Yoe Sung Moon, Kang Chang Soo, Han Sung Sik, Bang In Seok
Department of Biological Sciences, Dankook University, Cheonan 330-714, South Korea.
Comp Biochem Physiol B Biochem Mol Biol. 2006 Jun;144(2):199-205. doi: 10.1016/j.cbpb.2006.02.010. Epub 2006 Feb 28.
Hinnavins, together with lysozymes, are the main types of antibacterial peptides/proteins previously isolated from the larval haemolymph of the cabbage butterfly, Artogeia rapae as part of the humoral immune response to a bacterial invasion. One of these antibacterial peptides, named hinnavin II, was purified and characterized after cDNA cloning. The purified hinnavin II was more active against Gram negative than against Gram positive bacteria. Hinnavin II also showed a powerful synergistic effect on the inhibition of bacterial growth with purified lysozyme. The cDNA has a total length of 186 bp with a 114 coding region. The deduced protein sequence contains 38 amino acids with a coding capacity of 4142.8 Da. The result of a multiple sequence alignment and phylogenetic analysis with Clustal W indicated that mature hinnavin II showed an approximately 78.9% amino acid sequence identity with cecropin A and originated from a group containing mostly lepidopteran cecropins.
辛那文与溶菌酶一样，是先前从菜粉蝶（粉纹夜蛾）幼虫血淋巴中分离出的主要抗菌肽/蛋白质类型，是对细菌入侵的体液免疫反应的一部分。其中一种抗菌肽名为辛那文II，在进行cDNA克隆后对其进行了纯化和表征。纯化后的辛那文II对革兰氏阴性菌的活性比对革兰氏阳性菌的活性更强。辛那文II在抑制细菌生长方面还与纯化的溶菌酶表现出强大的协同作用。该cDNA全长186 bp，编码区为114 bp。推导的蛋白质序列包含38个氨基酸，编码能力为4142.8 Da。使用Clustal W进行的多序列比对和系统发育分析结果表明，成熟的辛那文II与天蚕素A的氨基酸序列同一性约为78.9% , 并且起源于一个主要包含鳞翅目天蚕素的群体。
