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International Journal of Peptides
Volume 2009 (2009), Article ID 136284, 5 pages
Research Article

Isolation and Characterization of a Defensin-Like Peptide (Coprisin) from the Dung Beetle, Copris tripartitus

1National Academy of Agricultural Science, RDA, Suwon 441-707, South Korea
2School of Life Sciences and Biotechnology, College of Natural Sciences, Kyungpook National University, Daegu 702-701, South Korea
3Department of Biotechnology, Daegu University, Kyungbuk 712-714, South Korea
4Center for Genome Science, Korea National Institute of Health, Seoul 122-701, South Korea
5College of Agriculture and Life Sciences, Chonnam National University, Gwangju 500-757, South Korea

Received 17 February 2009; Revised 3 July 2009; Accepted 13 August 2009

Academic Editor: Yuan-Jian Li

Copyright © 2009 Jae-Sam Hwang et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


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- , exhibited potent antibacterial activities against Escherichia coli and Staphylococcus aureus.