Discovery by proteogenomics and characterization of an RF-amide neuropeptide from cone snail venom

Samuel Robinson, Helena Safavi-Hemami, Shrinivasan Cheenu Raghuraman, Julita S Imperial, Anthony Troy Papenfuss, Russell W Teichert, Anthony Wayne Purcell, Baldomero Marquez Olivera, Raymond Stanley Norton

Research output: Contribution to journalArticleResearchpeer-review

31 Citations (Scopus)


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 calcium imaging of mouse dorsal root ganglion (DRG) cells revealed that the peptide elicits an increase in intracellular calcium levels in a subset of DRG neurons. Unusually for most Conus venom peptides, it also elicited an increase in intracellular calcium levels in a subset of non-neuronal cells.
Original languageEnglish
Pages (from-to)38 - 47
Number of pages10
JournalJournal of Proteomics
Publication statusPublished - 2015

Cite this