B-lymphocyte mitogenicity in vitro of a synthetic lipopeptide fragment derived from bacterial lipoprotein.
Lipoprotein from the outer membrane of Escherichia coli is a potent mitogen towards lymphocytes of different species. A lipopeptide fragment corresponding to the N-terminal part of the lipoprotein was prepared by chemical synthesis. The mitogenicity of the compound was demonstrated by measuring the incorporation of both [3H]thymidine into DNA and [3H]uridine into RNA at various times after the addition of lipopeptide to mouse spleen cell cultures. The lipopeptide also activated B-lymphocyte development into immunoglobulin secreting cells, as shown by a hemolytic plaque assay. The mitogenicity of the synthetic compound was comparable to the activity of the B-lymphocyte mitogens lipoprotein and lipopolysaccharide. Thus, it was shown that a fragment of a bacterial surface component prepared by chemical synthesis, exhibits a marked biological activity.
D000818:Animals; D001402:B-Lymphocytes / Q000187:drug effects / Q000276:immunology*; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins / Q000138:chemical synthesis / Q000494:pharmacology*; D004926:Escherichia coli / Q000276:immunology*; D008074:Lipoproteins / Q000494:pharmacology*; D008213:Lymphocyte Activation / Q000187:drug effects*; D008565:Membrane Proteins / Q000138:chemical synthesis / Q000494:pharmacology*; D051379:Mice; D008815:Mice, Inbred Strains; D008934:Mitogens
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D008074:Lipoproteins; D008565:Membrane Proteins; D008934:Mitogens