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Toxins
Special Issues
Evolution of Animal Toxins
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Evolution of Animal Toxins

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

Deadline for manuscript submissions: closed (1 May 2022) | Viewed by 8143

Special Issue Editor

Dr. Dušan Kordiš

E-Mail Website
Guest Editor
Department of Molecular and Biomedical Sciences, Josef Stefan Institute, 1000 Ljubljana, Slovenia
Interests: molecular evolution; adaptive evolution of toxins; evolution of animal toxin multigene families; functional diversification after gene duplication; PLA2 and BPTI neurotoxins; phylogenomic analysis of protein superfamilies; structure–function relationships; regulatory evolution; genome evolution
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Many animals rely on the production of complex venoms for predation and defense. Animal venoms have evolved through millions of years of natural selection in a co-evolutionary process involving the prey and the predator that is often referred to as an “arms race”. As such, they are extremely efficient, being usually effective at a very low concentration via highly specific interactions with key physiological targets (ion channels, enzymes, and membrane receptors). Animal toxins are valuable systems for understanding a variety of different evolutionary processes, including those relating to convergence, adaptive molecular evolution, gene duplication, and protein neofunctionalization. Recent studies have revealed that a limited number of toxin scaffolds have been convergently recruited by two or more venomous lineages. The evolution of animal toxin families through the “birth and death” model is often accompanied by strong evidence of adaptive evolution. Positive selection prevails in venomous animals and acts mostly on the surface-exposed amino acid residues. The modification of surface-exposed residues may facilitate neofunctionalization of the animal toxins by modification of protein–target interactions. The role of gene duplication is crucial to organismal evolution by facilitating the evolution of new protein functions. Gene duplication can also contribute to gene dosage effects (where the protein dosage is increased by the duplication of protein-coding genes), which might be particularly relevant to the production of highly potent animal toxins. Gene duplication, positive selection, and protein neofunctionalization therefore work together to provide the evolutionary novelty that allows for adaptation of animal toxins to different prey, as well as overcoming prey defenses against them.

This Special Issue of Toxins will accept original research articles and authoritative reviews on any aspect of the evolution of animal toxins. It aims to provide readers with an updated and comprehensive picture of this exciting area of research.

Prof. Dr. Dušan Kordiš
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

  • animal toxins
  • molecular evolution
  • adaptive evolution
  • gene duplication
  • neofunctionalization
  • evolutionary novelty

Published Papers (2 papers)

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Research

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16 pages, 3720 KiB  
Article
Contextual Constraints: Dynamic Evolution of Snake Venom Phospholipase A2
by Vivek Suranse, Timothy N. W. Jackson and Kartik Sunagar
Toxins 2022, 14(6), 420; https://doi.org/10.3390/toxins14060420 - 20 Jun 2022
Cited by 7 | Viewed by 2867
Abstract
Venom is a dynamic trait that has contributed to the success of numerous organismal lineages. Predominantly composed of proteins, these complex cocktails are deployed for predation and/or self-defence. Many non-toxic physiological proteins have been convergently and recurrently recruited by venomous animals into their [...] Read more.
Venom is a dynamic trait that has contributed to the success of numerous organismal lineages. Predominantly composed of proteins, these complex cocktails are deployed for predation and/or self-defence. Many non-toxic physiological proteins have been convergently and recurrently recruited by venomous animals into their toxin arsenal. Phospholipase A2 (PLA2) is one such protein and features in the venoms of many organisms across the animal kingdom, including snakes of the families Elapidae and Viperidae. Understanding the evolutionary history of this superfamily would therefore provide insight into the origin and diversification of venom toxins and the evolution of novelty more broadly. The literature is replete with studies that have identified diversifying selection as the sole influence on PLA2 evolution. However, these studies have largely neglected the structural/functional constraints on PLA2s, and the ecology and evolutionary histories of the diverse snake lineages that produce them. By considering these crucial factors and employing evolutionary analyses integrated with a schema for the classification of PLA2s, we uncovered lineage-specific differences in selection regimes. Thus, our work provides novel insights into the evolution of this major snake venom toxin superfamily and underscores the importance of considering the influence of evolutionary and ecological contexts on molecular evolution. Full article
(This article belongs to the Special Issue Evolution of Animal Toxins)
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Review

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25 pages, 7544 KiB  
Review
The Natterin Proteins Diversity: A Review on Phylogeny, Structure, and Immune Function
by Carla Lima, Geonildo Rodrigo Disner, Maria Alice Pimentel Falcão, Ana Carolina Seni-Silva, Adolfo Luis Almeida Maleski, Milena Marcolino Souza, Mayara Cristina Reis Tonello and Monica Lopes-Ferreira
Toxins 2021, 13(8), 538; https://doi.org/10.3390/toxins13080538 - 31 Jul 2021
Cited by 20 | Viewed by 4099
Abstract
Since the first record of the five founder members of the group of Natterin proteins in the venom of the medically significant fish Thalassophryne nattereri, new sequences have been identified in other species. In this work, we performed a detailed screening using [...] Read more.
Since the first record of the five founder members of the group of Natterin proteins in the venom of the medically significant fish Thalassophryne nattereri, new sequences have been identified in other species. In this work, we performed a detailed screening using available genome databases across a wide range of species to identify sequence members of the Natterin group, sequence similarities, conserved domains, and evolutionary relationships. The high-throughput tools have enabled us to dramatically expand the number of members within this group of proteins, which has a remote origin (around 400 million years ago) and is spread across Eukarya organisms, even in plants and primitive Agnathans jawless fish. Overall, the survey resulted in 331 species presenting Natterin-like proteins, mainly fish, and 859 putative genes. Besides fish, the groups with more species included in our analysis were insects and birds. The number and variety of annotations increased the knowledge of the obtained sequences in detail, such as the conserved motif AGIP in the pore-forming loop involved in the transmembrane barrel insertion, allowing us to classify them as important constituents of the innate immune defense system as effector molecules activating immune cells by interacting with conserved intracellular signaling mechanisms in the hosts. Full article
(This article belongs to the Special Issue Evolution of Animal Toxins)
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