Parallel induction of cecropin and lysozyme in larvae of the silkworm, Bombyx mori.
Lysozyme activity in the hemolymph of Bombyx mori increased in parallel with cecropin activity after injection of the larvae with soluble peptidoglycan or UV-killed bacteria. The lysozyme and cecropin A genes were expressed in parallel in the fat body after injection of peptidoglycan as detected by northern blot hybridization. The elicitor specificity for lysozyme induction was identical to that for cecropin, suggesting a common mechanism for recognition of bacteria and following signal transduction introducing to the simultaneous synthesis of cecropin and lysozyme. Bacterial cells killed by UV-irradiation were also effective as elicitor when added to the fat body culture, suggesting that phagocytosis of bacteria by hemocytes may not be an essential process for the induction of antibacterial protein synthesis in the silkworm.
Morishima
I
I
Laboratory of Metabolic Biochemistry, Tottori University, Japan.
Horiba
T
T
Iketani
M
M
Nishioka
E
E
Yamano
Y
Y
D000818:Animals; D023181:Antimicrobial Cationic Peptides; D015152:Blotting, Northern; D012831:Bombyx / Q000276:immunology*; D015870:Gene Expression; D006458:Hemolymph / Q000276:immunology; D007301:Insect Hormones / Q000096:biosynthesis / Q000235:genetics; D009113:Muramidase / Q000096:biosynthesis* / Q000235:genetics; D010452:Peptide Biosynthesis; D010455:Peptides / Q000235:genetics; D010457:Peptidoglycan / Q000276:immunology
D023181:Antimicrobial Cationic Peptides; D007301:Insect Hormones; D010455:Peptides; D010457:Peptidoglycan; C031161:cecropin A; D009113:Muramidase