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Toxins
Special Issues
Predatory and Defensive Venom Peptides
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Predatory and Defensive Venom Peptides

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

Deadline for manuscript submissions: closed (15 December 2022) | Viewed by 6843

Special Issue Editor

Prof. Dr. Richard J. Lewis

E-Mail Website1 Website2
Guest Editor
Institute for Molecular Bioscience, The University of Queensland, Brisbane Qld 4072, Australia
Interests: conotoxins; ciguatoxins; structure–function; therapeutic development; pain
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Venomous plants and animals have evolved a suite of venom peptide toxins that target a broad diversity of membrane proteins, including ion channels, GPCRs, and transporters, typically with exquisite potency and selectivity. Only recently have we started to understand which venom peptides have evolved to facilitate prey capture and those optimised and/or repurposed for defence. This Special Issue will accept research publications and authoritative reviews on all aspects relating to the origins, evolution, venomics, structure–function relationship, therapeutic potential, and mode of action of venom peptides evolved for predation or defence.

Prof. Dr. Richard J. Lewis
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a double-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Toxins is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • conotoxins
  • venom peptides
  • disulfide bonds
  • ion channel pharmacology
  • venomics
  • mass spectrometry
  • transcriptomics
  • evolution
  • histology
  • diet diversification

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Published Papers (2 papers)

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Research

19 pages, 2651 KiB  
Article
Venomics Reveals a Non-Compartmentalised Venom Gland in the Early Diverged Vermivorous Conus distans
by Jutty Rajan Prashanth, Sebastien Dutertre, Subash Kumar Rai and Richard J. Lewis
Toxins 2022, 14(3), 226; https://doi.org/10.3390/toxins14030226 - 19 Mar 2022
Cited by 2 | Viewed by 2807
Abstract
The defensive use of cone snail venom is hypothesised to have first arisen in ancestral worm-hunting snails and later repurposed in a compartmentalised venom duct to facilitate the dietary shift to molluscivory and piscivory. Consistent with its placement in a basal lineage, we [...] Read more.
The defensive use of cone snail venom is hypothesised to have first arisen in ancestral worm-hunting snails and later repurposed in a compartmentalised venom duct to facilitate the dietary shift to molluscivory and piscivory. Consistent with its placement in a basal lineage, we demonstrate that the C. distans venom gland lacked distinct compartmentalisation. Transcriptomics revealed C. distans expressed a wide range of structural classes, with inhibitory cysteine knot (ICK)-containing peptides dominating. To better understand the evolution of the venom gland compartmentalisation, we compared C. distans to C. planorbis, the earliest diverging species from which a defence-evoked venom has been obtained, and fish-hunting C. geographus from the Gastridium subgenus that injects distinct defensive and predatory venoms. These comparisons support the hypothesis that venom gland compartmentalisation arose in worm-hunting species and enabled repurposing of venom peptides to facilitate the dietary shift from vermivory to molluscivory and piscivory in more recently diverged cone snail lineages. Full article
(This article belongs to the Special Issue Predatory and Defensive Venom Peptides)
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18 pages, 1766 KiB  
Article
A Combined Transcriptomics and Proteomics Approach Reveals the Differences in the Predatory and Defensive Venoms of the Molluscivorous Cone Snail Cylinder ammiralis (Caenogastropoda: Conidae)
by Samuel Abalde, Sébastien Dutertre and Rafael Zardoya
Toxins 2021, 13(9), 642; https://doi.org/10.3390/toxins13090642 - 10 Sep 2021
Cited by 8 | Viewed by 3316
Abstract
Venoms are complex mixtures of proteins that have evolved repeatedly in the animal kingdom. Cone snail venoms represent one of the best studied venom systems. In nature, this venom can be dynamically adjusted depending on its final purpose, whether to deter predators or [...] Read more.
Venoms are complex mixtures of proteins that have evolved repeatedly in the animal kingdom. Cone snail venoms represent one of the best studied venom systems. In nature, this venom can be dynamically adjusted depending on its final purpose, whether to deter predators or hunt prey. Here, the transcriptome of the venom gland and the proteomes of the predation-evoked and defensive venoms of the molluscivorous cone snail Cylinder ammiralis were catalogued. A total of 242 venom-related transcripts were annotated. The conotoxin superfamilies presenting more different peptides were O1, O2, T, and M, which also showed high expression levels (except T). The three precursors of the J superfamily were also highly expressed. The predation-evoked and defensive venoms showed a markedly distinct profile. A total of 217 different peptides were identified, with half of them being unique to one venom. A total of 59 peptides ascribed to 23 different protein families were found to be exclusive to the predatory venom, including the cono-insulin, which was, for the first time, identified in an injected venom. A total of 43 peptides from 20 protein families were exclusive to the defensive venom. Finally, comparisons of the relative abundance (in terms of number of peptides) of the different conotoxin precursor superfamilies showed that most of them present similar abundance regardless of the diet. Full article
(This article belongs to the Special Issue Predatory and Defensive Venom Peptides)
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