Polyclonal B-cell activation by a synthetic analogue of bacterial lipoprotein is functionally different from activation by bacterial lipopolysaccharide.
The reactivity of 38 murine strains to a synthetic analogue of bacterial lipoprotein, tripalmitoyl-pentapeptide (TPP), was tested and compared with the reactivity to lipopolysaccharide (LPS). These strains include common laboratory mice and H-2 recombinant inbred lines, as well as some newly bred lines originating from animals recently captured in different regions of Europe. All animals analysed were reactive to TPP and polyclonally activated to proliferation and immunoglobulin synthesis. Large differences in mitogen reactivities of various H-2 recombinant inbred strains suggest that MHC or closely linked gene products influence the reactivity to the LPS and TPP mitogens. By analysing the frequencies of precursor cells reactive to TPP or LPS and the isotype patterns obtained after stimulation, we demonstrated that both mitogens activate individual B cells in different ways.
D000818:Animals; D001402:B-Lymphocytes / Q000276:immunology*; D002455:Cell Division; D005260:Female; D007136:Immunoglobulins / Q000096:biosynthesis; D055666:Lipopeptides; D008070:Lipopolysaccharides / Q000494:pharmacology*; D008213:Lymphocyte Activation; D008297:Male; D051379:Mice; D008815:Mice, Inbred Strains; D009842:Oligopeptides / Q000494:pharmacology*; D051381:Rats; D011919:Rats, Inbred Strains
D007136:Immunoglobulins; D055666:Lipopeptides; D008070:Lipopolysaccharides; D009842:Oligopeptides; C038293:2,3-bis(palmitoyloxy)-2-propyl-N-palmitoyl-cysteinyl-seryl-seryl-asparaginyl-alanine