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KMID : 0578320100290040419
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Molecules and Cells
2010 Volume.29 No. 4 p.419 ~ p.423
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Characterization and cDNA Cloning of a Cecropin-Like Antimicrobial Peptide, Papiliocin, from the Swallowtail Butterfly, Papilio xuthus
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Kim Seong-Ryul
Hong Mee-Yeon
Park Seung-Won
Choi Kwang-Ho
Yun Eun-Young
Goo Tae-Won
Kang Seok-Woo
Suh Hwa-Jin
Kim Ik-Soo
Hwang Jae-Sam
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Abstract
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Cecropin is a well-studied antimicrobial peptide that is synthesized in fat body cells and hemocytes of insects in response to hypodermic injury or bacterial infection. A 503 bp cDNA encoding for a cecropin-like peptide was isolated by employing annealing control primer (ACP)-based differential display PCR and 5´-RACE with immunized Papilio xuthus larvae. The open reading frame of the isolated cDNA encoded for a 62-amino acid prepropeptide with a putative 22-residue signal peptide, a 2-residue propeptide, and a 38-residue mature peptide with a theoretical mass of 4060.89 Da. The deduced amino acid sequence of the peptide evidenced a significant degree of identity with other lepidopteran cecropins. This peptide was named papiliocin. RT-PCR results revealed that the papiliocin transcript was de-tected at significant levels after injection with bacterial lipopolysaccharide (LPS). On the basis of the deduced amino acid sequence of papiliocin, a 38-mer mature peptide was chemically synthesized via the Fmoc method, and its antimicrobial activity was analyzed. The synthetic papiliocin peptide evidenced a broad spectrum of activity against fungi, Gram-positive and Gram-negative bacteria, and also evidenced no hemolytic activity against human red blood cells.
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KEYWORD
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antimicrobial peptide, cDNA, cecropin, Papilio xuthus, papiliocin
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