Bao Yanyuan, Yamano Yoshiaki, Morishima Isao
Department of Biochemistry and Biotechnology, Faculty of Agriculture, Tottori University, Tottori, Japan.
Comp Biochem Physiol B Biochem Mol Biol. 2007 May;147(1):45-8. doi: 10.1016/j.cbpb.2006.12.016. Epub 2007 Jan 16.
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.
通过筛选来自野蚕蓖麻蚕免疫幼虫脂肪体的cDNA文库，分离出一个编码可能的酚氧化酶原激活丝氨酸蛋白酶（PAP）的cDNA克隆。该cDNA编码一个438个氨基酸的开放阅读框，带有一个预测的20个残基的信号肽。蓖麻蚕PAP与家蚕和烟草天蛾的PAP具有高度的序列相似性，它们都包含两个氨基末端剪切结构域，随后是一个羧基末端催化结构域。该基因在未免疫幼虫的脂肪体中几乎检测不到表达，但在用β-1,3-葡聚糖或细菌细胞注射幼虫后会被诱导表达。
