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

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 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
Volume114
DOIs
Publication statusPublished - 2015

Cite this

Robinson, S., Safavi-Hemami, H., Raghuraman, S. C., Imperial, J. S., Papenfuss, A. T., Teichert, R. W., ... Norton, R. S. (2015). Discovery by proteogenomics and characterization of an RF-amide neuropeptide from cone snail venom. Journal of Proteomics, 114, 38 - 47. https://doi.org/10.1016/j.jprot.2014.11.003
Robinson, Samuel ; Safavi-Hemami, Helena ; Raghuraman, Shrinivasan Cheenu ; Imperial, Julita S ; Papenfuss, Anthony Troy ; Teichert, Russell W ; Purcell, Anthony Wayne ; Olivera, Baldomero Marquez ; Norton, Raymond Stanley. / Discovery by proteogenomics and characterization of an RF-amide neuropeptide from cone snail venom. In: Journal of Proteomics. 2015 ; Vol. 114. pp. 38 - 47.
@article{7d7163c071ca45ed99d4077e0390e11b,
title = "Discovery by proteogenomics and characterization of an RF-amide neuropeptide from cone snail venom",
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 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.",
author = "Samuel Robinson and Helena Safavi-Hemami and Raghuraman, {Shrinivasan Cheenu} and Imperial, {Julita S} and Papenfuss, {Anthony Troy} and Teichert, {Russell W} and Purcell, {Anthony Wayne} and Olivera, {Baldomero Marquez} and Norton, {Raymond Stanley}",
year = "2015",
doi = "10.1016/j.jprot.2014.11.003",
language = "English",
volume = "114",
pages = "38 -- 47",
journal = "Journal of Proteomics",
issn = "1874-3919",
publisher = "Elsevier",

}

Robinson, S, Safavi-Hemami, H, Raghuraman, SC, Imperial, JS, Papenfuss, AT, Teichert, RW, Purcell, AW, Olivera, BM & Norton, RS 2015, 'Discovery by proteogenomics and characterization of an RF-amide neuropeptide from cone snail venom' Journal of Proteomics, vol. 114, pp. 38 - 47. https://doi.org/10.1016/j.jprot.2014.11.003

Discovery by proteogenomics and characterization of an RF-amide neuropeptide from cone snail venom. / Robinson, Samuel; Safavi-Hemami, Helena; Raghuraman, Shrinivasan Cheenu; Imperial, Julita S; Papenfuss, Anthony Troy; Teichert, Russell W; Purcell, Anthony Wayne; Olivera, Baldomero Marquez; Norton, Raymond Stanley.

In: Journal of Proteomics, Vol. 114, 2015, p. 38 - 47.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - Discovery by proteogenomics and characterization of an RF-amide neuropeptide from cone snail venom

AU - Robinson, Samuel

AU - Safavi-Hemami, Helena

AU - Raghuraman, Shrinivasan Cheenu

AU - Imperial, Julita S

AU - Papenfuss, Anthony Troy

AU - Teichert, Russell W

AU - Purcell, Anthony Wayne

AU - Olivera, Baldomero Marquez

AU - Norton, Raymond Stanley

PY - 2015

Y1 - 2015

N2 - 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.

AB - 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.

UR - http://www.sciencedirect.com/science/article/pii/S1874391914005168/pdfft?md5=829270994a6b8202864fa39f94047bfc&pid=1-s2.0-S1874391914005168-main.pdf

U2 - 10.1016/j.jprot.2014.11.003

DO - 10.1016/j.jprot.2014.11.003

M3 - Article

VL - 114

SP - 38

EP - 47

JO - Journal of Proteomics

JF - Journal of Proteomics

SN - 1874-3919

ER -

Robinson S, Safavi-Hemami H, Raghuraman SC, Imperial JS, Papenfuss AT, Teichert RW et al. Discovery by proteogenomics and characterization of an RF-amide neuropeptide from cone snail venom. Journal of Proteomics. 2015;114:38 - 47. https://doi.org/10.1016/j.jprot.2014.11.003