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Toxins
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Animal Venoms: Unraveling the Molecular Complexity (2nd Edition)
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Animal Venoms: Unraveling the Molecular Complexity (2nd Edition)

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

Deadline for manuscript submissions: 30 June 2025 | Viewed by 7854

Special Issue Editors

Prof. Dr. Ren Lai

E-Mail Website
Guest Editor
Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming 650223, China
Interests: toxin; venom; peptide; ion channel; inhibitor; coagulation; neuron
Special Issues, Collections and Topics in MDPI journals
Dr. Qiumin Lu

E-Mail Website
Guest Editor
Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming 650223, China
Interests: animal toxins; structure-function; natural medicines; drug discovery; platelets; thrombus
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

In the different cultures around the world, venomous animals have long sparked a sense of mystery and fear. However, the questions of why animal venoms are toxic and why they can be used for medicinal purposes have always puzzled us. It is now known that animal venoms contain various toxins with specific structures and functions, which is the main answer to the above questions. A large number of studies have shown that these toxins are mainly proteins and peptides. Animal venoms are extremely large resources for animal toxin research, and the vast majority of venomous animals have not yet been explored.

In recent years, omics research on venoms or glands of spiders, conus, scorpions, amphibians, and snakes has shown that the astonishing diversity of peptide toxins is widely present in various venomous animals. This Special Issue aims to provide scholars with the latest research on the diversity of animal toxins: analyzing the molecular diversity of animal venoms, discovering new animal toxins, and elucidating the mechanism of interaction between animal toxins and their targets. To enhance our understanding of these important issues, we encourage experts in the field of animal toxins to contribute research papers and reviews on unraveling the molecular complexity of animal toxins to this Special Issue.

Prof. Dr. Ren Lai
Dr. Qiumin Lu
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

  • venomous animal
  • venom
  • toxin
  • protein
  • peptide
  • receptor
  • ion channel
  • transcriptomics
  • proteomics
  • bioinformatics

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Related Special Issue

Published Papers (5 papers)

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Research

20 pages, 10727 KiB  
Article
α-Latrotoxin Actions in the Absence of Extracellular Ca2+ Require Release of Stored Ca2+
by Jennifer K. Blackburn, Quazi Sufia Islam, Ouafa Benlaouer, Svetlana A. Tonevitskaya, Evelina Petitto and Yuri A. Ushkaryov
Toxins 2025, 17(2), 73; https://doi.org/10.3390/toxins17020073 - 6 Feb 2025
Viewed by 768
Abstract
α-Latrotoxin (αLTX) causes exhaustive release of neurotransmitters from nerve terminals in the absence of extracellular Ca2+ (Ca2+e). To investigate the mechanisms underlying this effect, we loaded mouse neuromuscular junctions with BAPTA-AM. This membrane-permeable Ca2+-chelator demonstrates that Ca [...] Read more.
α-Latrotoxin (αLTX) causes exhaustive release of neurotransmitters from nerve terminals in the absence of extracellular Ca2+ (Ca2+e). To investigate the mechanisms underlying this effect, we loaded mouse neuromuscular junctions with BAPTA-AM. This membrane-permeable Ca2+-chelator demonstrates that Ca2+e-independent effects of αLTX require an increase in cytosolic Ca2+ (Ca2+cyt). We also show that thapsigargin, which depletes Ca2+ stores, induces neurotransmitter release, but inhibits the effect of αLTX. We then studied αLTX’s effects on Ca2+cyt using neuroblastoma cells expressing signaling-capable or signaling-incapable variants of latrophilin-1, a G protein-coupled receptor of αLTX. Our results demonstrate that αLTX acts as a cation ionophore and a latrophilin agonist. In model cells at 0 Ca2+e, αLTX forms membrane pores and allows the influx of Na+; this reverses the Na+-Ca2+ exchanger, leading to the release of stored Ca2+ and inhibition of its extrusion. Concurrently, αLTX stimulates latrophilin signaling, which depletes a Ca2+ store and induces transient opening of Ca2+ channels in the plasmalemma that are sensitive to inhibitors of store-operated Ca2+ entry. These results indicate that Ca2+ release from intracellular stores and that Ca2+ influx through latrophilin-activated store-operated Ca2+ channels contributes to αLTX actions and may be involved in physiological control of neurotransmitter release at nerve terminals. Full article
(This article belongs to the Special Issue Animal Venoms: Unraveling the Molecular Complexity (2nd Edition))
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20 pages, 5295 KiB  
Article
Peptide Toxin Diversity and a Novel Antimicrobial Peptide from the Spider Oxyopes forcipiformis
by Kexin Wang, James Mwangi, Kaixun Cao, Yi Wang, Jinai Gao, Min Yang, Brenda B. Michira, Qiumin Lu and Juan Li
Toxins 2024, 16(11), 466; https://doi.org/10.3390/toxins16110466 - 31 Oct 2024
Viewed by 1555
Abstract
Spider venoms are emerging as a rich source of bioactive peptide toxins with therapeutic potential. Lynx spiders of the genus Oxyopes are small, cursorial hunters that employ complex venom to subdue arthropod prey. However, extracting crude venom from these diminutive arachnids poses significant [...] Read more.
Spider venoms are emerging as a rich source of bioactive peptide toxins with therapeutic potential. Lynx spiders of the genus Oxyopes are small, cursorial hunters that employ complex venom to subdue arthropod prey. However, extracting crude venom from these diminutive arachnids poses significant challenges. This study presents a transcriptome analysis of venom glands from an undescribed Oxyopes forcipiformis species, revealing 339 putative protein and peptide toxin sequences categorized into seven functional groups. The venom composition was dominated by membrane-active peptides (40.71%), venom auxiliary proteins (22.71%), neurotoxins (15.63%), channel active peptides (7.08%) and uncharacterized components (13.87%). Additionally, phylogenetic analysis of 65 disulfide-bond-rich peptides yielded six distinct families based on sequence homology and cysteine framework. Finally, a novel antimicrobial peptide, GK37, was identified using in silico and homology analyses. Our data suggested that GK37 presented significant antibacterial activity against Gram-positive bacteria Staphylococcus aureus with a minimum inhibitory concentration (MIC) of 1.552 µM by disrupting bacterial membranes. At 4× MICs, GK37 almost showed no hemolytic activity on blood cells or toxicity against Hek293T cells. Our findings provided a basis for targeted studies of the diversity and pharmacological effects of lynx spider peptide. We elucidated a valuable high-throughput approach for obtaining proteins and peptides from small-group spiders. Full article
(This article belongs to the Special Issue Animal Venoms: Unraveling the Molecular Complexity (2nd Edition))
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15 pages, 4082 KiB  
Article
From Venom to Vein: Factor VII Activation as a Major Pathophysiological Target for Procoagulant Australian Elapid Snake Venoms
by Uthpala Chandrasekara, Abhinandan Chowdhury, Lorenzo Seneci, Christina N. Zdenek, Nathan Dunstan and Bryan G. Fry
Toxins 2024, 16(10), 430; https://doi.org/10.3390/toxins16100430 - 6 Oct 2024
Cited by 3 | Viewed by 1602
Abstract
Australian elapid snake venoms are uniquely procoagulant, utilizing blood clotting enzyme Factor Xa (FXa) as a toxin, which evolved as a basal trait in this clade. The subsequent recruitment of Factor Va (FVa) as a toxin occurred in the last common ancestor of [...] Read more.
Australian elapid snake venoms are uniquely procoagulant, utilizing blood clotting enzyme Factor Xa (FXa) as a toxin, which evolved as a basal trait in this clade. The subsequent recruitment of Factor Va (FVa) as a toxin occurred in the last common ancestor of taipans (Oxyuranus species) and brown snakes (Pseudonaja species). Factor II (prothrombin) activation has been stated as the primary mechanism for the lethal coagulopathy, but this hypothesis has never been tested. The additional activation of Factor VII (FVII) by Oxyuranus/Pseudonaja venoms has historically been considered as a minor, unimportant novelty. This study aimed to investigate the significance of toxic FVII activation relative to prothrombin activation by testing a wide taxonomical range of Australian elapid species with procoagulant venoms. The activation of FVII or prothrombin, with and without the Factor Va as a cofactor, was assessed, along with the structural changes involved in these processes. All procoagulant species could activate FVII, establishing this as a basal trait. In contrast, only some lineages could activate prothrombin, indicating that this is a derived trait. For species able to activate both zymogens, Factor VII was consistently more strongly activated than prothrombin. FVa was revealed as an essential cofactor for FVII activation, a mechanism previously undocumented. Species lacking FVa in their venom utilized endogenous plasma FVa to exert this activity. The ability of the human FXa:FVa complex to activate FVII was also revealed as a new feedback loop in the endogenous clotting cascade. Toxin sequence analyses identified structural changes essential for the derived trait of prothrombin activation. This study presents a paradigm shift in understanding how elapid venoms activate coagulation factors, highlighting the critical role of FVII activation in the pathophysiological effects upon the coagulation cascade produced by Australian elapid snake venoms. It also documented the novel use of Factor Va as a cofactor for FVII activation for both venom and endogenous forms of FXa. These findings are crucial for developing better antivenoms and treatments for snakebite victims and have broader implications for drug design and the treatment of coagulation disorders. The research also advances the evolutionary biology knowledge of snake venoms. Full article
(This article belongs to the Special Issue Animal Venoms: Unraveling the Molecular Complexity (2nd Edition))
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14 pages, 2179 KiB  
Article
Transcriptomic Analysis Reveals Diverse Expression of Scorpion Toxin Genes in Mesobuthus martensii
by Zhongxian Yang, Haiquan Wang, Yan Zhao, Jianyu Huang, Chao Zhang and Zhiyong Di
Toxins 2024, 16(9), 399; https://doi.org/10.3390/toxins16090399 - 18 Sep 2024
Cited by 1 | Viewed by 1604
Abstract
Scorpions, an ancient group of venomous invertebrates, have existed for over 430 million years. Their toxins, important for predation and defense, exhibit a variety of biological and pharmacological activities. Research on scorpion toxins has spanned decades. Notably, the toxin genes of Mesobuthus martensii [...] Read more.
Scorpions, an ancient group of venomous invertebrates, have existed for over 430 million years. Their toxins, important for predation and defense, exhibit a variety of biological and pharmacological activities. Research on scorpion toxins has spanned decades. Notably, the toxin genes of Mesobuthus martensii (Scorpiones: Buthidae), a well-known Chinese herbal medicine, have been described at genomic and proteomic levels. However, previous studies primarily focused on the toxin genes expressed in the venom glands, overlooking their expression in multiple tissues. This study analyzed transcriptomes from 14 tissues of M. martensii. Gene annotation revealed 83 toxin and toxin-like genes, including those affecting sodium, potassium, calcium, and chloride ion channels. Approximately 70% of toxin genes were highly expressed in the vesicle; additionally, some exhibited low or no expression in the vesicle while showing high expression in other tissues. Beyond the vesicle, high expression levels of toxin genes were observed in metasoma segments II-V, blood, lateral eyes, chelicerae, legs, pedipalp chelae, femurs, and patellae. This expression pattern suggests that toxin genes are recruited from multiple tissues and may help prevent intraspecific harm during courtship and competition for prey. These findings inspire further research into the evolutionary recruitment process of scorpion toxins. Full article
(This article belongs to the Special Issue Animal Venoms: Unraveling the Molecular Complexity (2nd Edition))
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23 pages, 4058 KiB  
Article
Aligning Post-Column ESI-MS, MALDI-MS, and Coagulation Bioassay Data of Naja spp., Ophiophagus hannah, and Pseudonaja textillis Venoms Chromatographically to Assess MALDI-MS and ESI-MS Complementarity with Correlation of Bioactive Toxins to Mass Spectrometric Data
by Haifeng Xu, Susan El-Asal, Hafsa Zakri, Rama Mutlaq, Natascha T. B. Krikke, Nicholas R. Casewell, Julien Slagboom and Jeroen Kool
Toxins 2024, 16(9), 379; https://doi.org/10.3390/toxins16090379 - 29 Aug 2024
Cited by 1 | Viewed by 1500
Abstract
Snakebite is a serious health issue in tropical and subtropical areas of the world and results in various pathologies, such as hemotoxicity, neurotoxicity, and local swelling, blistering, and tissue necrosis around the bite site. These pathologies may ultimately lead to permanent morbidity and [...] Read more.
Snakebite is a serious health issue in tropical and subtropical areas of the world and results in various pathologies, such as hemotoxicity, neurotoxicity, and local swelling, blistering, and tissue necrosis around the bite site. These pathologies may ultimately lead to permanent morbidity and may even be fatal. Understanding the chemical and biological properties of individual snake venom toxins is of great importance when developing a newer generation of safer and more effective snakebite treatments. Two main approaches to ionizing toxins prior to mass spectrometry (MS) analysis are electrospray ionization (ESI) and matrix-assisted laser desorption ionization (MALDI). In the present study, we investigated the use of both ESI-MS and MALDI-MS as complementary techniques for toxin characterization in venom research. We applied nanofractionation analytics to separate crude elapid venoms using reversed-phase liquid chromatography (RPLC) and high-resolution fractionation of the eluting toxins into 384-well plates, followed by online LC-ESI-MS measurements. To acquire clear comparisons between the two ionization approaches, offline MALDI-MS measurements were performed on the nanofractionated toxins. For comparison to the LC-ESI-MS data, we created so-called MALDI-MS chromatograms of each toxin. We also applied plasma coagulation assaying on 384-well plates with nanofractionated toxins to demonstrate parallel biochemical profiling within the workflow. The plotting of post-column acquired MALDI-MS data as so-called plotted MALDI-MS chromatograms to directly align the MALDI-MS data with ESI-MS extracted ion chromatograms allows the efficient correlation of intact mass toxin results from the two MS-based soft ionization approaches with coagulation bioassay chromatograms. This facilitates the efficient correlation of chromatographic bioassay peaks with the MS data. The correlated toxin masses from ESI-MS and/or MALDI-MS were all around 6–8 or 13–14 kDa, with one mass around 20 kDa. Between 24 and 67% of the toxins were observed with good intensity from both ionization methods, depending on the venom analyzed. All Naja venoms analyzed presented anticoagulation activity, whereas pro-coagulation was only observed for the Pseudonaja textillis venom. The data of MALDI-MS can provide complementary identification and characterization power for toxin research on elapid venoms next to ESI-MS. Full article
(This article belongs to the Special Issue Animal Venoms: Unraveling the Molecular Complexity (2nd Edition))
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