Publication: Characterization of a novel peptide from pathogenic leptospira and its cytotoxic effect
Issued Date
2020-11-01
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ISSN
20760817
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2-s2.0-85094636108
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Mahidol University
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SCOPUS
Bibliographic Citation
Pathogens. Vol.9, No.11 (2020), 1-13
Suggested Citation
Saksakon Paratsaphan, Saengduen Moonsom, Onrapak Reamtong, Sittiruk Roytrakul, Vanaporn Wuthiekanun, Nicholas P.J. Day, Piengchan Sonthayanon Characterization of a novel peptide from pathogenic leptospira and its cytotoxic effect. Pathogens. Vol.9, No.11 (2020), 1-13. doi:10.3390/pathogens9110906 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/59863
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Title
Characterization of a novel peptide from pathogenic leptospira and its cytotoxic effect
Abstract
© 2020 by the authors. Licensee MDPI, Basel, Switzerland. Leptospirosis is a zoonotic infectious disease caused by pathogenic Leptospira species. Virulence proteins have been shown to be key determinants of the pathogenesis of pathogenic Leptospira. A specific peptide at a mass-to-charge ratio of 7000 Da was identified in Leptospira whole cells using matrix-assisted laser/desorption ionization time-of-flight (MALDI-TOF) mass spectrometry. This peptide was specifically present in pathogenic Leptospira and in clinical isolates. We report here the characterization of this specific peptide using a proteomics approach. This peptide was significantly matched to a hypothetical conserved L. interrogans protein (LA2458) with a calculated molecular weight of 7140.136 Da containing a tellurite-resistance domain at its C terminus (TerB-C). The amino acid sequences revealed the presence of hydrophobic transmembrane portions and two linear B-cell epitopes. Despite its low abundance, this synthetic peptide demonstrated dose-dependent cytotoxicity toward African green monkey kidney (Vero) cells via the apoptosis pathway. The concentration of the peptide 100 µM induced about 50% of cell death after a 24 h exposure. This peptide could be useful for the diagnosis of leptospirosis and the study of pathogenesis.