Structure, Function and Evolution of Conotoxins

A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Animal Venoms".

Deadline for manuscript submissions: 31 July 2025 | Viewed by 1286

Special Issue Editors


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Guest Editor
Department of Biology, Linderstrøm-Lang Centre for Protein Science, University of Copenhagen, 2200 Copenhagen, Denmark
Interests: Conotoxins; structure-function relationships; recombinant expression systems for animal toxins; disulfide-bond formation

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Guest Editor
University of Utah School of MedicineThis link is disabled., Salt Lake City, UT, USA
Interests: peptide analysis; molecular biology; neuropeptide and GPCR signaling; bioinformatics; cell culture

Special Issue Information

Dear Colleagues,

Marine snails of the genus Conus produce complex venoms that contain a wide variety of bioactive peptide toxins, known as conotoxins. Conotoxins are highly diverse in sequence and are rich in disulfide bonds that are crucial for structural stability. They often target cell surface receptors and channels to disrupt prey physiology. In recent years, we have seen a surge in available toxin sequence data obtained using transcriptomics and proteomics approaches. This vast resource presents a range of exciting possibilities for the field, but at the same time illuminates the relative paucity of available structural and functional information.

This Special Issue is dedicated to research that expands our knowledge about conotoxin structure, function, and evolution, and the intriguing interplay between the three. Covering a broad range of topics, this Special Issue will include papers that investigate conotoxins from poorly characterized toxin families, as well as detailed accounts of structure–function relationships in toxins from well-known families. We also encourage submissions that describe conoidean toxins other than conotoxins within these same overarching topics. Moreover, we welcome contributions describing the development of new methodologies concerning, for instance, the production of conotoxins, the identification of their molecular targets, the analysis of post-translational modifications, and the improved structural prediction of disulfide-rich peptides. Review articles that describe existing knowledge and present current challenges in the field, as well as ideas for future research, are encouraged. 

Prof. Dr. Lars Ellgaard
Dr. Thomas Lund Koch
Guest Editors

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Keywords

  • conotoxins
  • conoidean toxins
  • disulfide bonds
  • functional assays
  • molecular evolution
  • phylogenetics
  • structure–activity relationship
  • structure determination
  • structure prediction

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Published Papers (1 paper)

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Research

26 pages, 5099 KiB  
Article
Potential Ancestral Conoidean Toxins in the Venom Cocktail of the Carnivorous Snail Raphitoma purpurea (Montagu, 1803) (Neogastropoda: Raphitomidae)
by Giacomo Chiappa, Giulia Fassio, Maria Vittoria Modica and Marco Oliverio
Toxins 2024, 16(8), 348; https://doi.org/10.3390/toxins16080348 - 9 Aug 2024
Viewed by 969
Abstract
Venomous marine gastropods of the superfamily Conoidea possess a rich arsenal of toxins, including neuroactive toxins. Venom adaptations might have played a fundamental role in the radiation of conoideans; nevertheless, there is still no knowledge about the venom of the most diversified family [...] Read more.
Venomous marine gastropods of the superfamily Conoidea possess a rich arsenal of toxins, including neuroactive toxins. Venom adaptations might have played a fundamental role in the radiation of conoideans; nevertheless, there is still no knowledge about the venom of the most diversified family of the group: Raphitomidae Bellardi, 1875. In this study, transcriptomes were produced from the carcase, salivary glands, and proximal and distal venom ducts of the northeastern Atlantic species Raphitoma purpurea (Montagu, 1803). Using a gut barcoding approach, we were also able to report, for the first time, molecular evidence of a vermivorous diet for the genus. Transcriptomic analyses revealed over a hundred putative venom components (PVC), including 69 neurotoxins. Twenty novel toxin families, including some with high levels of expansion, were discovered. No significant difference was observed between the distal and proximal venom duct secretions. Peptides related to cone snail toxins (Cerm06, Pgam02, and turritoxin) and other venom-related proteins (disulfide isomerase and elevenin) were retrieved from the salivary glands. These salivary venom components may constitute ancestral adaptations for venom production in conoideans. Although often neglected, salivary gland secretions are of extreme importance for understanding the evolutionary history of conoidean venom. Full article
(This article belongs to the Special Issue Structure, Function and Evolution of Conotoxins)
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