Characterization and cDNA cloning of a cecropin-like antimicrobial peptide, papiliocin, from the swallowtail butterfly, Papilio xuthus

• Published in: Molecules and cells 2010, 29(4), , pp.419-423
• Main Authors: Kim, S.R., National Academy of Agricultural Science, RDA, Suwon, Republic of Korea, Hong, M.Y., National Academy of Agricultural Science, RDA, Suwon, Republic of Korea, Park, S.W., National Academy of Agricultural Science, RDA, Suwon, Republic of Korea, Choi, K.H., National Academy of Agricultural Science, RDA, Suwon, Republic of Korea, Yun, E.Y., National Academy of Agricultural Science, RDA, Suwon, Republic of Korea, Goo, T.W., National Academy of Agricultural Science, RDA, Suwon, Republic of Korea, Kang, S.W., National Academy of Agricultural Science, RDA, Suwon, Republic of Korea, Suh, H.J., Daegu University, Gyeongsan, Republic of Korea, Kim, I.S., Chonnam National University, Gwangju, Republic of Korea, Hwang, J.S., National Academy of Agricultural Science, RDA, Suwon, Republic of Korea
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Antimicrobial Cationic Peptides - genetics; Antimicrobial Cationic Peptides - metabolism; Antimicrobial Cationic Peptides - pharmacology; antimicrobial peptide; Base Sequence; Biochemistry; Biomedical and Life Sciences; Biomedicine; Biotechnology; Butterflies - genetics; Butterflies - metabolism; Candida albicans - drug effects; Candida albicans - growth & development; cDNA; cecropin; Cecropins - genetics; Cecropins - metabolism; Cecropins - pharmacology; Cell Biology; Cloning, Molecular; DNA, Complementary - genetics; Gene Expression Profiling; Gram-Negative Bacteria - drug effects; Gram-Negative Bacteria - growth & development; Gram-Positive Bacteria - drug effects; Gram-Positive Bacteria - growth & development; Hemolysis - drug effects; Humans; Insect Proteins - genetics; Insect Proteins - metabolism; Insect Proteins - pharmacology; Life Sciences; Microbial Sensitivity Tests; Molecular Sequence Data; PAPILIO XUTHUS; papiliocin; Reverse Transcriptase Polymerase Chain Reaction; Sequence Homology, Amino Acid; 생물학
• ISSN: 1016-8478; 0219-1032
• DOI: 10.1007/s10059-010-0050-y

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 detected 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.