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Toxins
Special Issues
Research on Invertebrate Venomics
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Research on Invertebrate Venomics

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

Deadline for manuscript submissions: closed (31 August 2023) | Viewed by 6023

Special Issue Editor

Dr. Ivan Koludarov

E-Mail Website
Guest Editor
Department of Informatics, Bioinformatics & Computational Biology, TUM (Technical University of Munich), i12, Boltzmannstr. 3, 85748 Garching/Munich, Germany
Interests: venomics; comparative genomics; gene evolution; evolution of function; machine learning

Special Issue Information

Dear Colleagues,

Traditional venom research is centred around a handful of species, most of which are snakes. However, the large majority of venomous species belong to various clades of invertebrates: hy-menopterans, spiders, cnidarians, molluscs and others. The knowledge about their venom’s com-position and evolution is comparatively scarce. Modern advances in methodology, in particular in transcriptomics and proteomics, coupled with a more robust theoretical framework have pro-duced some insightful studies on invertebrate venoms; however, most of them remain to be looked into. The aim of the present Special Issue is to highlight the recent advances, new discov-eries and hypotheses in invertebrate venomics research.

Dr. Ivan Koludarov
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

  • invertebrate venomics 
  • hymenopteran venoms
  • spider venoms
  • arachnid venoms
  • cnidarian venoms
  • venom evolution
  • small peptide venomics

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Published Papers (2 papers)

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Research

25 pages, 10222 KiB  
Article
Functional and Proteomic Insights into Aculeata Venoms
by Daniel Dashevsky, Kate Baumann, Eivind A. B. Undheim, Amanda Nouwens, Maria P. Ikonomopoulou, Justin O. Schmidt, Lilin Ge, Hang Fai Kwok, Juanita Rodriguez and Bryan G. Fry
Toxins 2023, 15(3), 224; https://doi.org/10.3390/toxins15030224 - 16 Mar 2023
Cited by 4 | Viewed by 3223
Abstract
Aculeate hymenopterans use their venom for a variety of different purposes. The venom of solitary aculeates paralyze and preserve prey without killing it, whereas social aculeates utilize their venom in defence of their colony. These distinct applications of venom suggest that its components [...] Read more.
Aculeate hymenopterans use their venom for a variety of different purposes. The venom of solitary aculeates paralyze and preserve prey without killing it, whereas social aculeates utilize their venom in defence of their colony. These distinct applications of venom suggest that its components and their functions are also likely to differ. This study investigates a range of solitary and social species across Aculeata. We combined electrophoretic, mass spectrometric, and transcriptomic techniques to characterize the compositions of venoms from an incredibly diverse taxon. In addition, in vitro assays shed light on their biological activities. Although there were many common components identified in the venoms of species with different social behavior, there were also significant variations in the presence and activity of enzymes such as phospholipase A2s and serine proteases and the cytotoxicity of the venoms. Social aculeate venom showed higher presence of peptides that cause damage and pain in victims. The venom-gland transcriptome from the European honeybee (Apis mellifera) contained highly conserved toxins which match those identified by previous investigations. In contrast, venoms from less-studied taxa returned limited results from our proteomic databases, suggesting that they contain unique toxins. Full article
(This article belongs to the Special Issue Research on Invertebrate Venomics)
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16 pages, 3604 KiB  
Article
Molecular Diversity of Linear Peptides Revealed by Transcriptomic Analysis of the Venom Gland of the Spider Lycosa poonaensis
by Alhussin Mohamed Abdelhakeem Megaly, Masahiro Miyashita, Mohammed Abdel-Wahab, Yoshiaki Nakagawa and Hisashi Miyagawa
Toxins 2022, 14(12), 854; https://doi.org/10.3390/toxins14120854 - 3 Dec 2022
Cited by 3 | Viewed by 2267
Abstract
Spider venom is a complex mixture of bioactive components. Previously, we identified two linear peptides in Lycosa poonaensis venom using mass spectrometric analysis and predicted the presence of more linear peptides therein. In this study, a transcriptomic analysis of the L. poonaensis venom [...] Read more.
Spider venom is a complex mixture of bioactive components. Previously, we identified two linear peptides in Lycosa poonaensis venom using mass spectrometric analysis and predicted the presence of more linear peptides therein. In this study, a transcriptomic analysis of the L. poonaensis venom gland was conducted to identify other undetermined linear peptides in the venom. The results identified 87 contigs encoding peptides and proteins in the venom that were similar to those in other spider venoms. The number of contigs identified as neurotoxins was the highest, and 15 contigs encoding 17 linear peptide sequences were identified. Seven peptides that were representative of each family were chemically synthesized, and their biological activities were evaluated. All peptides showed significant antibacterial activity against Gram-positive and Gram-negative bacteria, although their selectivity for bacterial species differed. All peptides also exhibited paralytic activity against crickets, but none showed hemolytic activity. The secondary structure analysis based on the circular dichroism spectroscopy showed that all these peptides adopt an amphiphilic α-helical structure. Their activities appear to depend on the net charge, the arrangement of basic and acidic residues, and the hydrophobicity of the peptides. Full article
(This article belongs to the Special Issue Research on Invertebrate Venomics)
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