Bactrocerin‐1: A novel inducible antimicrobial peptide from pupae of oriental fruit fly Bactrocera dorsalis Hendel |
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Authors: | Xiang‐Li Dang Jin‐Huan Tian Wan‐Ying Yang Wen‐Xian Wang Jun Ishibashi Ai Asaoka Hui‐Yu Yi Yi‐Feng Li Yang Cao Minoru Yamakawa Shuo‐Yang Wen |
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Affiliation: | 1. Zhejiang Institute of Subtropical Crops, Wenzhou, P.R. China;2. Department of Entomology, South China Agricultural University, Guangzhou, P.R. China;3. Department of Material Science and Engineering, Jinan University, Guangzhou, P.R. China;4. College of Animal Science, South China Agricultural University, Guangzhou, P.R. China;5. Innate Immunity Research Unit, National Institute of Agrobiological Sciences, Ibaraki, Japan;6. Graduate School of Life and Environmental Sciences, University of Tsukuba, Ibaraki, Japan |
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Abstract: | A novel antimicrobial peptide, Bactrocerin‐1, was purified and characterized from an immunized dipteran insect, Bactrocera dorsalis. Bactrocerin‐1 has 20 amino acid residues with a mass of 2,325.95 Da. The amino acid sequence of Bactrocerin‐1 showed very high similarity to the active fragment (46V‐65S‐NH2) of Coleoptericin A. The composition of amino acid residues revealed that Bactrocerin‐1 is a hydrophobic, positively charged, and Lys/Ile/Gly‐rich peptide. Minimal growth inhibition concentration (MIC) measurements for synthesized Bactrocerin‐1 showed a very broad spectrum of anti‐microbial activity against Gram‐positive bacteria, Gram‐negative bacteria, and fungi. Bactrocerin‐1 did not show hemolytic activity toward mouse red blood cells even at a concentration of 50 µM. Analysis of the Helical‐wheel projection and the CD spectrum suggested that Bactrocerin‐1 contains the amphipathic α‐helix. © 2009 Wiley Periodicals, Inc. |
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Keywords: | Bactrocera dorsalis Bactrocerin‐1 Lys/Ile/Gly‐rich antimicrobial peptide |
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