Induction of antibacterial protein synthesis by soluble peptidoglycan in isolated fat body from larvae of the silkworm, Bombyx mori.
Synthesis and secretion of bactericidal protein (cecropin) and lysozyme were induced by soluble peptidoglycan fragments (SPG) from Escherichia coli in a culture of fat body from Bombyx mori larvae. The rate of the secretion by fat body increased as a function of SPG concentration added to the culture medium. The induction of bactericidal activity was specific for peptidoglycan of a particular structure. Thus, SPG from Micrococcus luteus was 500-times less potent than E. coli SPG, and various glucans and peptides structurally related to peptidoglycan were all ineffective as elicitor. These results support the hypothesis that bacteria invading the haemocoel have to be partially degraded to generate peptidoglycan fragments as a signal molecule, which subsequently acts on a receptor on fat body cells and induces antibacterial protein synthesis.
Iketani
M
M
Laboratory of Metabolic Biochemistry, Faculty of Agriculture, Tottori University, Japan.
Morishima
I
I
D000818:Animals; D000900:Anti-Bacterial Agents / Q000096:biosynthesis*; D012831:Bombyx / Q000378:metabolism*; D004305:Dose-Response Relationship, Drug; D004790:Enzyme Induction; D005216:Fat Body / Q000187:drug effects* / Q000378:metabolism; D005786:Gene Expression Regulation; D006458:Hemolymph / Q000737:chemistry; D007301:Insect Hormones / Q000096:biosynthesis; D007814:Larva / Q000378:metabolism; D009113:Muramidase / Q000096:biosynthesis; D009924:Organ Culture Techniques; D010457:Peptidoglycan / Q000494:pharmacology*
D000900:Anti-Bacterial Agents; D007301:Insect Hormones; D010457:Peptidoglycan; D009113:Muramidase