Characterization and cDNA cloning of a cecropin-like antimicrobial peptide, papiliocin, from the swallowtail butterfly, Papilio xuthus
| Autor: | Iksoo Kim, Seok Woo Kang, Hwa Jin Suh, Seung-Won Park, Kwang-Ho Choi, Mee Yeon Hong, Seong Ryul Kim, Eun Young Yun, Jae Sam Hwang, Tae Won Goo |
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| Rok vydání: | 2009 |
| Předmět: |
Signal peptide
animal structures DNA Complementary Papilio xuthus Molecular Sequence Data Peptide Microbial Sensitivity Tests Gram-Positive Bacteria Hemolysis Complementary DNA Candida albicans Gram-Negative Bacteria Animals Humans Amino Acid Sequence Cloning Molecular Molecular Biology Peptide sequence chemistry.chemical_classification biology Base Sequence Sequence Homology Amino Acid Reverse Transcriptase Polymerase Chain Reaction Gene Expression Profiling fungi Cecropins Cell Biology General Medicine biology.organism_classification Molecular biology Amino acid Open reading frame Cecropin chemistry Biochemistry Insect Proteins Butterflies Antimicrobial Cationic Peptides |
| Zdroj: | Molecules and cells. 29(4) |
| ISSN: | 0219-1032 |
| Popis: | 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. RTPCR 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. |
| Databáze: | OpenAIRE |
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