Toxins: From the Wild to the Lab

A special issue of Toxins (ISSN 2072-6651).

Deadline for manuscript submissions: 30 June 2024 | Viewed by 612

Special Issue Editors

Laboratoire Architecture et Fonction des Macromolécules Biologiques (AFMB), Faculté des Sciences—Campus Luminy, CNRS (Centre National de la Recherche Scientifique)/Aix‐Marseille Université, F-13288 Marseille, CEDEX 09, France
Interests: the structure-function relationships of enzymes; macromolecular receptors and cell-adhesion molecules
CEA, Institut des Sciences du Vivant Frédéric Joliot, Département Médicaments et Technologies pour la Santé (DMTS), Service d’Ingénierie Moléculaire pour la Santé (SIMoS), Université Paris-Saclay, EMR 9004 CNRS/CEA, F-91191 Gif-sur-Yvette, France
Interests: toxins; voltage-gated sodium channels; voltage-gated potassium channels; voltage-gated calcium channels; nicotinic acetylcholine receptors; venom toxins; marine toxins; bacterial toxins
Special Issues, Collections and Topics in MDPI journals
IPMC (Institut de Pharmacologie Moléculaire et Cellulaire), LabEx ICST (Laboratory of Excellence “Ion Channel Science and Therapeutics”), FHU InovPain (Fédération Hospitalo-Universitaire “Innovative Solutions in Refractory Chronic Pain”), Université Côte d’Azur, CNRS (Centre National de la Recherche Scientifique), 660 Route des Lucioles, Sophia-Antipolis, F-06560 Nice, France
Interests: pharmacology of ion channels (ASICs, Cav, TRP, 5-HT3 channels) related to pain using animal toxins; purification of new peptidic toxins from venoms

Special Issue Information

Dear Colleagues,

Natural substances have been of interest for several centuries, and many toxins of animal, plant, bacterial, or fungal origins have been identified and characterized. There is a long way to go, from finding venomous species in their natural habitat, through collecting their venom under strict safety and species preservation conditions, to the extraction of natural toxins in the laboratory. State-of-the-art technologies are making it possible to explore, as close as possible to their site of action, the functioning of these tools on a molecular level and to design some of them that will contribute to the development and progress of diagnostic medicine or therapeutics.

In this Special Issue of the journal Toxins, titled “Toxins: From the Wild to the Lab”, research and review articles concerning the latest discoveries in the field of venoms and toxinology will be presented to cover broad areas ranging from the composition and evolution of venoms to the mechanism of action, structural conservation versus variability, and therapeutic applicability of toxins. This Special Issue is open, albeit not restricted, to the communications that were presented during the 29th Meeting of Toxinology (RT29) organized by the French Society of Toxinology (SFET) on the 30th of November and 1st of December 2023 at the Institut Pasteur of Paris.

Dr. Pascale Marchot
Dr. Evelyne Benoit
Dr. Sylvie Diochot
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at 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.


  • animal toxin
  • bacterial toxin
  • marine toxin
  • toxinomics
  • venomics
  • structure–function interactions
  • therapeutic drugs

Published Papers (1 paper)

Order results
Result details
Select all
Export citation of selected articles as:


27 pages, 7782 KiB  
Viper Venom Phospholipase A2 Database: The Structural and Functional Anatomy of a Primary Toxin in Envenomation
Toxins 2024, 16(2), 71; - 01 Feb 2024
Viewed by 461
Viper venom phospholipase A2 enzymes (vvPLA2s) and phospholipase A2-like (PLA2-like) proteins are two of the principal toxins in viper venom that are responsible for the severe myotoxic and neurotoxic effects caused by snakebite envenoming, among other pathologies. As snakebite envenoming is the deadliest [...] Read more.
Viper venom phospholipase A2 enzymes (vvPLA2s) and phospholipase A2-like (PLA2-like) proteins are two of the principal toxins in viper venom that are responsible for the severe myotoxic and neurotoxic effects caused by snakebite envenoming, among other pathologies. As snakebite envenoming is the deadliest neglected tropical disease, a complete understanding of these proteins’ properties and their mechanisms of action is urgently needed. Therefore, we created a database comprising information on the holo-form, cofactor-bound 3D structure of 217 vvPLA2 and PLA2-like proteins in their physiologic environment, as well as 79 membrane-bound viper species from 24 genera, which we have made available to the scientific community to accelerate the development of new anti-snakebite drugs. In addition, the analysis of the sequenced, 3D structure of the database proteins reveals essential aspects of the anatomy of the proteins, their toxicity mechanisms, and the conserved binding site areas that may anchor universal interspecific inhibitors. Moreover, it pinpoints hypotheses for the molecular origin of the myotoxicity of the PLA2-like proteins. Altogether, this study provides an understanding of the diversity of these toxins and how they are conserved, and it indicates how to develop broad, interspecies, efficient small-molecule inhibitors to target the toxin’s many mechanisms of action. Full article
(This article belongs to the Special Issue Toxins: From the Wild to the Lab)
Show Figures

Figure 1

Back to TopTop