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Animal Venoms and Their Components: Molecular Mechanisms of Action v...
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Animal Venoms and Their Components: Molecular Mechanisms of Action v 2.0

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

Deadline for manuscript submissions: closed (30 September 2023) | Viewed by 9703

Special Issue Editor

Dr. Yuri Utkin

E-Mail Website
Guest Editor
Laboratory of Molecular Toxinology, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia
Interests: nicotinic acetylcholine receptor; venoms; snake; scorpion; animal toxins
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

This is a second version of the previous Special Issue, which attracted 23 papers on various aspects of the molecular mechanisms underlying the action of animal venoms and toxins. This Special Issue also intends to unite papers on the molecular basis of the action of venoms and toxins in one issue. As animal venoms comprise numerous toxins of different natures, the mechanisms of their action are quite diverse, which requires the application of different approaches and methods for investigation. In prey, venoms and toxins affect various vitally important systems that may result in severe illness or death. During evolution, animal toxins acquired the ability to bind selectively and with high affinity to biological targets in organisms. However, at present, not all toxin targets have been identified, and not all the molecular mechanisms underlying the effects of toxins are understood. This understanding is very important for the efficient treatment of envenomation, which still continues to be a significant problem. On the other hand, their high selectivity and efficiency make toxins valuable molecular tools for fundamental research. Moreover, toxins with known mechanisms of action may serve as templates for drug development. All this suggests that studying the molecular mechanisms of action of animal venoms and their toxins is a very challenging but important task. The aim of this Special Issue of Toxins is to present a modern understanding of the various aspects of the molecular mechanisms underlying the action of animal venoms and their components. 

Dr. Yuri Utkin
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

  • venom
  • snake
  • scorpion
  • spider
  • marine snail
  • jelly fish
  • sea anemone
  • toxin
  • biological target
  • molecular mechanism

Published Papers (5 papers)

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Research

13 pages, 1459 KiB  
Article
Effects of the Heterodimeric Neurotoxic Phospholipase A2 from the Venom of Vipera nikolskii on the Contractility of Rat Papillary Muscles and Thoracic Aortas
by Alexey Averin, Vladislav Starkov, Victor Tsetlin and Yuri Utkin
Toxins 2024, 16(2), 100; https://doi.org/10.3390/toxins16020100 - 10 Feb 2024
Viewed by 1413
Abstract
Phospholipases A2 (PLA2s) are a large family of snake toxins manifesting diverse biological effects, which are not always related to phospholipolytic activity. Snake venom PLA2s (svPLA2s) are extracellular proteins with a molecular mass of 13–14 kDa. [...] Read more.
Phospholipases A2 (PLA2s) are a large family of snake toxins manifesting diverse biological effects, which are not always related to phospholipolytic activity. Snake venom PLA2s (svPLA2s) are extracellular proteins with a molecular mass of 13–14 kDa. They are present in venoms in the form of monomers, dimers, and larger oligomers. The cardiovascular system is one of the multiple svPLA2 targets in prey organisms. The results obtained previously on the cardiovascular effects of monomeric svPLA2s were inconsistent, while the data on the dimeric svPLA2 crotoxin from the rattlesnake Crotalus durissus terrificus showed that it significantly reduced the contractile force of guinea pig hearts. Here, we studied the effects of the heterodimeric svPLA2 HDP-1 from the viper Vipera nikolskii on papillary muscle (PM) contractility and the tension of the aortic rings (ARs). HDP-1 is structurally different from crotoxin, and over a wide range of concentrations, it produced a long-term, stable, positive inotropic effect in PMs, which did not turn into contractures at the concentrations studied. This also distinguishes HDP-1 from the monomeric svPLA2s, which at high concentrations inhibited cardiac function. HDP-1, when acting on ARs preconstricted with 10 μM phenylephrine, induced a vasorelaxant effect, similar to some other svPLA2s. These are the first indications of the cardiac and vascular effects of true vipers’ heterodimeric svPLA2s. Full article
(This article belongs to the Special Issue Animal Venoms and Their Components: Molecular Mechanisms of Action v 2.0)
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21 pages, 14253 KiB  
Article
Proteomic Profiling of Extracellular Vesicles Isolated from Plasma and Peritoneal Exudate in Mice Induced by Crotalus scutulatus scutulatus Crude Venom and Its Purified Cysteine-Rich Secretory Protein (Css-CRiSP)
by Armando Reyes, Joseph D. Hatcher, Emelyn Salazar, Jacob Galan, Anton Iliuk, Elda E. Sanchez and Montamas Suntravat
Toxins 2023, 15(7), 434; https://doi.org/10.3390/toxins15070434 - 02 Jul 2023
Cited by 1 | Viewed by 1883
Abstract
Increased vascular permeability is a frequent outcome of viperid snakebite envenomation, leading to local and systemic complications. We reported that snake venom cysteine-rich secretory proteins (svCRiSPs) from North American pit vipers increase vascular permeability both in vitro and in vivo. They also induce [...] Read more.
Increased vascular permeability is a frequent outcome of viperid snakebite envenomation, leading to local and systemic complications. We reported that snake venom cysteine-rich secretory proteins (svCRiSPs) from North American pit vipers increase vascular permeability both in vitro and in vivo. They also induce acute activation of several adhesion and signaling molecules that may play a critical role in the pathophysiology of snakebites. Extracellular vesicles (EVs) have gained interest for their diverse functions in intercellular communication, regulating cellular processes, blood-endothelium interactions, vascular permeability, and immune modulation. They also hold potential as valuable biomarkers for diagnosing, predicting, and monitoring therapeutic responses in different diseases. This study aimed to identify proteins in peritoneal exudate and plasma EVs isolated from BALB/c mice following a 30 min post-injection of Crotalus scutulatus scutulatus venom and its purified CRiSP (Css-CRiSP). EVs were isolated from these biofluids using the EVtrap method. Proteomic analysis of exudate- and plasma-derived EVs was performed using LC-MS/MS. We observed significant upregulation or downregulation of proteins involved in cell adhesion, cytoskeleton rearrangement, signal transduction, immune responses, and vesicle-mediated transports. These findings suggest that svCRiSPs play a crucial role in the acute effects of venom and contribute to the local and systemic toxicity of snakebites. Full article
(This article belongs to the Special Issue Animal Venoms and Their Components: Molecular Mechanisms of Action v 2.0)
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14 pages, 5467 KiB  
Article
Functional Characterization of a New Degradation Peptide BmTX4-P1 from Traditional Chinese Scorpion Medicinal Material
by Chenhu Qin, Xuhua Yang, Yuanyuan Zhang, Gang Deng, Xin Huang, Zheng Zuo, Fang Sun, Zhijian Cao, Zongyun Chen and Yingliang Wu
Toxins 2023, 15(5), 340; https://doi.org/10.3390/toxins15050340 - 15 May 2023
Cited by 1 | Viewed by 1227
Abstract
Thermally processed Buthus martensii Karsch scorpion is an important traditional Chinese medical material that has been widely used to treat various diseases in China for over one thousand years. Our recent work showed that thermally processed Buthus martensii Karsch scorpions contain many degraded [...] Read more.
Thermally processed Buthus martensii Karsch scorpion is an important traditional Chinese medical material that has been widely used to treat various diseases in China for over one thousand years. Our recent work showed that thermally processed Buthus martensii Karsch scorpions contain many degraded peptides; however, the pharmacological activities of these peptides remain to be studied. Here, a new degraded peptide, BmTX4-P1, was identified from processed Buthus martensii Karsch scorpions. Compared with the venom-derived wild-type toxin peptide BmTX4, BmTX4-P1 missed some amino acids at the N-terminal and C-terminal regions, while containing six conserved cysteine residues, which could be used to form disulfide bond-stabilized α-helical and β-sheet motifs. Two methods (chemical synthesis and recombinant expression) were used to obtain the BmTX4-P1 peptide, named sBmTX4-P1 and rBmTX4-P1. Electrophysiological experimental results showed that sBmTX4-P1 and rBmTX4-P1 exhibited similar activities to inhibit the currents of hKv1.2 and hKv1.3 channels. In addition, the experimental electrophysiological results of recombinant mutant peptides of BmTX4-P1 indicated that the two residues of BmTX4-P1 (Lys22 and Tyr31) were the key residues for its potassium channel inhibitory activity. In addition to identifying a new degraded peptide, BmTX4-P1, from traditional Chinese scorpion medicinal material with high inhibitory activities against the hKv1.2 and hKv1.3 channels, this study also provided a useful method to obtain the detailed degraded peptides from processed Buthus martensii Karsch scorpions. Thus, the study laid a solid foundation for further research on the medicinal function of these degraded peptides. Full article
(This article belongs to the Special Issue Animal Venoms and Their Components: Molecular Mechanisms of Action v 2.0)
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20 pages, 1388 KiB  
Article
In Silico Study of the Mechanisms Underlying the Action of the Snake Natriuretic-Like Peptide Lebetin 2 during Cardiac Ischemia
by Hinda Allaoui, Nedra Rached, Naziha Marrakchi, Ameur Cherif, Amor Mosbah and Erij Messadi
Toxins 2022, 14(11), 787; https://doi.org/10.3390/toxins14110787 - 11 Nov 2022
Cited by 3 | Viewed by 1653
Abstract
Lebetin 2 (L2), a natriuretic-like peptide (NP), exerts potent cardioprotection in myocardial infarction (MI), with stronger effects than B-type natriuretic peptide (BNP). To determine the molecular mechanisms underlying its cardioprotection effect, we used molecular modeling, molecular docking and molecular dynamics (MD) simulation to [...] Read more.
Lebetin 2 (L2), a natriuretic-like peptide (NP), exerts potent cardioprotection in myocardial infarction (MI), with stronger effects than B-type natriuretic peptide (BNP). To determine the molecular mechanisms underlying its cardioprotection effect, we used molecular modeling, molecular docking and molecular dynamics (MD) simulation to describe the binding mode, key interaction residues as well as mechanistic insights into L2 interaction with NP receptors (NPRs). L2 binding affinity was determined for human, rat, mouse and chicken NPRs, and the stability of receptor–ligand complexes ascertained during 100 ns-long MD simulations. We found that L2 exhibited higher affinity for all human NPRs compared to BNP, with a rank preference for NPR-A > NPR-C > NPR-B. Moreover, L2 affinity for human NPR-A and NPR-C was higher in other species. Both docking and MD studies revealed that the NPR-C–L2 interaction was stronger in all species compared to BNP. Due to its higher affinity to human receptors, L2 could be used as a therapeutic approach in MI patients. Moreover, the stronger interaction of L2 with NPR-C could highlight a new L2 signaling pathway that would explain its additional effects during cardiac ischemia. Thus, L2 is a promising candidate for drug design toward novel compounds with high potency, affinity and stability. Full article
(This article belongs to the Special Issue Animal Venoms and Their Components: Molecular Mechanisms of Action v 2.0)
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24 pages, 3761 KiB  
Article
Diversity of Phospholipases A2 from Bothrops atrox Snake Venom: Adaptive Advantages for Snakes Compromising Treatments for Snakebite Patients
by Leijiane F. Sousa, Amanda P. Freitas, Bruna L. Cardoso, Tiago H. M. Del-Rei, Vanessa A. Mendes, Daniele P. Oréfice, Marisa M. T. Rocha, Benedito C. Prezoto and Ana M. Moura-da-Silva
Toxins 2022, 14(8), 543; https://doi.org/10.3390/toxins14080543 - 08 Aug 2022
Cited by 1 | Viewed by 2727
Abstract
The evolution of snake venoms resulted in multigene toxin families that code for structurally similar isoforms eventually harboring distinct functions. PLA2s are dominant toxins in viper venoms, and little is known about the impact of their diversity on human envenomings and [...] Read more.
The evolution of snake venoms resulted in multigene toxin families that code for structurally similar isoforms eventually harboring distinct functions. PLA2s are dominant toxins in viper venoms, and little is known about the impact of their diversity on human envenomings and neutralization by antivenoms. Here, we show the isolation of three distinct PLA2s from B. atrox venom. FA1 is a Lys-49 homologue, and FA3 and FA4 are catalytic Asp-49 PLA2s. FA1 and FA3 are basic myotoxic proteins, while FA4 is an acid non-myotoxic PLA2. FA3 was the most potent toxin, inducing higher levels of edema, inflammatory nociception, indirect hemolysis, and anticoagulant activity on human, rat, and chicken plasmas. FA4 presented lower anticoagulant activity, and FA1 had only a slight effect on human and rat plasmas. PLA2s presented differential reactivities with antivenoms, with an emphasis on FA3, which was not recognized or neutralized by the antivenoms used in this study. Our findings reveal the functional and antigenic diversity among PLA2s from B. atrox venom, highlighting the importance of assessing venom variability for understanding human envenomations and treatment with antivenoms, particularly evident here as the antivenom fails to recognize FA3, the most active multifunctional toxin described. Full article
(This article belongs to the Special Issue Animal Venoms and Their Components: Molecular Mechanisms of Action v 2.0)
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