Understanding the diversity and distribution of cyclotides from plants of varied genetic origin

Ravipati, Anjaneya S., Poth, Aaron G., Henriques, Sonia Troeira, Bhandari, Murari, Huang, Yen-Hua, Nino, Jaime, Colgrave, Michelle L. and Craik, David J. (2017) Understanding the diversity and distribution of cyclotides from plants of varied genetic origin. Journal of Natural Products, 80 5: 1522-1530. doi:10.1021/acs.jnatprod.7b00061


Author Ravipati, Anjaneya S.
Poth, Aaron G.
Henriques, Sonia Troeira
Bhandari, Murari
Huang, Yen-Hua
Nino, Jaime
Colgrave, Michelle L.
Craik, David J.
Title Understanding the diversity and distribution of cyclotides from plants of varied genetic origin
Journal name Journal of Natural Products   Check publisher's open access policy
ISSN 1520-6025
0163-3864
Publication date 2017-05-26
Sub-type Article (original research)
DOI 10.1021/acs.jnatprod.7b00061
Open Access Status Not yet assessed
Volume 80
Issue 5
Start page 1522
End page 1530
Total pages 9
Place of publication Washington, DC, United States
Publisher American Chemical Society
Language eng
Abstract Cyclotides are a large family of naturally occurring plant-derived macrocyclic cystine-knot peptides, with more than 400 having been identified in species from the Violaceae, Rubiaceae, Cucurbitaceae, Fabaceae, and Solanaceae families. Nevertheless, their specialized distribution within the plant kingdom remains poorly understood. In this study, the diversity of cyclotides was explored through the screening of 197 plants belonging to 43 different families. In total, 28 cyclotides were sequenced from 15 plant species, one of which belonged to the Rubiaceae and 14 to the Violaceae. Every Violaceae species screened contained cyclotides, but they were only sparsely represented in Rubiaceae and nonexistent in other families. The study thus supports the hypothesis that cyclotides are ubiquitous in the Violaceae, and it adds to the list of plants found to express kalata S and cycloviolacin O12. Finally, previous studies suggested the existence of cyclotide isoforms with either an Asn or an Asp at the C-terminal processing site of the cyclotide domain within the precursor proteins. Here we found that despite the discovery of a few cyclotides genuinely containing an Asp in loop 6 as evidenced by gene sequencing, deamidation of Asn during enzymatic digestion resulted in the artifactual presence of Asp isoforms. This result is consistent with studies suggesting that peptides can undergo deamidation after being subjected to external factors, including pH, temperature, and enzymatic digestion.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
Institute for Molecular Bioscience - Publications
 
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