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Toxins
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Toxins: From the Wild to the Lab
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Toxins: From the Wild to the Lab

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

Deadline for manuscript submissions: closed (31 December 2024) | Viewed by 11246

Special Issue Editors

Dr. Pascale Marchot

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Guest Editor
Laboratoire Architecture et Fonction des Macromolécules Biologiques (AFMB), CNRS/Aix-Marseille Université, Faculté des Sciences—Campus Luminy, F-13288 Marseille, CEDEX 09, France
Interests: animal toxins; biochemistry; enzymology; imine toxin; molecular toxinology; neurobiology; neuroscience; pathology; pharmacology; phycotoxins; physiology; snake venom; structure-function relationships; synapses
Special Issues, Collections and Topics in MDPI journals
Dr. Evelyne Benoit

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Guest Editor
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
Dr. Sylvie Diochot

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Guest Editor
Institut de Pharmacologie Moléculaire et Cellulaire, Université Côte d’Azur, CNRS UMR7275, INSERM U1323, Sophia Antipolis, F-06560 Valbonne, France
Interests: animal toxins; animal venom; electrophysiology; ion channel; neurobiology; neuropharmacology; neurophysiology; neurotransmission; patch clamp
Special Issues, Collections and Topics in MDPI journals

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 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

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

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Published Papers (6 papers)

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Research

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20 pages, 3411 KiB  
Article
Veratridine Induces Vasorelaxation in Mouse Cecocolic Mesenteric Arteries
by Joohee Park, Christina Sahyoun, Jacinthe Frangieh, Léa Réthoré, Coralyne Proux, Linda Grimaud, Emilie Vessières, Jennifer Bourreau, César Mattei, Daniel Henrion, Céline Marionneau, Ziad Fajloun, Claire Legendre and Christian Legros
Toxins 2024, 16(12), 533; https://doi.org/10.3390/toxins16120533 - 10 Dec 2024
Viewed by 1250
Abstract
The vegetal alkaloid toxin veratridine (VTD) is a selective voltage-gated Na+ (NaV) channel activator, widely used as a pharmacological tool in vascular physiology. We have previously shown that NaV channels, expressed in arteries, contribute to vascular tone in mouse [...] Read more.
The vegetal alkaloid toxin veratridine (VTD) is a selective voltage-gated Na+ (NaV) channel activator, widely used as a pharmacological tool in vascular physiology. We have previously shown that NaV channels, expressed in arteries, contribute to vascular tone in mouse mesenteric arteries (MAs). Here, we aimed to better characterize the mechanisms of action of VTD using mouse cecocolic arteries (CAs), a model of resistance artery. Using wire myography, we found that VTD induced vasorelaxation in mouse CAs. This VTD-induced relaxation was insensitive to prazosin, an α1-adrenergic receptor antagonist, but abolished by atropine, a muscarinic receptor antagonist. Indeed, VTD–vasorelaxant effect was totally inhibited by the NaV channel blocker tetrodotoxin (0.3 µM), the NO synthase inhibitor L-NNA (20 µM), and low extracellular Na+ concentration (14.9 mM) and was partially blocked by the NCX1 antagonist SEA0400 (45.4% at 1 µM). Thus, we assumed that the VTD-induced vasorelaxation in CAs was due to acetylcholine release by parasympathetic neurons, which induced NO synthase activation mediated by the NCX1-Ca2+ entry mode in endothelial cells (ECs). We demonstrated NCX1 expression in ECs by RT-qPCR and immunohisto- and western immunolabelling. VTD did not induce an increase in intracellular Ca2+ ([Ca2+]i), while SEA0400 partially blocked acetylcholine-triggered [Ca2+]i elevations in Mile Sven 1 ECs. Altogether, these results illustrate that VTD activates NaV channels in parasympathetic neurons and then vasorelaxation in resistance arteries, which could explain arterial hypotension after VTD intoxication. Full article
(This article belongs to the Special Issue Toxins: From the Wild to the Lab)
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20 pages, 9763 KiB  
Article
Stable Convergent Polyneuronal Innervation and Altered Synapse Elimination in Orbicularis oculi Muscles from Patients with Blepharospasm Responding Poorly to Recurrent Botulinum Type-A Neurotoxin Injections
by Brigitte Girard, Aurélie Couesnon, Emmanuelle Girard and Jordi Molgó
Toxins 2024, 16(12), 506; https://doi.org/10.3390/toxins16120506 - 24 Nov 2024
Viewed by 1289
Abstract
Botulinum neurotoxin type-A (BoNT/A), which blocks quantal acetylcholine (ACh) release at the neuromuscular junction (NMJ), has demonstrated its efficacy in the symptomatic treatment of blepharospasm. In 3.89% of patients treated for blepharospasm at Tenon Hospital, BoNT/A was no longer effective in relieving the [...] Read more.
Botulinum neurotoxin type-A (BoNT/A), which blocks quantal acetylcholine (ACh) release at the neuromuscular junction (NMJ), has demonstrated its efficacy in the symptomatic treatment of blepharospasm. In 3.89% of patients treated for blepharospasm at Tenon Hospital, BoNT/A was no longer effective in relieving the patient’s symptoms, and a partial upper myectomy of the Orbicularis oculi muscle was performed. We used surgical waste samples from 14 patients treated with repeated injections of either abobotulinumtoxinA (Dysport®) or incobotulinumtoxinA (Xeomin®). These muscle fragments were compared to others from 4 normal subjects, naïve of BoNT/A. The morphological study was performed blinded to the BoNT/A treatment and between treated and control samples. Neuromuscular specimens analyzed by confocal laser scanning microscopy, using fluorescent staining and immune-labeling of presynaptic proteins, revealed that the pattern of innervation (e.g., polyneuronal and convergent innervation), the muscle nicotinic ACh receptors (nAChRs), and the NMJs exhibited marked differences in BoNT/A-treated muscles (regardless of the toxin clinically used), with respect to controls. BoNT/A-treated junctions exhibited profuse polyneuronal innervation in which 2–6 axons innervated 74.84% of single muscle fibers, while 99.47% of control junctions were mono-innervated. Another new finding was the stable convergent innervation, in which several motor axons end onto the same endplate. Morphological signs of synapse elimination included the presence of retraction bulbs in axons and nerve terminals and a reduced extension of postsynaptic nAChRs. These outcomes suggest that synapse elimination is altered and raise questions on the origin and factors contributing to the plasticity changes observed and the functioning of NMJs. Full article
(This article belongs to the Special Issue Toxins: From the Wild to the Lab)
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14 pages, 2730 KiB  
Article
Rattlesnake Crotalphine Analgesic Active on Tetrodotoxin-Sensitive Na+ Current in Mouse Dorsal Root Ganglion Neurons
by Aurélie Antunes, Philippe Robin, Gilles Mourier, Rémy Béroud, Michel De Waard, Denis Servent and Evelyne Benoit
Toxins 2024, 16(8), 359; https://doi.org/10.3390/toxins16080359 - 15 Aug 2024
Viewed by 1455
Abstract
Crotalphine is an analgesic peptide identified from the venom of the South American rattlesnake Crotalus durissus terrificus. Although its antinociceptive effect is well documented, its direct mechanisms of action are still unclear. The aim of the present work was to study the [...] Read more.
Crotalphine is an analgesic peptide identified from the venom of the South American rattlesnake Crotalus durissus terrificus. Although its antinociceptive effect is well documented, its direct mechanisms of action are still unclear. The aim of the present work was to study the action of the crotalid peptide on the NaV1.7 channel subtype, a genetically validated pain target. To this purpose, the effects of crotalphine were evaluated on the NaV1.7 component of the tetrodotoxin-sensitive Na+ current in the dorsal root ganglion neurons of adult mice, using the whole-cell patch-clamp configuration, and on cell viability, using propidium iodide fluorescence and trypan blue assays. The results show that 18.7 µM of peptide inhibited 50% of the Na+ current. The blocking effect occurred without any marked change in the current activation and inactivation kinetics, but it was more important as the membrane potential was more positive. In addition, crotalphine induced an increase in the leakage current amplitude of approximately 150% and led to a maximal 31% decrease in cell viability at a high 50 µM concentration. Taken together, these results point out, for the first time, the effectiveness of crotalphine in acting on the NaV1.7 channel subtype, which may be an additional target contributing to the peptide analgesic properties and, also, although less efficiently, on a second cell plasma membrane component, leading to cell loss. Full article
(This article belongs to the Special Issue Toxins: From the Wild to the Lab)
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27 pages, 7788 KiB  
Article
Viper Venom Phospholipase A2 Database: The Structural and Functional Anatomy of a Primary Toxin in Envenomation
by Ana L. Novo de Oliveira, Miguel T. Lacerda, Maria J. Ramos and Pedro A. Fernandes
Toxins 2024, 16(2), 71; https://doi.org/10.3390/toxins16020071 - 1 Feb 2024
Cited by 8 | Viewed by 3385 | Correction
Abstract
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)
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Review

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18 pages, 3279 KiB  
Review
Rattlesnake Roundup: Point-of-Care Thrombelastographic Methods Define the Molecular Impacts on Coagulation of Crotalus Venom Toxins In Vitro and In Vivo
by Vance G. Nielsen
Toxins 2025, 17(2), 87; https://doi.org/10.3390/toxins17020087 - 13 Feb 2025
Viewed by 595
Abstract
A malalignment between rattlesnake-envenomed patients’ degree of compromised coagulation and the data generated by standard hematological determinations generated with blood samples anticoagulated with calcium (Ca) chelating agents is almost certain. Many rattlesnake venom toxins are Ca-independent toxins that likely continue to damage plasmatic [...] Read more.
A malalignment between rattlesnake-envenomed patients’ degree of compromised coagulation and the data generated by standard hematological determinations generated with blood samples anticoagulated with calcium (Ca) chelating agents is almost certain. Many rattlesnake venom toxins are Ca-independent toxins that likely continue to damage plasmatic and cellular components of coagulation in blood samples (anticoagulated with Ca chelation) during transportation from the emergency department to the clinical laboratory. The most straightforward approach to abrogate this patient–laboratory malalignment is to reduce “needle to activation time”—the time from blood collection to commencement of laboratory analysis—with utilization of point-of-care (POC) technology such as thrombelastography. The workflow and history of standard and POC approaches to hematological assessment is reviewed. Further, using a preclinical model of envenomation with four different rattlesnake venoms, the remarkably diverse damage to coagulation revealed with POC thrombelastography is presented. It is anticipated that future investigation and potential changes in clinical monitoring practices with POC methods of hematological assessment will improve the management of envenomed patients and assist in precision care. Full article
(This article belongs to the Special Issue Toxins: From the Wild to the Lab)
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Other

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34 pages, 21874 KiB  
Conference Report
Report from the 29th Meeting on Toxinology, “Toxins: From the Wild to the Lab”, Organized by the French Society of Toxinology on 30 November–1 December 2023
by Pascale Marchot, Ziad Fajloun, Christian Legros, Évelyne Benoit and Sylvie Diochot
Toxins 2024, 16(3), 147; https://doi.org/10.3390/toxins16030147 - 13 Mar 2024
Cited by 1 | Viewed by 2076
Abstract
The French Society of Toxinology (SFET), which celebrated its 30th anniversary this year, organized its 29th annual Meeting (RT29), shared by 87 participants, on 30 November–1 December 2023. The RT29 main theme, “Toxins: From the Wild to the Lab”, focused on research in [...] Read more.
The French Society of Toxinology (SFET), which celebrated its 30th anniversary this year, organized its 29th annual Meeting (RT29), shared by 87 participants, on 30 November–1 December 2023. The RT29 main theme, “Toxins: From the Wild to the Lab”, focused on research in the field of animal venoms and animal, bacterial, fungal, or plant toxins, from their discovery in nature to their study in the laboratory. The exploration of the functions of toxins, their structures, their molecular or cellular ligands, their mode of action, and their potential therapeutic applications were emphasized during oral communications and posters through three sessions, of which each was dedicated to a secondary theme. A fourth, “miscellaneous” session allowed participants to present recent out-of-theme works. The abstracts of nine invited and 15 selected lectures, those of 24 posters, and the names of the Best Oral Communication and Best Poster awardees, are presented in this report. Full article
(This article belongs to the Special Issue Toxins: From the Wild to the Lab)
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