PMID: 19940394Nov 27, 2009Paper

Structural characterization and cytolytic activity of a potent antimicrobial motif in longicin, a defensin-like peptide in the tick Haemaphysalis longicornis

The Journal of Veterinary Medical Science
Morshedur RahmanKozo Fujisaki

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 beta-sheet, which was also observed in the modeled tertiary structure. CD spectroscopic results also showed the existence of a beta-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 beta-sheet as well as the alpha-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 activit...Continue Reading

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Citations

Apr 21, 2011·Parasites & Vectors·Tereza ChrudimskáLibor Grubhoffer
Sep 13, 2016·Developmental and Comparative Immunology·Vivian Montero-AlejoRolando Perdomo-Morales
Nov 22, 2011·Tropical Animal Health and Production·Remil Linggatong GalayKozo Fujisaki
Dec 7, 2021·Journal of Peptide Science : an Official Publication of the European Peptide Society·Kabuzi R MbuayamaAnabella R M Gaspar

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