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Beta-1,3-glucan inducible expression of prophenoloxidase-activating proteinase from eri-silkworm, Samia cynthia ricini.

Research paper by Yanyuan Y Bao, Yoshiaki Y Yamano, Isao I Morishima

Indexed on: 20 Feb '07Published on: 20 Feb '07Published in: Comparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology



Abstract

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.