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Toxins
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Animal Venoms: Proteomics, Biochemical Activities and Application
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Animal Venoms: Proteomics, Biochemical Activities and Application

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

Deadline for manuscript submissions: closed (6 October 2023) | Viewed by 8714

Special Issue Editors

Dr. Tianfang Wang

E-Mail Website
Guest Editor
Centre for Bioinnovation, University of the Sunshine Coast, Maroochydore, QLD 4558, Australia
Interests: functional proteomics; peptide chemistry; biodiscovery; natural bioactive peptides; computational chemistry
Prof. Dr. Hu Li

E-Mail Website
Guest Editor
Department of Entomology, China Agricultural University, Beijing, China
Interests: DNA Sequencing; genomics; phylogenetic analysis; evolution; population genetics; biodiversity; ecology and evolution; systematics; RNA; taxonomy
Prof. Dr. Scott F. Cummins

E-Mail Website
Guest Editor
Centre for Bioinnovation, University of the Sunshine Coast, Maroochydore, QLD 4558, Australia
Interests: molecular neuroethology; protein pheromones; neuropeptides; functional genomics; invertebrate biology; invasive species

Special Issue Information

Dear Colleagues,

Venoms, found in major animal groups, have evolved into highly effective biochemical weapons, with toxins consisting of important proteins that contribute to the fitness of venomous species. Recent advances in proteomic techniques, particularly mass spectrometry, enable deep exploration of venom proteins and peptides, answering questions about toxin arsenals in different animals, including their origin, post-translational modifications, and interactions with target biomolecules. Additionally, the identification of venom proteins has inspired translational research, showcasing diverse bioactivities that have various potential applications. Since each venom exhibits distinct components of protein, methodologies are needed to enable quantitative MS/proteomic analyses of venom diversity and novel protein functions.  This Special Issue seeks research and review articles covering proteomic analysis, proximity labelling, protein post-translational modifications, and protein–protein interactions within venoms of different animals. Manuscripts focusing on new proteomic strategies, technological innovations in proteomics, and the development of bioassays characterising venom's biochemical activity and potential agrochemical, pharmaceutical, therapeutic, and diagnostic uses are encouraged. We also welcome manuscripts on quantitative proteomics analyses, mass spectrometry imaging combined with spatial transcriptomics, in situ hybridisation techniques, the analysis of intact venom proteins, the application of proteo-transcriptomics, and the development of bioinformatic tools for venom proteomic analysis.

Dr. Tianfang Wang
Prof. Dr. Hu Li
Prof. Dr. Scott F. Cummins
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

  • venom
  • protemics
  • biochemical activity
  • pharmaceutics
  • therapeutics
  • toxin
  • protein
  • peptide
  • post-translational modification

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Published Papers (4 papers)

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Research

12 pages, 3698 KiB  
Article
Proteomic Investigation of Cape Cobra (Naja nivea) Venom Reveals First Evidence of Quaternary Protein Structures
by Lewis O. McFarlane and Tara L. Pukala
Toxins 2024, 16(2), 63; https://doi.org/10.3390/toxins16020063 - 23 Jan 2024
Cited by 3 | Viewed by 1960
Abstract
Naja nivea (N. nivea) is classed as a category one snake by the World Health Organization since its envenomation causes high levels of mortality and disability annually. Despite this, there has been little research into the venom composition of N. nivea, [...] Read more.
Naja nivea (N. nivea) is classed as a category one snake by the World Health Organization since its envenomation causes high levels of mortality and disability annually. Despite this, there has been little research into the venom composition of N. nivea, with only one full venom proteome published to date. Our current study separated N. nivea venom using size exclusion chromatography before utilizing a traditional bottom-up proteomics approach to unravel the composition of the venom proteome. As expected by its clinical presentation, N. nivea venom was found to consist mainly of neurotoxins, with three-finger toxins (3FTx), making up 76.01% of the total venom proteome. Additionally, cysteine-rich secretory proteins (CRISPs), vespryns (VESPs), cobra venom factors (CVFs), 5′-nucleotidases (5′NUCs), nerve growth factors (NGFs), phospholipase A2s (PLA2), acetylcholinesterases (AChEs), Kunitz-type serine protease inhibitor (KUN), phosphodiesterases (PDEs), L-amino acid oxidases (LAAOs), hydrolases (HYDs), snake venom metalloproteinases (SVMPs), and snake venom serine protease (SVSP) toxins were also identified in decreasing order of abundance. Interestingly, contrary to previous reports, we find PLA2 toxins in N. nivea venom. This highlights the importance of repeatedly profiling the venom of the same species to account for intra-species variation. Additionally, we report the first evidence of covalent protein complexes in N. nivea venom, which likely contribute to the potency of this venom. Full article
(This article belongs to the Special Issue Animal Venoms: Proteomics, Biochemical Activities and Application)
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20 pages, 2638 KiB  
Article
Unveiling the Protein Components of the Secretory-Venom Gland and Venom of the Scorpion Centruroides possanii (Buthidae) through Omic Technologies
by Patricia Elizabeth García-Villalvazo, Juana María Jiménez-Vargas, Gisela Jareth Lino-López, Erika Patricia Meneses, Manuel de Jesús Bermúdez-Guzmán, Carlos Eduardo Barajas-Saucedo, Iván Delgado Enciso, Lourival Domingos Possani and Laura Leticia Valdez-Velazquez
Toxins 2023, 15(8), 498; https://doi.org/10.3390/toxins15080498 - 9 Aug 2023
Cited by 3 | Viewed by 2209
Abstract
Centruroides possanii is a recently discovered species of “striped scorpion” found in Mexico. Certain species of Centruroides are known to be toxic to mammals, leading to numerous cases of human intoxications in the country. Venom components are thought to possess therapeutic potential and/or [...] Read more.
Centruroides possanii is a recently discovered species of “striped scorpion” found in Mexico. Certain species of Centruroides are known to be toxic to mammals, leading to numerous cases of human intoxications in the country. Venom components are thought to possess therapeutic potential and/or biotechnological applications. Hence, obtaining and analyzing the secretory gland transcriptome and venom proteome of C. possanii is relevant, and that is what is described in this communication. Since this is a newly described species, first, its LD50 to mice was determined and estimated to be 659 ng/g mouse weight. Using RNA extracted from this species and preparing their corresponding cDNA fragments, a transcriptome analysis was obtained on a Genome Analyzer (Illumina) using the 76-base pair-end sequencing protocol. Via high-throughput sequencing, 19,158,736 reads were obtained and ensembled in 835,204 sequences. Of them, 28,399 transcripts were annotated with Pfam. A total of 244 complete transcripts were identified in the transcriptome of C. possanii. Of these, 109 sequences showed identity to toxins that act on ion channels, 47 enzymes, 17 protease inhibitors (PINs), 11 defense peptides (HDPs), and 60 in other components. In addition, a sample of the soluble venom obtained from this scorpion was analyzed using an Orbitrap Velos apparatus, which allowed for identification by liquid chromatography followed by mass spectrometry (LC-MS/MS) of 70 peptides and proteins: 23 toxins, 27 enzymes, 6 PINs, 3 HDPs, and 11 other components. Until now, this work has the highest number of scorpion venom components identified through omics technologies. The main novel findings described here were analyzed in comparison with the known data from the literature, and this process permitted some new insights in this field. Full article
(This article belongs to the Special Issue Animal Venoms: Proteomics, Biochemical Activities and Application)
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14 pages, 31813 KiB  
Article
Molecular Characterization and Functional Analysis of the Dipeptidyl Peptidase IV from Venom of the Ectoparasitoid Scleroderma guani
by Chaoyan Wu, Cheng Yang, Yuqin Wang, Jun Wang and Jiaying Zhu
Toxins 2023, 15(5), 311; https://doi.org/10.3390/toxins15050311 - 27 Apr 2023
Cited by 3 | Viewed by 1526
Abstract
Dipeptidyl peptidase IV (DPPIV) is a proline-specific serine peptidase that remains poorly investigated in terms of venom composition. Here, we describe the molecular characteristics and possible functions of DPPIV as a major venom component of the ant-like bethylid ectoparasitoid, Scleroderma guani, named [...] Read more.
Dipeptidyl peptidase IV (DPPIV) is a proline-specific serine peptidase that remains poorly investigated in terms of venom composition. Here, we describe the molecular characteristics and possible functions of DPPIV as a major venom component of the ant-like bethylid ectoparasitoid, Scleroderma guani, named SgVnDPPIV. The SgVnDPPIV gene was cloned, which encodes a protein with the conserved catalytic triads and substrate binding sites of mammalian DPPIV. This venom gene is highly expressed in the venom apparatus. Recombinant SgVnDPPIV, produced in Sf9 cells using the baculovirus expression system, has high enzymatic activity, which can be efficiently inhibited by vildagliptin and sitagliptin. Functional analysis revealed that SgVnDPPIV affects genes related to detoxification, lipid synthesis and metabolism, response to stimuli, and ion exchange in pupae of Tenebrio molitor, an envenomated host of S. guani. The present work contributes towards understanding the role of venom DPPIV involved in the interaction between parasitoid wasp and its host. Full article
(This article belongs to the Special Issue Animal Venoms: Proteomics, Biochemical Activities and Application)
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22 pages, 3174 KiB  
Article
Application of an Extracellular Matrix-Mimicking Fluorescent Polymer for the Detection of Proteolytic Venom Toxins
by Eric Wachtel, Matyas A. Bittenbinder, Bas van de Velde, Julien Slagboom, Axel de Monts de Savasse, Luis L. Alonso, Nicholas R. Casewell, Freek J. Vonk and Jeroen Kool
Toxins 2023, 15(4), 294; https://doi.org/10.3390/toxins15040294 - 18 Apr 2023
Cited by 1 | Viewed by 2299
Abstract
The cytotoxicity caused by snake venoms is a serious medical problem that greatly contributes to the morbidity observed in snakebite patients. The cytotoxic components found in snake venoms belong to a variety of toxin classes and may cause cytotoxic effects by targeting a [...] Read more.
The cytotoxicity caused by snake venoms is a serious medical problem that greatly contributes to the morbidity observed in snakebite patients. The cytotoxic components found in snake venoms belong to a variety of toxin classes and may cause cytotoxic effects by targeting a range of molecular structures, including cellular membranes, the extracellular matrix (ECM) and the cytoskeleton. Here, we present a high-throughput assay (384-well plate) that monitors ECM degradation by snake venom toxins via the application of fluorescent versions of model ECM substrates, specifically gelatin and collagen type I. Both crude venoms and fractionated toxins of a selection of medically relevant viperid and elapid species, separated via size-exclusion chromatography, were studied using the self-quenching, fluorescently labelled ECM–polymer substrates. The viperid venoms showed significantly higher proteolytic degradation when compared to elapid venoms, although the venoms with higher snake venom metalloproteinase content did not necessarily exhibit stronger substrate degradation than those with a lower one. Gelatin was generally more readily cleaved than collagen type I. In the viperid venoms, which were subjected to fractionation by SEC, two (B. jararaca and C. rhodostoma, respectively) or three (E. ocellatus) active proteases were identified. Therefore, the assay allows the study of proteolytic activity towards the ECM in vitro for crude and fractionated venoms. Full article
(This article belongs to the Special Issue Animal Venoms: Proteomics, Biochemical Activities and Application)
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