Special Issue "Animal Poisons and Venoms in Drug Discovery"

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

Deadline for manuscript submissions: 31 December 2021.

Special Issue Editors

Dr. Antonio Garcia Soares
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Guest Editor
Department of Cellular and Integrative Physiology, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229-3900, USA
Interests: Pharmacology; Toxicology; Ion channels; Electrophysiology; Kidney diseases, Hypertension, Cardiovascular function
Dr. Tarek Mohamed Abd El-Aziz
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Guest Editor
1. Department of Cellular and Integrative Physiology, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229-3900, USA
2. Zoology Department, Faculty of Science, Minia University, El-Minia 61519, Egypt
Interests: animal venoms and toxins; drug discovery; ion channels and membrane receptors; electrophysiology; pharmacology; snakebite; antivenom production

Special Issue Information

Dear Colleagues,

The development of new drugs represents one of the biggest challenging activities of the pharmaceutical industry. Since the middle of the 20th century, a growing number of potential therapeutic agents have been extracted and isolated from plants, animal venoms, and microorganism toxins. While the preliminary effort with regard to animal poisons and venoms was to understand the effects of snake and spider bites and scorpion stings on humans and to elaborate the action of the toxins, toxins from animal poisons and venoms display wide-ranging pharmacological activities, targeting mainly ion channels, membrane receptors, and components of the hemostatic system with high selectivity and affinity. Animal poisons and venoms are complex chemical mixtures of biologically active proteins. Animal venom components were also understood to be medical tools for thousands of years in Ayurveda, homeopathy, and traditional/folk medicine for the treatment of a variety of pathophysiological conditions.

In the past few decades, several potential drugs in use or in clinical trials have been isolated or derived from animal venoms. Since 1981, 10 toxin-based molecules have received FDA approval, five from snakes (Captopril, Tirofiban, Eptifibatide, Batroxobin, and Cobratide), two from lizards (Exenatide and Lixisenatide), two from leeches (Bivalirudin and Desirudin), and one from cone snails (Ziconotide). Many additional animal venom components are also currently in different clinical stages as therapeutic drugs.

This Special Issue of Toxins on “Animal Poisons and Venoms in Drug Discovery” aims to provide a comprehensive view not only of snake venom but also several other animal toxins having therapeutic potential for drug discovery. We welcome all research including original research articles, reviews, and short communications focused on the characterization, pharmacology, and therapeutic applications of animal poisons and venoms and their subcomponents. We hope that researchers will share their valuable studies using snake venoms for drug development.

Dr. Antonio Garcia Soares
Dr. Tarek Mohamed Abd El-Aziz
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 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 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

  • Animal poisons and venoms
  • Bioactive proteins and peptides
  • Drug discovery
  • Pharmacology
  • Therapeutic applications
  • Ion channels
  • Membrane proteins
  • Antimicrobial agents

Published Papers (4 papers)

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Research

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Article
Phosphoproteomics Identifies Significant Biomarkers Associated with the Proliferation and Metastasis of Prostate Cancer
Toxins 2021, 13(8), 554; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13080554 - 09 Aug 2021
Viewed by 799
Abstract
The spider peptide toxins HNTX-III and JZTX-I are a specific inhibitor and activator of TTX-S VGSCs, respectively. They play important roles in regulating MAT-LyLu cell metastasis in prostate cancer. In order to identify key biomarkers involved in the regulation of MAT-LyLu cell metastasis, [...] Read more.
The spider peptide toxins HNTX-III and JZTX-I are a specific inhibitor and activator of TTX-S VGSCs, respectively. They play important roles in regulating MAT-LyLu cell metastasis in prostate cancer. In order to identify key biomarkers involved in the regulation of MAT-LyLu cell metastasis, iTRAQ-based quantitative phosphoproteomics analysis was performed on cells treated with HNTX-III, JZTX-I and blank. A total of 554 unique phosphorylated proteins and 1779 distinct phosphorylated proteins were identified, while 55 and 36 phosphorylated proteins were identified as differentially expressed proteins in HNTX-III and JZTX-I treated groups compared with control groups. Multiple bioinformatics analysis based on quantitative phosphoproteomics data suggested that the differentially expressed phosphorylated proteins and peptides were significantly associated with the migration and invasion of prostate tumors. Specifically, the toxins HNTX-III and JZTX-I have opposite effects on tumor formation and metastasis by regulating the expression and phosphorylation level of causal proteins. Herein, we highlighted three key proteins EEF2, U2AF2 and FLNC which were down-regulated in HNTX-III treated cells and up-regulated in JZTX-I treated cells. They played significant roles in cancer related physiological and pathological processes. The differentially expressed phosphorylated proteins identified in this study may serve as potential biomarkers for precision medicine for prostate cancer in the near future. Full article
(This article belongs to the Special Issue Animal Poisons and Venoms in Drug Discovery)
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Article
Identification and Characterization of Novel Proteins from Arizona Bark Scorpion Venom That Inhibit Nav1.8, a Voltage-Gated Sodium Channel Regulator of Pain Signaling
Toxins 2021, 13(7), 501; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13070501 - 18 Jul 2021
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Abstract
The voltage-gated sodium channel Nav1.8 is linked to neuropathic and inflammatory pain, highlighting the potential to serve as a drug target. However, the biophysical mechanisms that regulate Nav1.8 activation and inactivation gating are not completely understood. Progress has been hindered by a lack [...] Read more.
The voltage-gated sodium channel Nav1.8 is linked to neuropathic and inflammatory pain, highlighting the potential to serve as a drug target. However, the biophysical mechanisms that regulate Nav1.8 activation and inactivation gating are not completely understood. Progress has been hindered by a lack of biochemical tools for examining Nav1.8 gating mechanisms. Arizona bark scorpion (Centruroides sculpturatus) venom proteins inhibit Nav1.8 and block pain in grasshopper mice (Onychomys torridus). These proteins provide tools for examining Nav1.8 structure–activity relationships. To identify proteins that inhibit Nav1.8 activity, venom samples were fractioned using liquid chromatography (reversed-phase and ion exchange). A recombinant Nav1.8 clone expressed in ND7/23 cells was used to identify subfractions that inhibited Nav1.8 Na+ current. Mass-spectrometry-based bottom-up proteomic analyses identified unique peptides from inhibitory subfractions. A search of the peptides against the AZ bark scorpion venom gland transcriptome revealed four novel proteins between 40 and 60% conserved with venom proteins from scorpions in four genera (Centruroides, Parabuthus, Androctonus, and Tityus). Ranging from 63 to 82 amino acids, each primary structure includes eight cysteines and a “CXCE” motif, where X = an aromatic residue (tryptophan, tyrosine, or phenylalanine). Electrophysiology data demonstrated that the inhibitory effects of bioactive subfractions can be removed by hyperpolarizing the channels, suggesting that proteins may function as gating modifiers as opposed to pore blockers. Full article
(This article belongs to the Special Issue Animal Poisons and Venoms in Drug Discovery)
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Article
Identification of a Novel Cathelicidin from the Deinagkistrodon acutus Genome with Antibacterial Activity by Multiple Mechanisms
Toxins 2020, 12(12), 771; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins12120771 - 04 Dec 2020
Viewed by 716
Abstract
The abuse of antibiotics and the consequent increase of drug-resistant bacteria constitute a serious threat to human health, and new antibiotics are urgently needed. Research shows that antimicrobial peptides produced by natural organisms are potential substitutes for antibiotics. Based on Deinagkistrodonacutus (known [...] Read more.
The abuse of antibiotics and the consequent increase of drug-resistant bacteria constitute a serious threat to human health, and new antibiotics are urgently needed. Research shows that antimicrobial peptides produced by natural organisms are potential substitutes for antibiotics. Based on Deinagkistrodonacutus (known as five-pacer viper) genome bioinformatics analysis, we discovered a new cathelicidin antibacterial peptide which was called FP-CATH. Circular dichromatic analysis showed a typical helical structure. FP-CATH showed broad-spectrum antibacterial activity. It has antibacterial activity to Gram-negative bacteria and Gram-positive bacteria including methicillin-resistant Staphylococcus aureus (MRSA). The results of transmission electron microscopy (TEM) and scanning electron microscopy (SEM) showed that FP-CATH could cause the change of bacterial cell integrity, having a destructive effect on Gram-negative bacteria and inducing Gram-positive bacterial surface formation of vesicular structure. FP-CATH could bind to LPS and showed strong binding ability to bacterial DNA. In vivo, FP-CATH can improve the survival rate of nematodes in bacterial invasion experiments, and has a certain protective effect on nematodes. To sum up, FP-CATH is likely to play a role in multiple mechanisms of antibacterial action by impacting bacterial cell integrity and binding to bacterial biomolecules. It is hoped that the study of FP-CATH antibacterial mechanisms will prove useful for development of novel antibiotics. Full article
(This article belongs to the Special Issue Animal Poisons and Venoms in Drug Discovery)
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Review

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Review
The Search for Natural and Synthetic Inhibitors That Would Complement Antivenoms as Therapeutics for Snakebite Envenoming
Toxins 2021, 13(7), 451; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13070451 - 29 Jun 2021
Cited by 2 | Viewed by 1125
Abstract
A global strategy, under the coordination of the World Health Organization, is being unfolded to reduce the impact of snakebite envenoming. One of the pillars of this strategy is to ensure safe and effective treatments. The mainstay in the therapy of snakebite envenoming [...] Read more.
A global strategy, under the coordination of the World Health Organization, is being unfolded to reduce the impact of snakebite envenoming. One of the pillars of this strategy is to ensure safe and effective treatments. The mainstay in the therapy of snakebite envenoming is the administration of animal-derived antivenoms. In addition, new therapeutic options are being explored, including recombinant antibodies and natural and synthetic toxin inhibitors. In this review, snake venom toxins are classified in terms of their abundance and toxicity, and priority actions are being proposed in the search for snake venom metalloproteinase (SVMP), phospholipase A2 (PLA2), three-finger toxin (3FTx), and serine proteinase (SVSP) inhibitors. Natural inhibitors include compounds isolated from plants, animal sera, and mast cells, whereas synthetic inhibitors comprise a wide range of molecules of a variable chemical nature. Some of the most promising inhibitors, especially SVMP and PLA2 inhibitors, have been developed for other diseases and are being repurposed for snakebite envenoming. In addition, the search for drugs aimed at controlling endogenous processes generated in the course of envenoming is being pursued. The present review summarizes some of the most promising developments in this field and discusses issues that need to be considered for the effective translation of this knowledge to improve therapies for tackling snakebite envenoming. Full article
(This article belongs to the Special Issue Animal Poisons and Venoms in Drug Discovery)
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