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Title: Identification and characterization of roseltide, a knottin-type neutrophil elastase inhibitor derived from hibiscus sabdariffa
Authors: Nguyen, Giang Kien Truc
Tam, James Pingkwan
Loo, Shining
Kam, Antony
Xiao, Tianshu
Liu, Chuan Fa
Keywords: Neutrophil
Leukocyte Elastase Inhibitor
DRNTU::Science::Biological sciences
Issue Date: 2016
Source: Loo, S., Kam, A., Xiao, T., Nguyen, G. K. T., Liu, C. F., & Tam, J. P. (2016). Identification and characterization of roseltide, a knottin-type neutrophil elastase inhibitor derived from hibiscus sabdariffa. Scientific Reports, 6, 39401-. doi:10.1038/srep39401
Series/Report no.: Scientific Reports
Abstract: Plant knottins are of therapeutic interest due to their high metabolic stability and inhibitory activity against proteinases involved in human diseases. The only knottin-type proteinase inhibitor against porcine pancreatic elastase was first identified from the squash family in 1989. Here, we report the identification and characterization of a knottin-type human neutrophil elastase inhibitor from Hibiscus sabdariffa of the Malvaceae family. Combining proteomic and transcriptomic methods, we identified a panel of novel cysteine-rich peptides, roseltides (rT1-rT8), which range from 27 to 39 residues with six conserved cysteine residues. The 27-residue roseltide rT1 contains a cysteine spacing and amino acid sequence that is different from the squash knottin-type elastase inhibitor. NMR analysis demonstrated that roseltide rT1 adopts a cystine-knot fold. Transcriptome analyses suggested that roseltides are bioprocessed by asparagine endopeptidases from a three-domain precursor. The cystine-knot structure of roseltide rT1 confers its high resistance against degradation by endopeptidases, 0.2 N HCl, and human serum. Roseltide rT1 was shown to inhibit human neutrophil elastase using enzymatic and pull-down assays. Additionally, roseltide rT1 ameliorates neutrophil elastase-stimulated cAMP accumulation in vitro. Taken together, our findings demonstrate that roseltide rT1 is a novel knottin-type neutrophil elastase inhibitor with therapeutic potential for neutrophil elastase associated diseases.
DOI: 10.1038/srep39401
Schools: School of Biological Sciences 
Rights: © 2016 The Authors (Nature Publishing Group). This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit
Fulltext Permission: open
Fulltext Availability: With Fulltext
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