Structural Characterization and Cytolytic Activity of a Potent Antimicrobial Motif in Longicin, a Defensin-Like Peptide in the Tick Haemaphysalis longicornis
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- RAHMAN Md. Morshedur
- Department of Frontier Veterinary Medicine, Kagoshima University
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- TSUJI Naotoshi
- National Institute of Animal Health, National Agricultural Research Organization
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- BOLDBAATAR Damdinsuren
- Department of Frontier Veterinary Medicine, Kagoshima University
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- BATTUR Banzragch
- Department of Frontier Veterinary Medicine, Kagoshima University
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- LIAO Min
- Department of Frontier Veterinary Medicine, Kagoshima University
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- UMEMIYA-SHIRAFUJI Rika
- Department of Frontier Veterinary Medicine, Kagoshima University
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- YOU Myungjo
- Department of Veterinary Parasitology, College of Veterinary Medicine, Chonbuk National University
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- TANAKA Tetsuya
- Department of Frontier Veterinary Medicine, Kagoshima University
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- FUJISAKI Kozo
- Department of Frontier Veterinary Medicine, Kagoshima University
Bibliographic Information
- Other Title
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- Parasitology: Structural characterization and cytolytic activity of a potent antimicrobial motif in longicin, a defensin-like peptide in the tick Haemaphysalis longicornis
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Abstract
Longicin, a defensin-like peptide, was recently identified in the hard tick Haemaphysalis longicornis. Longicin and one of its synthetic partial analogs (P4) displayed antimicrobial/fungicidal/parasiticidal activity. In the present study, we compared longicin-derived synthetic analogs in order to characterize the antimicrobial motif (P4) by analyzing some structural features using various bioinformatic tools and/or CD spectroscopy. According to the chemicophysical characteristics, P4 is suggested to be a cationic peptide with hydrophobic and amphipathic character. The predicted secondary structure indicated the existence of a β-sheet, which was also observed in the modeled tertiary structure. CD spectroscopic results also showed the existence of a β-sheet and transition to a helical conformation in the presence of membrane-mimicking conditions. These structural observations on P4 suggested that the antimicrobial activity could be due to the β-sheet as well as the α-helix. In addition, a sequence homology search showed that molecules identified in other ticks and organisms also have the P4 analogous domain at their C-terminal, which indicates P4 as a conserved domain. The peptide P4 also showed low cytolytic activity. Based on the present result and previously reported studies, the peptide P4 could be suggested as a novel antimicrobial domain indicating future therapeutic agent against bacteria.<br>
Journal
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- Journal of Veterinary Medical Science
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Journal of Veterinary Medical Science 72 (2), 149-156, 2010
JAPANESE SOCIETY OF VETERINARY SCIENCE
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Keywords
Details 詳細情報について
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- CRID
- 1390001206428051456
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- NII Article ID
- 130000134519
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- NII Book ID
- AA10796138
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- ISSN
- 13477439
- 09167250
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- NDL BIB ID
- 10592972
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed