Beta-1,3-glucan inducible expression of prophenoloxidase-activating proteinase from eri-silkworm, Samia cynthia ricini.
A cDNA clone encoding possible prophenoloxidase-activating serine protease (PAP) was isolated by screening the cDNA library from immunized larval fat body of the wild silkmoth, Samia cynthia ricini. The cDNA encodes a 438 amino acid open reading frame with a predicted 20 residue signal peptide. Samia PAP has high sequence similarity to Bombyx mori and Manduca sexta PAPs, which contain two amino terminal clip domains followed by a carboxyl-terminal catalytic domain. The expression of the gene was barely detectable in the fat body of naive larvae, but induced after injection of the larvae with beta-1,3-glucans or bacterial cells.
Bao
Yanyuan
Y
Department of Biochemistry and Biotechnology, Faculty of Agriculture, Tottori University, Tottori, Japan.
Yamano
Yoshiaki
Y
Morishima
Isao
I
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D012831:Bombyx / Q000201:enzymology*; D018076:DNA, Complementary / Q000235:genetics / Q000302:isolation & purification; D004790:Enzyme Induction / Q000187:drug effects; D008969:Molecular Sequence Data; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics*; D047071:beta-Glucans / Q000494:pharmacology*
D018076:DNA, Complementary; D047071:beta-Glucans; C033363:beta-1,3-glucan; D012697:Serine Endopeptidases; C022435:prephenoloxidase-activating enzyme