A continent of plant defense peptide diversity: Cyclotides in Australian Hybanthus (Violaceae)

Simonsen, S. M., Sando, L., Ireland, D. C., Colgrave, M. L., Bharathi, R., Goransson, U. and Craik, D. J. (2005) A continent of plant defense peptide diversity: Cyclotides in Australian Hybanthus (Violaceae). Plant Cell, 17 11: 3176-3189. doi:10.1105/tpc.105.034678

Author Simonsen, S. M.
Sando, L.
Ireland, D. C.
Colgrave, M. L.
Bharathi, R.
Goransson, U.
Craik, D. J.
Title A continent of plant defense peptide diversity: Cyclotides in Australian Hybanthus (Violaceae)
Journal name Plant Cell   Check publisher's open access policy
ISSN 1040-4651
Publication date 2005-01-01
Year available 2005
Sub-type Article (original research)
DOI 10.1105/tpc.105.034678
Open Access Status DOI
Volume 17
Issue 11
Start page 3176
End page 3189
Total pages 14
Place of publication Rockville
Publisher Amer Soc Plant Biologists
Language eng
Subject C1
250302 Biological and Medical Chemistry
780105 Biological sciences
Abstract Cyclotides are plant-derived miniproteins that have the unusual features of a head-to-tail cyclized peptide backbone and a knotted arrangement of disulfide bonds. It had been postulated that they might be an especially large family of host defense agents, but this had not yet been tested by field data on cyclotide variation in wild plant populations. In this study, we sampled Australian Hybanthus (Violaceae) to gain an insight into the level of variation within populations, within species, and between species. A wealth of cyclotide diversity was discovered: at least 246 new cyclotides are present in the 11 species sampled, and 26 novel sequences were characterized. A new approach to the discovery of cyclotide sequences was developed based on the identification of a conserved sequence within a signal sequence in cyclotide precursors. The number of cyclotides in the Violaceae is now estimated to be >9000. Cyclotide physicochemical profiles were shown to be a useful taxonomic feature that reflected species and their morphological relationships. The novel sequences provided substantial insight into the tolerance of the cystine knot framework in cyclotides to amino acid substitutions and will facilitate protein engineering applications of this framework.
Keyword Biochemistry & Molecular Biology
Plant Sciences
Cell Biology
Cyclic Cystine Knot
Inhibitory Macrocyclic Peptides
Anti-hiv Activity
Kalata B1
Circular Proteins
Precursor Protein
Q-Index Code C1
Institutional Status UQ

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Created: Wed, 15 Aug 2007, 15:45:31 EST