Sugiyama M, Kuniyoshi H, Kotani E, Taniai K, Kadono-Okuda K, Kato Y, Yamamoto M, Shimabukuro M, Chowdhury S, Xu J
Laboratory of Biological Defense, National Institute of Sericultural and Entomological Science, Ibaraki, Japan.
Insect Biochem Mol Biol. 1995 Mar;25(3):385-92. doi: 10.1016/0965-1748(94)00080-2.
A Bombyx mori cDNA was cloned that hybridized with Hyalophora cecropia attacin probe and its nucleotide sequence was determined. This cDNA consisted of 846 nucleotides and the deduced amino acid sequence showed that the cDNA encodes an attacin precursor protein. The putative mature protein of B. mori attacin had 70.4, 68.3 and 18.8% identity in amino acid sequences with that of H. cecropia acidic and basic attacins and Sarcophaga peregrina sarcotoxin IIA, respectively. B. mori and H. cecropia attacins and S. peregrina sarcotoxin IIA had two subdomains in each G domain, suggesting that common amino acid residues in the subdomains are conserved during evolution and plays an important role in the activity of the antibacterial proteins. Expression of B. mori attacin gene was rapidly induced by the injection of Escherichia coli cells into B. mori larvae and continued at least for 48 h mainly in fat bodies and hemocytes.
克隆了一个与天蚕蛾(Hyalophora cecropia)抗菌肽探针杂交的家蚕(Bombyx mori)cDNA,并测定了其核苷酸序列。该cDNA由846个核苷酸组成,推导的氨基酸序列表明该cDNA编码一种抗菌肽前体蛋白。家蚕抗菌肽的假定成熟蛋白在氨基酸序列上与天蚕蛾酸性和碱性抗菌肽以及棕尾别麻蝇(Sarcophaga peregrina)的肌毒素IIA分别具有70.4%、68.3%和18.8%的同一性。家蚕和天蚕蛾的抗菌肽以及棕尾别麻蝇的肌毒素IIA在每个G结构域中有两个亚结构域,这表明亚结构域中的共同氨基酸残基在进化过程中是保守的,并且在抗菌蛋白的活性中起重要作用。将大肠杆菌细胞注射到家蚕幼虫中可迅速诱导家蚕抗菌肽基因的表达,且至少持续48小时,主要在脂肪体和血细胞中表达。