased isopycnic density. A number of lipid A-induced characteristic properties of endotoxin, such as B lymphocyte proliferative response in C3H/St mice, complement activation of normal human serum, Limulus lysate gelation, and lethal effects in mice, are modified as a result of binding of myelin basic protein with lipopolysaccharides.
mesh_terms: D000818:Animals; D001402:B-Lymphocytes; D001665:Binding Sites; D002500:Centrifugation, Isopycnic; D002850:Chromatography, Gel; D003167:Complement Activation; D005260:Female; D006801:Humans; D008050:Lipid A / Q000494:pharmacology; D008070:Lipopolysaccharides / Q000378:metabolism* / Q000502:physiology*; D008213:Lymphocyte Activation; D008297:Male; D051379:Mice; D008810:Mice, Inbred C57BL; D009026:Mortality; D004676:Myelin Basic Protein / Q000378:metabolism*; D009503:Neutropenia / Q000209:etiology; D011817:Rabbits
chemical_list: D008050:Lipid A; D008070:Lipopolysaccharides; D004676:Myelin Basic Protein