Special Issue "Venom Proteomics and Transcriptomics"

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

Deadline for manuscript submissions: closed (31 January 2020).

Special Issue Editors

Prof. Dr. Edwin A. De Pauw
E-Mail Website
Guest Editor
Laboratory of Mass Spectrometry - MolSys Research Unit, Allée du six Aout 11 - Quartier Agora - B4000 -Liège 1, Belgium
Interests: Mass Spectrometry, Physical Chemistry, Biophysics
Special Issues and Collections in MDPI journals
Prof. Dr. Loïc Quinton
E-Mail Website
Guest Editor
Laboratory of Mass Spectrometry - MolSys Research Unit, Allée du six Aout 11 - Quartier Agora - B4000 -Liège 1 - Belgium
Interests: Mass spectrometry, Toxinology, Biological Chemistry
Special Issues and Collections in MDPI journals

Special Issue Information

Dear Colleagues,

The deep analysis of venoms is receiving growing interest supported by important advances in sequencing methods, both at the nucleic acid and at the proteins/peptide level. The final toxins present in venoms can be characterized in detail, from their primary structure to their 3D fold. The level of detail that can be reached using mass spectrometry with only tiny amounts of sample opens new ways to characterize single organism toxins and to differentiate venoms from similar species of different geographical origin. The emphasis of this Special Issue will be on papers in which the methodological advances bring real breakthroughs and in which the complementarity of the approaches show a significant added value. Promising separation methods such as capillary electrophoresis and ion mobility are desired, as well as the 2D molecular mapping of venom glands by mass spectrometry imaging.

Prof. Dr. Edwin A. De Pauw
Dr. Loïc Quinton
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

  • toxins
  • mass spectrometry
  • mass spectrometry imaging
  • hyphenated methods
  • ion mobility
  • capillary electrophoresis

Published Papers (7 papers)

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Research

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Open AccessArticle
Proteotranscriptomic Insights into the Venom Composition of the Wolf Spider Lycosa tarantula
Toxins 2020, 12(8), 501; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins12080501 - 05 Aug 2020
Viewed by 1452
Abstract
Spider venoms represent an original source of novel compounds with therapeutic and agrochemical potential. Whereas most of the research efforts have focused on large mygalomorph spiders, araneomorph spiders are equally promising but require more sensitive and sophisticated approaches given their limited size and [...] Read more.
Spider venoms represent an original source of novel compounds with therapeutic and agrochemical potential. Whereas most of the research efforts have focused on large mygalomorph spiders, araneomorph spiders are equally promising but require more sensitive and sophisticated approaches given their limited size and reduced venom yield. Belonging to the latter group, the genus Lycosa (“wolf spiders”) contains many species widely distributed throughout the world. These spiders are ambush predators that do not build webs but instead rely strongly on their venom for prey capture. Lycosa tarantula is one of the largest species of wolf spider, but its venom composition is unknown. Using a combination of RNA sequencing of the venom glands and venom proteomics, we provide the first overview of the peptides and proteins produced by this iconic Mediterranean spider. Beside the typical small disulfide rich neurotoxins, several families of proteins were also identified, including cysteine-rich secretory proteins (CRISP) and Hyaluronidases. Proteomic analysis of the electrically stimulated venom validated 30 of these transcriptomic sequences, including nine putative neurotoxins and eight venom proteins. Interestingly, LC-MS venom profiles of manual versus electric stimulation, as well as female versus male, showed some marked differences in mass distribution. Finally, we also present some preliminary data on the biological activity of L. tarantula crude venom. Full article
(This article belongs to the Special Issue Venom Proteomics and Transcriptomics)
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Open AccessArticle
Venomics Approach Reveals a High Proportion of Lactrodectus-Like Toxins in the Venom of the Noble False Widow Spider Steatoda nobilis
Toxins 2020, 12(6), 402; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins12060402 - 18 Jun 2020
Cited by 2 | Viewed by 2555
Abstract
The noble false widow spider Steatoda nobilis originates from the Macaronesian archipelago and has expanded its range globally. Outside of its natural range, it may have a negative impact on native wildlife, and in temperate regions it lives in synanthropic environments where it [...] Read more.
The noble false widow spider Steatoda nobilis originates from the Macaronesian archipelago and has expanded its range globally. Outside of its natural range, it may have a negative impact on native wildlife, and in temperate regions it lives in synanthropic environments where it frequently encounters humans, subsequently leading to envenomations. S. nobilis is the only medically significant spider in Ireland and the UK, and envenomations have resulted in local and systemic neurotoxic symptoms similar to true black widows (genus Latrodectus). S. nobilis is a sister group to Latrodectus which possesses the highly potent neurotoxins called α-latrotoxins that can induce neuromuscular paralysis and is responsible for human fatalities. However, and despite this close relationship, the venom composition of S. nobilis has never been investigated. In this context, a combination of transcriptomic and proteomic cutting-edge approaches has been used to deeply characterise S. nobilis venom. Mining of transcriptome data for the peptides identified by proteomics revealed 240 annotated sequences, of which 118 are related to toxins, 37 as enzymes, 43 as proteins involved in various biological functions, and 42 proteins without any identified function to date. Among the toxins, the most represented in numbers are α-latrotoxins (61), δ-latroinsectotoxins (44) and latrodectins (6), all of which were first characterised from black widow venoms. Transcriptomics alone provided a similar representation to proteomics, thus demonstrating that our approach is highly sensitive and accurate. More precisely, a relative quantification approach revealed that latrodectins are the most concentrated toxin (28%), followed by α-latrotoxins (11%), δ-latroinsectotoxins (11%) and α-latrocrustotoxins (11%). Approximately two-thirds of the venom is composed of Latrodectus-like toxins. Such toxins are highly potent towards the nervous system of vertebrates and likely responsible for the array of symptoms occurring after envenomation by black widows and false widows. Thus, caution should be taken in dismissing S. nobilis as harmless. This work paves the way towards a better understanding of the competitiveness of S. nobilis and its potential medical importance. Full article
(This article belongs to the Special Issue Venom Proteomics and Transcriptomics)
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Open AccessArticle
An Integrated Proteomic and Transcriptomic Analysis Reveals the Venom Complexity of the Bullet Ant Paraponera clavata
Toxins 2020, 12(5), 324; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins12050324 - 14 May 2020
Cited by 3 | Viewed by 1491
Abstract
A critical hurdle in ant venom proteomic investigations is the lack of databases to comprehensively and specifically identify the sequence and function of venom proteins and peptides. To resolve this, we used venom gland transcriptomics to generate a sequence database that was used [...] Read more.
A critical hurdle in ant venom proteomic investigations is the lack of databases to comprehensively and specifically identify the sequence and function of venom proteins and peptides. To resolve this, we used venom gland transcriptomics to generate a sequence database that was used to assign the tandem mass spectrometry (MS) fragmentation spectra of venom peptides and proteins to specific transcripts. This was performed alongside a shotgun liquid chromatography–mass spectrometry (LC-MS/MS) analysis of the venom to confirm that these assigned transcripts were expressed as proteins. Through the combined transcriptomic and proteomic investigation of Paraponera clavata venom, we identified four times the number of proteins previously identified using 2D-PAGE alone. In addition to this, by mining the transcriptomic data, we identified several novel peptide sequences for future pharmacological investigations, some of which conform with inhibitor cysteine knot motifs. These types of peptides have the potential to be developed into pharmaceutical or bioinsecticide peptides. Full article
(This article belongs to the Special Issue Venom Proteomics and Transcriptomics)
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Open AccessArticle
Alteration of Bumblebee Venom Composition toward Higher Elevation
Toxins 2020, 12(1), 4; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins12010004 - 19 Dec 2019
Cited by 2 | Viewed by 2392
Abstract
Venomous animals use venom, a complex biofluid composed of unique mixtures of proteins and peptides, for either predation or defense. Bumblebees, which occur in various habitats due to their unique thermoregulatory properties, mainly use venom for defense. Herein, we conducted an exploratory analysis [...] Read more.
Venomous animals use venom, a complex biofluid composed of unique mixtures of proteins and peptides, for either predation or defense. Bumblebees, which occur in various habitats due to their unique thermoregulatory properties, mainly use venom for defense. Herein, we conducted an exploratory analysis of the venom composition of a bumblebee species (Bombus pascuorum) along an elevation gradient in the western Swiss Alps using shot-gun proteomic approaches to assess whether their defense mechanism varies along the gradient. The gradient was characterized by high temperatures and low humidity at low elevations and low temperatures and high humidity at high elevations. Venom composition is changing along the elevation gradient, with proteomic variation in the abundances of pain-inducing and allergenic proteins. In particular, the abundance of phospholipase A2-like, the main component of bumblebee venom, gradually decreases toward higher elevation (lower temperature), suggesting venom alteration and thus a decrease in bumblebee defense towards harsher environments. Larger datasets may complement this study to validate the observed novel trends. Full article
(This article belongs to the Special Issue Venom Proteomics and Transcriptomics)
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Open AccessArticle
The Peptide Venom Composition of the Fierce Stinging Ant Tetraponera aethiops (Formicidae: Pseudomyrmecinae)
Toxins 2019, 11(12), 732; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins11120732 - 14 Dec 2019
Cited by 5 | Viewed by 1566
Abstract
In the mutualisms involving certain pseudomyrmicine ants and different myrmecophytes (i.e., plants sheltering colonies of specialized “plant-ant” species in hollow structures), the ant venom contributes to the host plant biotic defenses by inducing the rapid paralysis of defoliating insects and causing intense pain [...] Read more.
In the mutualisms involving certain pseudomyrmicine ants and different myrmecophytes (i.e., plants sheltering colonies of specialized “plant-ant” species in hollow structures), the ant venom contributes to the host plant biotic defenses by inducing the rapid paralysis of defoliating insects and causing intense pain to browsing mammals. Using integrated transcriptomic and proteomic approaches, we identified the venom peptidome of the plant-ant Tetraponera aethiops (Pseudomyrmecinae). The transcriptomic analysis of its venom glands revealed that 40% of the expressed contigs encoded only seven peptide precursors related to the ant venom peptides from the A-superfamily. Among the 12 peptide masses detected by liquid chromatography-mass spectrometry (LC–MS), nine mature peptide sequences were characterized and confirmed through proteomic analysis. These venom peptides, called pseudomyrmecitoxins (PSDTX), share amino acid sequence identities with myrmeciitoxins known for their dual offensive and defensive functions on both insects and mammals. Furthermore, we demonstrated through reduction/alkylation of the crude venom that four PSDTXs were homo- and heterodimeric. Thus, we provide the first insights into the defensive venom composition of the ant genus Tetraponera indicative of a streamlined peptidome. Full article
(This article belongs to the Special Issue Venom Proteomics and Transcriptomics)
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Open AccessArticle
Alternative mRNA Splicing in Three Venom Families Underlying a Possible Production of Divergent Venom Proteins of the Habu Snake, Protobothrops flavoviridis
Toxins 2019, 11(10), 581; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins11100581 - 09 Oct 2019
Cited by 4 | Viewed by 1292
Abstract
Snake venoms are complex mixtures of toxic proteins encoded by various gene families that function synergistically to incapacitate prey. A huge repertoire of snake venom genes and proteins have been reported, and alternative splicing is suggested to be involved in the production of [...] Read more.
Snake venoms are complex mixtures of toxic proteins encoded by various gene families that function synergistically to incapacitate prey. A huge repertoire of snake venom genes and proteins have been reported, and alternative splicing is suggested to be involved in the production of divergent gene transcripts. However, a genome-wide survey of the transcript repertoire and the extent of alternative splicing still remains to be determined. In this study, the comprehensive analysis of transcriptomes in the venom gland was achieved by using PacBio sequencing. Extensive alternative splicing was observed in three venom protein gene families, metalloproteinase (MP), serine protease (SP), and vascular endothelial growth factors (VEGF). Eleven MP and SP genes and a VEGF gene are expressed as a total of 81, 61, and 8 transcript variants, respectively. In the MP gene family, individual genes are transcribed into different classes of MPs by alternative splicing. We also observed trans-splicing among the clustered SP genes. No other venom genes as well as non-venom counterpart genes exhibited alternative splicing. Our results thus indicate a potential contribution of mRNA alternative and trans-splicing in the production of highly variable transcripts of venom genes in the habu snake. Full article
(This article belongs to the Special Issue Venom Proteomics and Transcriptomics)
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Review

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Open AccessReview
Proteomic and Transcriptomic Techniques to Decipher the Molecular Evolution of Venoms
Toxins 2021, 13(2), 154; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13020154 - 16 Feb 2021
Viewed by 620
Abstract
Nature’s library of venoms is a vast and untapped resource that has the potential of becoming the source of a wide variety of new drugs and therapeutics. The discovery of these valuable molecules, hidden in diverse collections of different venoms, requires highly specific [...] Read more.
Nature’s library of venoms is a vast and untapped resource that has the potential of becoming the source of a wide variety of new drugs and therapeutics. The discovery of these valuable molecules, hidden in diverse collections of different venoms, requires highly specific genetic and proteomic sequencing techniques. These have been used to sequence a variety of venom glands from species ranging from snakes to scorpions, and some marine species. In addition to identifying toxin sequences, these techniques have paved the way for identifying various novel evolutionary links between species that were previously thought to be unrelated. Furthermore, proteomics-based techniques have allowed researchers to discover how specific toxins have evolved within related species, and in the context of environmental pressures. These techniques allow groups to discover novel proteins, identify mutations of interest, and discover new ways to modify toxins for biomimetic purposes and for the development of new therapeutics. Full article
(This article belongs to the Special Issue Venom Proteomics and Transcriptomics)
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