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Toxins
Special Issues
Insights into the Action and Application of Animal Toxins
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Insights into the Action and Application of Animal Toxins

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

Deadline for manuscript submissions: closed (31 July 2022) | Viewed by 6779

Special Issue Editor

Prof. Dr. Woei-Jer Chuang

E-Mail Website
Guest Editor
Department of Biochemistry and Molecular Biology, College of Medicine, National Cheng Kung University, Tainan 70101, Taiwan
Interests: protein engineering; structure-based drug design; protein biotechnology; structural biology; disintegrin/integrin; fibronectin type III domain; streptococcal pyrogenic exotoxin B

Special Issue Information

Dear Colleagues,

Animal venom consists of a mixture of biologically and pharmacologically active components, such as salts, micro-molecules, macro-molecules, peptides, and proteins, which are known as toxins. Venomous creatures such as snakes, scorpions, spiders, wasps, and honeybees produce toxins, used predominantly for capturing their prey and self-defense. Despite posing a threat to human health, animal toxins appear to be a promising candidate for various disease therapies and a useful pharmacological tool for target validation. The unique characteristic of being highly target-specific and selective makes animal toxins a very important tool which can be employed for carrying out various physiological, biochemical, and pathological studies that may contribute to the development of new therapies.

In this present era, much of the research interest has focused on the acquisition/collection of venom, active component isolation, and exploration of toxins’ effectiveness in targeting specific molecular mechanisms and/or pathways. Additionally, numerous pre-clinical and clinical trials have indicated the possible efficacy of venom and their bioactive components/chemicals in disease therapy. Venom possesses great pharmacological activities such as anti-inflammatory, anti-diabetic, anti-arthritic, and neuroprotective characteristics, as well as cardio-protective effects, derived from their bioactive chemicals. The enormous biodiversity of toxin-producing species presents a plethora of different types of venom that need to be further explored and analyzed for their therapeutic potential. 

This Special Issue of Toxins, entitled, “Insights into the Action and Application of Animal Toxins”, aims to enhance the contemporary understanding of animal toxins. We welcome all original research articles focused on animal toxins that may be relevant to their biological functions and therapeutic applications, as well as to elucidation of the structure-activity relationships of these proteins. We hope that researchers will share their valuable studies on the actions and applications of animal toxins.

Prof. Dr. Woei-Jer Chuang
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

  • animal toxin
  • therapeutic applications
  • pharmacology
  • drug discovery
  • bioactive proteins and peptides
  • molecular mechanism
  • venom
  • snake
  • scorpion
  • spider

Published Papers (3 papers)

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Research

15 pages, 1547 KiB  
Article
In Vitro Toxicity of Chinese Russell’s Viper (Daboia siamensis) Venom and Neutralisation by Antivenoms
by Mimi Lay, Qing Liang, Geoffrey K. Isbister and Wayne C. Hodgson
Toxins 2022, 14(7), 505; https://doi.org/10.3390/toxins14070505 - 20 Jul 2022
Cited by 2 | Viewed by 1741
Abstract
Daboia siamensis (Russell’s viper) is a highly venomous and medically important snake in China, as well as much of Asia. There is minimal information on the pharmacological activity of the venom of the Chinese species, and currently no commercially available specific antivenom in [...] Read more.
Daboia siamensis (Russell’s viper) is a highly venomous and medically important snake in China, as well as much of Asia. There is minimal information on the pharmacological activity of the venom of the Chinese species, and currently no commercially available specific antivenom in China. This has led to the use of non-specific antivenoms to treat D. siamensis envenomation. In this study, the in vitro neurotoxicity and myotoxicity of D. siamensis venom was examined and the efficacy of four antivenoms was investigated, including the recently developed Chinese D. siamensis monovalent antivenom (C-DsMAV) and three commercially available antivenoms (Thai D. siamensis (Thai-DsMAV) monovalent antivenom, Deinagkistrodon acutus monovalent antivenom (DaAV), and Gloydius brevicaudus monovalent antivenom (GbAV). D. siamensis venom (10–30 µg/mL) caused the concentration-dependent inhibition of indirect twitches in the chick biventer cervicis nerve muscle preparation, without abolishing contractile responses to exogenous agonists ACh or CCh, indicating pre-synaptic neurotoxicity. Myotoxicity was also evident at these concentrations with inhibition of direct twitches, an increase in baseline tension, and the partial inhibition of ACh, CCh, and KCl responses. The prior addition of C-DsMAV or Thai-DsMAV prevented the neurotoxic and myotoxic activity of D. siamensis venom (10 µg/mL). The addition of non-specific antivenoms (GbAV and DaAV) partially prevented the neurotoxic activity of venom (10 µg/mL) but failed to neutralize the myotoxic effects. We have shown that D. siamensis venom exhibits in vitro weak presynaptic neurotoxicity and myotoxicity, which can be prevented by the pre-addition of the Chinese and Thai Russell’s viper antivenoms. Non-specific antivenoms were poorly efficacious. There should be further development of a monospecific antivenom against D. siamensis envenomation in China. Full article
(This article belongs to the Special Issue Insights into the Action and Application of Animal Toxins)
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17 pages, 1691 KiB  
Article
Melittin Tryptophan Substitution with a Fluorescent Amino Acid Reveals the Structural Basis of Selective Antitumor Effect and Subcellular Localization in Tumor Cells
by Yonghui Lv, Xu Chen, Zhidong Chen, Zhanjun Shang, Yongxiao Li, Wanting Xu, Yuan Mo, Xinpei Wang, Daiyun Xu, Shengbin Li, Zhe Wang, Meiying Wu and Junqing Wang
Toxins 2022, 14(7), 428; https://doi.org/10.3390/toxins14070428 - 22 Jun 2022
Cited by 7 | Viewed by 2065
Abstract
Melittin is a membrane-active peptide with strong anticancer activity against various cancers. Despite decades of research, the role of the singular Trp in the anticancer activity and selectivity of melittin remains poorly understood. Here, we propose a theranostic solution based on the substitution [...] Read more.
Melittin is a membrane-active peptide with strong anticancer activity against various cancers. Despite decades of research, the role of the singular Trp in the anticancer activity and selectivity of melittin remains poorly understood. Here, we propose a theranostic solution based on the substitution of Trp19 with a noncanonical fluorescent amino acid (DapAMCA). The introduction of DapAMCA residue in melittin stabilized the helical structure of the peptide, as evaluated by circular dichroism spectra and molecular dynamics simulations. In vitro hemolytic and anticancer activity assays revealed that introducing DapAMCA residue in melittin changed its mode of action with the cell membrane, resulting in reduced hemolytic toxicity and an improved the selectivity index (SI), with up to a five-fold increase compared to melittin. In vitro fluorescence imaging of DapAMCA-labeled melittin (MELFL) in cancer cells demonstrated high membrane-penetrating activity, with strong nuclear and nucleolar localization ability. These findings provide implications for novel anticancer therapies based on Trp-substituted designs and nuclear/nucleolar targeted therapy. Full article
(This article belongs to the Special Issue Insights into the Action and Application of Animal Toxins)
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20 pages, 6271 KiB  
Article
Clinical and Evolutionary Implications of Dynamic Coagulotoxicity Divergences in Bothrops (Lancehead Pit Viper) Venoms
by Lachlan Allan Bourke, Christina N. Zdenek, Anita Mitico Tanaka-Azevedo, Giovanni Perez Machado Silveira, Sávio Stefanini Sant’Anna, Kathleen Fernandes Grego, Caroline Fabri Bittencourt Rodrigues and Bryan Grieg Fry
Toxins 2022, 14(5), 297; https://doi.org/10.3390/toxins14050297 - 22 Apr 2022
Cited by 8 | Viewed by 2440
Abstract
Despite coagulotoxicity being a primary weapon for prey capture by Bothrops species (lancehead pit vipers) and coagulopathy being a major lethal clinical effect, a genus-wide comparison has not been undertaken. To fill this knowledge gap, we used thromboelastography to compare 37 venoms, from [...] Read more.
Despite coagulotoxicity being a primary weapon for prey capture by Bothrops species (lancehead pit vipers) and coagulopathy being a major lethal clinical effect, a genus-wide comparison has not been undertaken. To fill this knowledge gap, we used thromboelastography to compare 37 venoms, from across the full range of geography, taxonomy, and ecology, for their action upon whole plasma and isolated fibrinogen. Potent procoagulant toxicity was shown to be the main venom effect of most of the species tested. However, the most basal species (B. pictus) was strongly anticoagulant; this is consistent with procoagulant toxicity being a novel trait that evolved within Bothrops subsequent to their split from anticoagulant American pit vipers. Intriguingly, two of the arboreal species studied (B. bilineatus and B. taeniatus) lacked procoagulant venom, suggesting differential evolutionary selection pressures. Notably, some terrestrial species have secondarily lost the procoagulant venom trait: the Mogi Mirim, Brazil locality of B. alternatus; San Andres, Mexico locality of B. asper; B. diporus; and the São Roque of B. jararaca. Direct action on fibrinogen was extremely variable; this is consistent with previous hypotheses regarding it being evolutionary decoupled due to procoagulant toxicity being the primary prey-capture weapon. However, human patients live long enough for fibrinogen depletion to be clinically significant. The extreme variability may be reflective of antivenom variability, with these results thereby providing a foundation for such future work of clinical relevance. Similarly, the venom diversification trends relative to ecological niche will also be useful for integration with natural history data, to reconstruct the evolutionary pressures shaping the venoms of these fascinating snakes. Full article
(This article belongs to the Special Issue Insights into the Action and Application of Animal Toxins)
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