Hwang Jae-Sam, Lee Juneyoung, Kim Yeon-Ju, Bang Hea-Son, Yun Eun-Young, Kim Seong-Ryul, Suh Hwa-Jin, Kang Bo-Ram, Nam Sung-Hee, Jeon Jae-Pil, Kim Iksoo, Lee Dong Gun
National Academy of Agricultural Science, RDA, Suwon 441-707, South Korea.
Int J Pept. 2009;2009. doi: 10.1155/2009/136284. Epub 2009 Oct 22.
The antibacterial activity of immune-related peptides, identified by a differential gene expression analysis, was investigated to suggest novel antibacterial peptides. A cDNA encoding a defensin-like peptide, Coprisin, was isolated from bacteria-immunized dung beetle, Copris tripartitus, by using differential dot blot hybridization. Northern blot analysis showed that Coprisin mRNA was up-regulated from 4 hours after bacteria injection and its expression level was reached a peak at 16 hours. The deduced amino acid sequence of Coprisin was composed of 80 amino acids with a predicted molecular weight of 8.6 kDa and a pI of 8.7. The amino acid sequence of mature Coprisin was found to be 79.1% and 67.4% identical to those of defensin-like peptides of Anomala cuprea and Allomyrina dichotoma, respectively. We also investigated active sequences of Coprisin by using amino acid modification. The result showed that the 9-mer peptide, LLCIALRKK-NH(2), exhibited potent antibacterial activities against Escherichia coli and Staphylococcus aureus.
通过差异基因表达分析鉴定的免疫相关肽的抗菌活性进行了研究,以寻找新型抗菌肽。利用差异点杂交技术,从经细菌免疫的蜣螂(粪金龟)中分离出一种编码防御素样肽Coprisin的cDNA。Northern印迹分析表明,Coprisin mRNA在细菌注射后4小时开始上调,在16小时达到表达峰值。Coprisin推导的氨基酸序列由80个氨基酸组成,预测分子量为8.6 kDa,pI为8.7。发现成熟Coprisin的氨基酸序列与铜绿丽金龟和双叉犀金龟的防御素样肽分别有79.1%和67.4%的同源性。我们还通过氨基酸修饰研究了Coprisin的活性序列。结果表明,九肽LLCIALRKK-NH(2)对大肠杆菌和金黄色葡萄球菌具有强大的抗菌活性。