Abstract
BackgroundJasmintides jS1 and jS2 from Jasminum sambac were previously identified as a novel family of cysteine-rich peptides (CRPs) with an unusual disulfide connectivity. However, very little else is known about jasmintides, particularly their molecular diversity and functions. Here, we report the discovery and characterization of a novel suite of jasmintides from J. sambac using transcriptomic, peptidomic, structural and functional tools.ResultsTranscriptomic analysis of leaves, flowers and roots revealed 14 unique jasmintide precursors, all of which possess a three-domain architecture comprising a signal peptide, a pro-domain and a mature jasmintide domain. Peptidomic analysis, using fractionated mixtures of jasmintides and chemical derivatization of cysteine to pseudolysine, trypsin digestion and MS/MS sequencing, revealed an additional 86 jasmintides, some of which were post-translationally modified. NMR analysis showed that jasmintide jS3 has three anti-parallel β-strands with a three-disulfide connectivity of CysI−CysV, CysII−CysIV and CysIII−CysVI, which is similar to jasmintide jS1. Jasmintide jS3 was able to withstand thermal, acidic and enzymatic degradation and, importantly, exhibited antifeedant activity against mealworm Tenebrio molitor.ConclusionTogether, this study expands the existing library of jasmintides and furthers our understanding of the molecular diversity and cystine framework of CRPs as scaffolds and tools for engineering peptides targeting pests.
Highlights
Jasmintides jS1 and jS2 from Jasminum sambac were previously identified as a novel family of cysteine-rich peptides (CRPs) with an unusual disulfide connectivity
On the basis of the strong dαN (i, i + 1) NOE connectivity, coupling constants measured by DQF-COSY and 1H-1D experiments, and hydrogen bond patterns determined by amide-hydrogen exchange experiments, jS3 was determined to be composed of a compact disulfide-constrained structure
The cysteine motifs differ between the families, with a C-C-CC-C-C motif found in cysteine knot α-amylase inhibitors and a C-C-C-C-C-C motif found in carboxypeptidase inhibitors
Summary
Jasmintides jS1 and jS2 from Jasminum sambac were previously identified as a novel family of cysteine-rich peptides (CRPs) with an unusual disulfide connectivity. Very little else is known about jasmintides, their molecular diversity and functions. We report the discovery and characterization of a novel suite of jasmintides from J. sambac using transcriptomic, peptidomic, structural and functional tools. Jasminum sambac, which belongs to the Oleaceae family, is a small shrub with fragrant white flowers native to India. A diverse array of secondary metabolites has been isolated from the flowers and leaves of J. sambac, including flavonoids, polyphenols and glycosides [3]. Peptides have attracted interest as potential therapeutic leads from plants [5,6,7,8,9,10,11,12,13,14,15,16]. Peptides are generally susceptible to proteolytic degradation, leading to Kumari et al BMC Plant Biology (2018) 18:144
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