Studies on the Chitin Binding Property of Novel Cysteine-Rich Peptides from Alternanthera sessilis

Hevein-like peptides make up a family of cysteine-rich peptides (CRPs) and play a role in plants in their defense against insects and fungal pathogens. In this study, we report the isolation and characterization of six hevein-like peptides, aSG1-G3 and aSR1-R3, collectively named altides from green...

Full description

Bibliographic Details
Main Authors:	Kini, Shruthi G., Nguyen, Phuong Q. T., Weissbach, Sophie, Mallagaray, Alvaro, Shin, Joon, Yoon, Ho Sup, Tam, James P.
Other Authors:	School of Biological Sciences
Format:	Journal Article
Language:	English
Published:	2016
Subjects:	peptide Titration
Online Access:	https://hdl.handle.net/10356/81890 http://hdl.handle.net/10220/39737

_version_	1824456463595077632
author	Kini, Shruthi G. Nguyen, Phuong Q. T. Weissbach, Sophie Mallagaray, Alvaro Shin, Joon Yoon, Ho Sup Tam, James P.
author2	School of Biological Sciences
author_facet	School of Biological Sciences Kini, Shruthi G. Nguyen, Phuong Q. T. Weissbach, Sophie Mallagaray, Alvaro Shin, Joon Yoon, Ho Sup Tam, James P.
author_sort	Kini, Shruthi G.
collection	NTU
description	Hevein-like peptides make up a family of cysteine-rich peptides (CRPs) and play a role in plants in their defense against insects and fungal pathogens. In this study, we report the isolation and characterization of six hevein-like peptides, aSG1-G3 and aSR1-R3, collectively named altides from green and red varieties of Alternanthera sessilis, a perennial herb belonging to the Amaranthaceae family. Proteomic analysis of altides revealed they contain six cysteines (6C), seven glycines, four prolines, and a conserved chitin-binding domain (SXYGY/SXFGY). Thus far, only four 6C-hevein-like peptides have been isolated and characterized; hence, our study expands the existing library of these peptides. Nuclear magnetic resonance (NMR) study of altides showed its three disulfide bonds were arranged in a cystine knot motif. As a consequence of this disulfide arrangement, they are stable against thermal and enzymatic degradation. Gene cloning studies revealed altides contain a three-domain precursor with an endoplasmic reticulum signal peptide followed by a mature CRP domain and a short C-terminal tail. This indicates that the biosynthesis of altides is through the secretory pathway. (1)H NMR titration experiments showed that the 29-30-amino acid altides bind to chitin oligomers with dissociation constants in the micromolar range. Aromatic residues in the chitin-binding domain of altides were involved in the binding interaction. To the best of our knowledge, aSR1 is the smallest hevein-like peptide with a dissociation constant toward chitotriose comparable to those of hevein and other hevein-like peptides. Together, our study expands the existing library of 6C-hevein-like peptides and provides insights into their structure, biosynthesis, and interaction with chitin oligosaccharides.
first_indexed	2025-02-19T03:54:30Z
format	Journal Article
id	ntu-10356/81890
institution	Nanyang Technological University
language	English
last_indexed	2025-02-19T03:54:30Z
publishDate	2016
record_format	dspace
spelling	ntu-10356/818902023-02-28T16:59:10Z Studies on the Chitin Binding Property of Novel Cysteine-Rich Peptides from Alternanthera sessilis Kini, Shruthi G. Nguyen, Phuong Q. T. Weissbach, Sophie Mallagaray, Alvaro Shin, Joon Yoon, Ho Sup Tam, James P. School of Biological Sciences peptide Titration Hevein-like peptides make up a family of cysteine-rich peptides (CRPs) and play a role in plants in their defense against insects and fungal pathogens. In this study, we report the isolation and characterization of six hevein-like peptides, aSG1-G3 and aSR1-R3, collectively named altides from green and red varieties of Alternanthera sessilis, a perennial herb belonging to the Amaranthaceae family. Proteomic analysis of altides revealed they contain six cysteines (6C), seven glycines, four prolines, and a conserved chitin-binding domain (SXYGY/SXFGY). Thus far, only four 6C-hevein-like peptides have been isolated and characterized; hence, our study expands the existing library of these peptides. Nuclear magnetic resonance (NMR) study of altides showed its three disulfide bonds were arranged in a cystine knot motif. As a consequence of this disulfide arrangement, they are stable against thermal and enzymatic degradation. Gene cloning studies revealed altides contain a three-domain precursor with an endoplasmic reticulum signal peptide followed by a mature CRP domain and a short C-terminal tail. This indicates that the biosynthesis of altides is through the secretory pathway. (1)H NMR titration experiments showed that the 29-30-amino acid altides bind to chitin oligomers with dissociation constants in the micromolar range. Aromatic residues in the chitin-binding domain of altides were involved in the binding interaction. To the best of our knowledge, aSR1 is the smallest hevein-like peptide with a dissociation constant toward chitotriose comparable to those of hevein and other hevein-like peptides. Together, our study expands the existing library of 6C-hevein-like peptides and provides insights into their structure, biosynthesis, and interaction with chitin oligosaccharides. NRF (Natl Research Foundation, S’pore) Accepted version 2016-01-21T04:04:29Z 2019-12-06T14:42:26Z 2016-01-21T04:04:29Z 2019-12-06T14:42:26Z 2015 Journal Article Kini, S. G., Nguyen, P. Q. T., Weissbach, S., Mallagaray, A., Shin, J., Yoon, H. S., et al. (2015). Studies on the Chitin Binding Property of Novel Cysteine-Rich Peptides from Alternanthera sessilis. Biochemistry, 54(43), 6639-6649. 0006-2960 https://hdl.handle.net/10356/81890 http://hdl.handle.net/10220/39737 10.1021/acs.biochem.5b00872 en Biochemistry © 2015 American Chemical Society. This is the author created version of a work that has been peer reviewed and accepted for publication by Biochemistry, American Chemical Society. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1021/acs.biochem.5b00872]. 29 p. application/pdf
spellingShingle	peptide Titration Kini, Shruthi G. Nguyen, Phuong Q. T. Weissbach, Sophie Mallagaray, Alvaro Shin, Joon Yoon, Ho Sup Tam, James P. Studies on the Chitin Binding Property of Novel Cysteine-Rich Peptides from Alternanthera sessilis
title	Studies on the Chitin Binding Property of Novel Cysteine-Rich Peptides from Alternanthera sessilis
title_full	Studies on the Chitin Binding Property of Novel Cysteine-Rich Peptides from Alternanthera sessilis
title_fullStr	Studies on the Chitin Binding Property of Novel Cysteine-Rich Peptides from Alternanthera sessilis
title_full_unstemmed	Studies on the Chitin Binding Property of Novel Cysteine-Rich Peptides from Alternanthera sessilis
title_short	Studies on the Chitin Binding Property of Novel Cysteine-Rich Peptides from Alternanthera sessilis
title_sort	studies on the chitin binding property of novel cysteine rich peptides from alternanthera sessilis
topic	peptide Titration
url	https://hdl.handle.net/10356/81890 http://hdl.handle.net/10220/39737
work_keys_str_mv	AT kinishruthig studiesonthechitinbindingpropertyofnovelcysteinerichpeptidesfromalternantherasessilis AT nguyenphuongqt studiesonthechitinbindingpropertyofnovelcysteinerichpeptidesfromalternantherasessilis AT weissbachsophie studiesonthechitinbindingpropertyofnovelcysteinerichpeptidesfromalternantherasessilis AT mallagarayalvaro studiesonthechitinbindingpropertyofnovelcysteinerichpeptidesfromalternantherasessilis AT shinjoon studiesonthechitinbindingpropertyofnovelcysteinerichpeptidesfromalternantherasessilis AT yoonhosup studiesonthechitinbindingpropertyofnovelcysteinerichpeptidesfromalternantherasessilis AT tamjamesp studiesonthechitinbindingpropertyofnovelcysteinerichpeptidesfromalternantherasessilis

Studies on the Chitin Binding Property of Novel Cysteine-Rich Peptides from Alternanthera sessilis

Similar Items