Special Issue "Venoms-Based Marine Drug Discovery: Proteomic and Transcriptomic Approaches"

A special issue of Marine Drugs (ISSN 1660-3397).

Deadline for manuscript submissions: closed (30 September 2020).

Special Issue Editors

Dr. Sebastien Dutertre
E-Mail Website
Guest Editor
Institut des Biomolécules Max Mousseron, UMR 5247, Université Montpellier, CNRS, Place Eugène Bataillon, 34095 Montpellier CEDEX 5, France
Interests: venoms; conotoxins; peptides; proteomics; transcriptomics; drug discovery
Special Issues, Collections and Topics in MDPI journals
Dr. Maria Vittoria Modica
E-Mail Website
Guest Editor
Department of Biology and Evolution of Marine Organisms, Stazione Zoologica Anton Dohrn, Villa Comunale, 80121 Naples, Italy
Interests: phylogeny; evolution; adaptations; venoms; transcriptomics; proteomics

Special Issue Information

Dear Colleagues,

Venomous marine organisms such as anemones, worms, fishes, corals, cone snails or snakes produce complex bioactive secretions in specialized glands and delivered through diverse anatomical structures that are used to subdue their preys or deter predators. These animal venoms have evolved through millions of years of natural selection, in a co-evolutionary process involving the prey and the predator, often referred to as an “arms race”. As such, they are extremely efficient and usually effective at a very low concentration via highly specific interactions with key physiological targets (ion channels, enzymes, and membrane components). The potency, specificity, and speed with which venom molecules interact with their molecular targets make them ideal candidates for therapeutic and biotechnological developments. Among the venom-derived drugs that are currently approved or in trial for human use, a major breakthrough from marine organisms includes the Ziconotide from a cone snail toxin, which has caused a paradigm shift in analgesic drug development, and the Dalazatide from a sea anemone toxin used to treat autoimmune diseases. However, the marine realm is still an underexplored environment, hosting a high number of venomous species that have been overlooked to date with respect to the composition and variability of their venom, and which could provide novel drug leads. In this Special Issue, we welcome any investigations of marine venomous creatures that employ transcriptomic and proteomic approaches.

Dr. Sebastien Dutertre
Dr. Maria Vittoria Modica
Guest Editors

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 papers will be 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 single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Marine Drugs 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 2400 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

  • transcriptomics
  • proteomics
  • venom
  • pharmacology
  • toxin

Published Papers (2 papers)

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Research

Article
Synthesis, Structural and Pharmacological Characterizations of CIC, a Novel α-Conotoxin with an Extended N-Terminal Tail
Mar. Drugs 2021, 19(3), 141; https://doi.org/10.3390/md19030141 - 02 Mar 2021
Viewed by 930
Abstract
Cone snails are venomous marine predators that rely on fast-acting venom to subdue their prey and defend against aggressors. The conotoxins produced in the venom gland are small disulfide-rich peptides with high affinity and selectivity for their pharmacological targets. A dominant group comprises [...] Read more.
Cone snails are venomous marine predators that rely on fast-acting venom to subdue their prey and defend against aggressors. The conotoxins produced in the venom gland are small disulfide-rich peptides with high affinity and selectivity for their pharmacological targets. A dominant group comprises α-conotoxins, targeting nicotinic acetylcholine receptors. Here, we report on the synthesis, structure determination and biological activity of a novel α-conotoxin, CIC, found in the predatory venom of the piscivorous species Conus catus and its truncated mutant Δ-CIC. CIC is a 4/7 α-conotoxin with an unusual extended N-terminal tail. High-resolution NMR spectroscopy shows a major influence of the N-terminal tail on the apparent rigidity of the three-dimensional structure of CIC compared to the more flexible Δ-CIC. Surprisingly, this effect on the structure does not alter the biological activity, since both peptides selectively inhibit α3β2 and α6/α3β2β3 nAChRs with almost identical sub- to low micromolar inhibition constants. Our results suggest that the N-terminal part of α-conotoxins can accommodate chemical modifications without affecting their pharmacology. Full article
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Article
Proteo-Transcriptomic Analysis Identifies Potential Novel Toxins Secreted by the Predatory, Prey-Piercing Ribbon Worm Amphiporus lactifloreus
Mar. Drugs 2020, 18(8), 407; https://doi.org/10.3390/md18080407 - 01 Aug 2020
Cited by 7 | Viewed by 1872
Abstract
Nemerteans (ribbon worms) employ toxins to subdue their prey, but research thus far has focused on the small-molecule components of mucus secretions and few protein toxins have been characterized. We carried out a preliminary proteotranscriptomic analysis of putative toxins produced by the hoplonemertean [...] Read more.
Nemerteans (ribbon worms) employ toxins to subdue their prey, but research thus far has focused on the small-molecule components of mucus secretions and few protein toxins have been characterized. We carried out a preliminary proteotranscriptomic analysis of putative toxins produced by the hoplonemertean Amphiporus lactifloreus (Hoplonemertea, Amphiporidae). No variants were found of known nemertean-specific toxin proteins (neurotoxins, cytotoxins, parbolysins or nemertides) but several toxin-like transcripts were discovered, expressed strongly in the proboscis, including putative metalloproteinases and sequences resembling sea anemone actitoxins, crown-of-thorn sea star plancitoxins, and multiple classes of inhibitor cystine knot/knottin family proteins. Some of these products were also directly identified in the mucus proteome, supporting their preliminary identification as secreted toxin components. Two new nemertean-typical toxin candidates could be described and were named U-nemertotoxin-1 and U-nemertotoxin-2. Our findings provide insight into the largely overlooked venom system of nemerteans and support a hypothesis in which the nemertean proboscis evolved in several steps from a flesh-melting organ in scavenging nemerteans to a flesh-melting and toxin-secreting venom apparatus in hunting hoplonemerteans. Full article
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