Special Issue "Animal Venoms and Their Components: Molecular Mechanisms of Action"

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

Deadline for manuscript submissions: 31 May 2020.

Special Issue Editor

Prof. Yuri N. Utkin
E-Mail Website
Guest Editor
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia
Interests: Isolation of proteins with new structural and pharmacological properties from animal venoms. Investigation of chemical and spatial structures of biologically active peptides and proteins, in particular animal toxins. Studying the mechanism of the ligand-receptor interaction. Elucidation of the general principles of protein recognition for particular cases of the neuroreceptor interactions with neuropeptides and neurotoxins. Characterization of ligand-binding sites in neuroreceptors as a prerequisite for rational drug design.

Special Issue Information

Dear Colleagues,

Animal venoms comprise numerous toxins, which, in turn, comprise peptides and proteins. In prey, these toxins affect various vitally important systems that may result in severe illness or death. During evolution, 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.

Prof. Yuri N. Utkin
Guest Editor

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

Open AccessArticle
Identification and Characterization of ShSPI, a Kazal-Type Elastase Inhibitor from the Venom of Scolopendra Hainanum
Toxins 2019, 11(12), 708; https://doi.org/10.3390/toxins11120708 - 05 Dec 2019
Abstract
Elastase is a globular glycoprotein and belongs to the chymotrypsin family. It is involved in several inflammatory cascades on the basis of cleaving the important connective tissue protein elastin, and is strictly regulated to a balance by several endogenous inhibitors. When elastase and [...] Read more.
Elastase is a globular glycoprotein and belongs to the chymotrypsin family. It is involved in several inflammatory cascades on the basis of cleaving the important connective tissue protein elastin, and is strictly regulated to a balance by several endogenous inhibitors. When elastase and its inhibitors are out of balance, severe diseases will develop, especially those involved in the cardiopulmonary system. Much attention has been attracted in seeking innovative elastase inhibitors and various advancements have been taken on clinical trials of these inhibitors. Natural functional peptides from venomous animals have been shown to have anti-protease properties. Here, we identified a kazal-type serine protease inhibitor named ShSPI from the cDNA library of the venom glands of Scolopendra hainanum. ShSPI showed significant inhibitory effects on porcine pancreatic elastase and human neutrophils elastase with Ki values of 225.83 ± 20 nM and 12.61 ± 2 nM, respectively. Together, our results suggest that ShSPI may be an excellent candidate to develop a drug for cardiopulmonary diseases. Full article
(This article belongs to the Special Issue Animal Venoms and Their Components: Molecular Mechanisms of Action)
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Open AccessArticle
The Latoia consocia Caterpillar Induces Pain by Targeting Nociceptive Ion Channel TRPV1
Toxins 2019, 11(12), 695; https://doi.org/10.3390/toxins11120695 - 27 Nov 2019
Abstract
Accidental contact with caterpillar bristles causes local symptoms such as severe pain, intense heat, edema, erythema, and pruritus. However, there is little functional evidence to indicate a potential mechanism. In this study, we analyzed the biological characteristics of the crude venom from the [...] Read more.
Accidental contact with caterpillar bristles causes local symptoms such as severe pain, intense heat, edema, erythema, and pruritus. However, there is little functional evidence to indicate a potential mechanism. In this study, we analyzed the biological characteristics of the crude venom from the larval stage of Latoia consocia living in South-West China. Intraplantar injection of the venom into the hind paws of mice induced severe acute pain behaviors in wild type (WT) mice; the responses were much reduced in TRPV1-deficit (TRPV1 KO) mice. The TRPV1-specific inhibitor, capsazepine, significantly attenuated the pain behaviors. Furthermore, the crude venom evoked strong calcium signals in the dorsal root ganglion (DRG) neurons of WT mice but not those of TRPV1 KO mice. Among the pain-related ion channels we tested, the crude venom only activated the TRPV1 channel. To better understand the venom components, we analyzed the transcriptome of the L. consocia sebaceous gland region. Our study suggests that TRPV1 serves as a primary nociceptor in caterpillar-induced pain and forms the foundation for elucidating the pain-producing mechanism. Full article
(This article belongs to the Special Issue Animal Venoms and Their Components: Molecular Mechanisms of Action)
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Open AccessArticle
Cloning and Immunosuppressive Properties of an Acyl-Activating Enzyme from the Venom Apparatus of Tetrastichus brontispae (Hymenoptera: Eulophidae)
Toxins 2019, 11(11), 672; https://doi.org/10.3390/toxins11110672 - 18 Nov 2019
Abstract
Venom injected into the host plays vital roles in facilitating successful parasitization and development for parasitoid wasps, especially those devoid of polydnavirus, and the abundant venom proteins appear to be most likely involved in parasitization success. Previously, we found the four most abundant [...] Read more.
Venom injected into the host plays vital roles in facilitating successful parasitization and development for parasitoid wasps, especially those devoid of polydnavirus, and the abundant venom proteins appear to be most likely involved in parasitization success. Previously, we found the four most abundant venom proteins, including 4-coumarate:CoA ligase-like 4 (4CL4-like), in the Tetrastichus brontispae (Hymenoptera: Eulophidae) venom apparatus. In this study, we cloned, expressed T. brontispae 4CL4-like (Tb4CL4-like) in Escherichia coli, and investigated its immunosuppressive properties. The deduced amino acid sequence for Tb4CL4-like shares high identity at conserved amino acids associated with the acyl-activating enzyme (AAE) consensus motif but shows only <40% identity with the members in the AAE superfamily. mRNA abundance analysis indicated that Tb4CL4-like was transcribed mainly in the venom apparatus. Recombinant Tb4CL4-like inhibited Octodonta nipae (Coleoptera: Chrysomelidae) pupal cellular encapsulation and spreading by targeting the hemocyte cytoskeleton and reduced the hemocyte-mediated phagocytosis of E. coli in vivo. Moreover, Tb4CL4-like exhibited greater affinity to palmitic acid and linolenic acid based on the molecular docking assay and is hypothesized to be involved in fatty acid metabolism. In conclusion, our results suggest that Tb4CL4-like may be an immunity-related AAE protein that is involved in the regulation of host immunity through fatty acid metabolism-derived signaling pathways. Full article
(This article belongs to the Special Issue Animal Venoms and Their Components: Molecular Mechanisms of Action)
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Open AccessArticle
An Antiviral Peptide from Alopecosa nagpag Spider Targets NS2B–NS3 Protease of Flaviviruses
Toxins 2019, 11(10), 584; https://doi.org/10.3390/toxins11100584 - 10 Oct 2019
Abstract
Flaviviruses are single-stranded RNA viruses predominantly transmitted by the widely distributed Aedes mosquitoes in nature. As important human pathogens, the geographic reach of Flaviviruses and their threats to public health are increasing, but there is currently no approved specific drug for treatment. In [...] Read more.
Flaviviruses are single-stranded RNA viruses predominantly transmitted by the widely distributed Aedes mosquitoes in nature. As important human pathogens, the geographic reach of Flaviviruses and their threats to public health are increasing, but there is currently no approved specific drug for treatment. In recent years, the development of peptide antivirals has gained much attention. Natural host defense peptides which uniquely evolved to protect the hosts have been shown to have antiviral properties. In this study, we firstly collected the venom of the Alopecosa nagpag spider from Shangri-La County, Yunnan Province. A defense peptide named Av-LCTX-An1a (Antiviral-Lycotoxin-An1a) was identified from the spider venom, and its anti-dengue serotype-2 virus (DENV2) activity was verified in vitro. Moreover, a real-time fluorescence-based protease inhibition assay showed that An1a functions as a DENV2 NS2B–NS3 protease inhibitor. Furthermore, we also found that An1a restricts zika virus (ZIKV) infection by inhibiting the ZIKV NS2B–NS3 protease. Together, our findings not only demonstrate that An1a might be a candidate for anti-flavivirus drug but also indicate that spider venom is a potential resource library rich in antiviral precursor molecules. Full article
(This article belongs to the Special Issue Animal Venoms and Their Components: Molecular Mechanisms of Action)
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Open AccessArticle
In Vitro and In Vivo Antimalarial Activity of LZ1, a Peptide Derived from Snake Cathelicidin
Toxins 2019, 11(7), 379; https://doi.org/10.3390/toxins11070379 - 30 Jun 2019
Abstract
Antimalarial drug resistance is an enormous global threat. Recently, antimicrobial peptides (AMPs) are emerging as a new source of antimalarials. In this study, an AMP LZ1 derived from snake cathelicidin was identified with antimalarial activity. In the in vitro antiplasmodial assay, LZ1 showed [...] Read more.
Antimalarial drug resistance is an enormous global threat. Recently, antimicrobial peptides (AMPs) are emerging as a new source of antimalarials. In this study, an AMP LZ1 derived from snake cathelicidin was identified with antimalarial activity. In the in vitro antiplasmodial assay, LZ1 showed strong suppression of blood stage Plasmodium falciparum (P. falciparum) with an IC50 value of 3.045 μM. In the in vivo antiplasmodial assay, LZ1 exerted a significant antimalarial activity against Plasmodium berghei (P. berghei) in a dose- and a time- dependent manner. In addition, LZ1 exhibited anti-inflammatory effects and attenuated liver-function impairment during P. berghei infection. Furthermore, by employing inhibitors against glycolysis and oxidative phosphorylation in erythrocytes, LZ1 specifically inhibited adenosine triphosphate (ATP) production in parasite-infected erythrocyte by selectively inhibiting the pyruvate kinase activity. In conclusion, the present study demonstrates that LZ1 is a potential candidate for novel antimalarials development. Full article
(This article belongs to the Special Issue Animal Venoms and Their Components: Molecular Mechanisms of Action)
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