Cloning of cDNAs for cecropins A and B, and expression of the genes in the silkworm, Bombyx mori.
cDNA clones coding cecropins A and B were isolated from a cDNA library constructed from the fat body of immunized Bombyx mori larvae. The cloned cDNAs had an open reading frame of 63 amino acids, indicating the primary translated peptides were processed to form mature cecropins of 35 amino acid residues. The homology in the coding regions of cecropins A and B was 73%. In immunized fat body, the expression of both cecropin A and B genes reached the maximal level 5 h after the injection of soluble peptidoglycan, and the high level was maintained until 9 h after immunization. The cecropin A and B genes were expressed at high levels in fat body and hemocytes, at lower but significant levels in malpighian tube, slightly in midgut, and none in silk gland.
Yamano
Y
Y
Laboratory of Metabolic Biochemistry, Faculty of Agriculture, Torrori University, Japan.
Matsumoto
M
M
Inoue
K
K
Kawabata
T
T
Morishima
I
I
D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000096:biosynthesis* / Q000737:chemistry; D023181:Antimicrobial Cationic Peptides; D001483:Base Sequence; D012831:Bombyx / Q000235:genetics*; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000737:chemistry / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D005216:Fat Body / Q000378:metabolism; D015870:Gene Expression / Q000235:genetics; D017344:Genes, Insect; D007301:Insect Hormones / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics*; D019476:Insect Proteins; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction; D012689:Sequence Homology, Nucleic Acid
D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D018076:DNA, Complementary; D007301:Insect Hormones; D019476:Insect Proteins; C031161:cecropin A; C031162:cecropin B protein, Insecta