Journal article
Discovery by proteogenomics and characterization of an RF-amide neuropeptide from cone snail venom
SD Robinson, H Safavi-Hemami, S Raghuraman, JS Imperial, AT Papenfuss, RW Teichert, AW Purcell, BM Olivera, RS Norton
Journal of Proteomics | Published : 2015
Abstract
In this study, a proteogenomic annotation strategy was used to identify a novel bioactive peptide from the venom of the predatory marine snail Conus victoriae. The peptide, conorfamide-Vc1 (CNF-Vc1), defines a new gene family. The encoded mature peptide was unusual for conotoxins in that it was cysteine-free and, despite low overall sequence similarity, contained two short motifs common to known neuropeptides/hormones. One of these was the C-terminal RF-amide motif, commonly observed in neuropeptides from a range of organisms, including humans. The mature venom peptide was synthesized and characterized structurally and functionally. The peptide was bioactive upon injection into mice, and cal..
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Awarded by National Institutes of Health
Funding Acknowledgements
We thank Johan Pas for specimen collection, Dorothy Loo and Dr. Nicholas Williamson for technical assistance with mass spectrometry, Dr. Joanna Gajewiak for peptide synthesis and My Thi Thao Huynh for assistance with image presentation. The authors acknowledge financial support from a Discovery Grant (DP110101331) from the Australian Research Council (BMO, AWP) and a National Institutes of Health Grant GM 48677 (BMO). AWP and RSN acknowledge fellowship support from the Australian National Health and Medical Research Council. HSH is supported by a Marie Curie Fellowship from the European Commission (CONBIOS 330486).