ArticleMolecular & cellular proteomics : MCP2014
Various conotoxin diversifications revealed by a venomic study of Conus flavidus.
Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 40 citations in OpenAlex.
- Comparative analysis of venom genes in the chromosome-level genomes of two closely related cone snails.BMC genomics · 2026Article
- Proteomic analysis of the venom of Conus flavidus from Red Sea reveals potential pharmacological applications.Journal, genetic engineering & biotechnology · 2024Article
- Article
- Biomaterials and Bioactive Natural Products from Marine Invertebrates: From Basic Research to Innovative Applications.Marine drugs · 2022Review
- Article
- The genome of the venomous snail Lautoconus ventricosus sheds light on the origin of conotoxin diversity.GigaScience · 2021Article
- Proteomic analysis of Red SeaThe journal of venomous animals and toxins including tropical diseases · 2021Article
- Identification of Conomarphin Variants in theMarine drugs · 2020Article
- Transcriptomic Profiling Reveals Extraordinary Diversity of Venom Peptides in Unexplored Predatory Gastropods of the Genus Clavus.Genome biology and evolution · 2020Article
- Discovery Methodology of Novel Conotoxins fromMarine drugs · 2018Review
- Conotoxin Diversity in Chelyconus ermineus (Born, 1778) and the Convergent Origin of Piscivory in the Atlantic and Indo-Pacific Cones.Genome biology and evolution · 2018Article
- Venomics-Accelerated Cone Snail Venom Peptide Discovery.International journal of molecular sciences · 2018Review
- A Transcriptomic Survey of Ion Channel-Based Conotoxins in the Chinese Tubular Cone Snail (Conus betulinus).Marine drugs · 2017Article
- Identification of a Novel O-Conotoxin Reveals an Unusual and Potent Inhibitor of the Human α9α10 Nicotinic Acetylcholine Receptor.Marine drugs · 2017Article
- Article
- Rapid expansion of the protein disulfide isomerase gene family facilitates the folding of venom peptides.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Why do we study animal toxins?Dong wu xue yan jiu = Zoological research · 2015Review
- Conotoxin gene superfamilies.Marine drugs · 2014Review
- Structure and function of μ-conotoxins, peptide-based sodium channel blockers with analgesic activity.Future medicinal chemistry · 2014Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Conotoxins are peptide neurotoxins produced by predatory cone snails. They are mostly cysteine-rich short peptides with remarkable structural diversity. The conserved signal peptide sequences of their mRNA-encoded precursors have enabled the grouping of known conotoxins into a limited number of superfamilies. However, the conotoxins within each superfamily often present variable sequences, cysteine frameworks, and post-translational modifications. To understand better how conotoxins are diversified, we performed a venomic study with C. flavidus, an uninvestigated vermivorous Conus species, by combining transcriptomic and proteomic analyses. In order to obtain the full-length conotoxin sequences, protease digestion was not performed with the venom extraction prior to spectra acquisition via tandem mass spectrometry (MS/MS). Because conotoxins are produced from mRNA-encoded precursors by means of proteolytic cleavage, nonspecific digestion of precursors was applied during the database search. Special attention was also paid in interpreting the MS/MS spectra. All together, these analyses identified 69 nonredundant cDNA sequences and 31 conotoxin components with confident MS/MS spectra. A new Q-superfamily was also identified. More importantly, this study revealed that conotoxin-encoding transcripts are diversified by hypermutation, fragment insertion/deletion, and mutation-induced premature termination, and that a single mRNA species can produce multiple toxin products through alternative post-translational modifications and alternative cleavages of the translated precursor. These multiple diversification strategies at different levels may explain, at least in part, the diversity of conotoxins, and provide the basis for further investigation.
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