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Anthozoan Toxins: Using New Approaches to Understand Their Composition, Distribution,...
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Anthozoan Toxins: Using New Approaches to Understand Their Composition, Distribution, and Function

A special issue of Marine Drugs (ISSN 1660-3397).

Deadline for manuscript submissions: closed (15 December 2020) | Viewed by 34144

Special Issue Editors

Dr. Peter Prentis

E-Mail Website
Guest Editor
Queensland University of Technology, School of Earth, Environmental and Biological Sciences, 2 George Street, Brisbane, Qld, 4001, Australia
Interests: evolution; cnidarians; functional genomics; comparative genomics
Dr. Jason Macrander

E-Mail Website
Guest Editor
Florida Southern College, 111 Lake Hollingsworth Drive, Lakeland, FL 33801, USA
Interests: molecular biology; genomics; toxins; evolutionary bioinformatics; cnidarians

Special Issue Information

Dear Colleagues,

Anthozoans (i.e., sea anemones, corals, and their relatives) are members of one of the largest groups of venomous marine animals, while simultaneously remaining one of the most poorly studied. Anthozoans are found in a variety of habitats, using toxins to capture prey, defend against predators, and compete during intra-/inter-specific encounters. Anthozoans also lack a centralized venom gland or duct, instead using a combination of cell- and tissue-specific venoms that have been subjected to evolutionary processes for hundreds of millions of years. Ultimately, the unique ecological, cellular, and evolutionary processes shaping protein function in this group remain largely unexplored and have significant potential for human health applications.

The purpose of this Special Issue is to bring together a diverse group of researchers that are developing new ways to study venom composition in this poorly studied group. This Special Issue entitled “Anthozoan Toxins: Using New Approaches to Understand Their Composition, Distribution, and Function” aims to collate papers describing new approaches to understanding anthozoan toxin diversity by focusing on: (1) new species and new toxins, (2) new approaches using bioinformatic and high-throughput techniques to identify and characterize toxins, and (3) new ways to think about toxin function as it relates to ecology and evolution and their potential application to human health.

Dr. Peter Prentis
Dr. Jason Macrander
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 single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Marine Drugs 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 2900 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
  • Anthozoan
  • Sea anemones
  • Corals
  • Detection methods
  • Protein function
  • Protein structure
  • Venom evolution

Published Papers (6 papers)

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Research

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17 pages, 641 KiB  
Article
Never, Ever Make an Enemy… Out of an Anemone: Transcriptomic Comparison of Clownfish Hosting Sea Anemone Venoms
by Alonso Delgado, Charlotte Benedict, Jason Macrander and Marymegan Daly
Mar. Drugs 2022, 20(12), 730; https://doi.org/10.3390/md20120730 - 23 Nov 2022
Cited by 8 | Viewed by 3854
Abstract
Sea anemones are predatory marine invertebrates and have diverse venom arsenals. Venom is integral to their biology, and is used in competition, defense, and feeding. Three lineages of sea anemones are known to have independently evolved symbiotic relationships with clownfish, however the evolutionary [...] Read more.
Sea anemones are predatory marine invertebrates and have diverse venom arsenals. Venom is integral to their biology, and is used in competition, defense, and feeding. Three lineages of sea anemones are known to have independently evolved symbiotic relationships with clownfish, however the evolutionary impact of this relationship on the venom composition of the host is still unknown. Here, we investigate the potential of this symbiotic relationship to shape the venom profiles of the sea anemones that host clownfish. We use transcriptomic data to identify differences and similarities in venom profiles of six sea anemone species, representing the three known clades of clownfish-hosting sea anemones. We recovered 1121 transcripts matching verified toxins across all species, and show that hemolytic and hemorrhagic toxins are consistently the most dominant and diverse toxins across all species examined. These results are consistent with the known biology of sea anemones, provide foundational data on venom diversity of these species, and allow for a review of existing hierarchical structures in venomic studies. Full article
(This article belongs to the Special Issue Anthozoan Toxins: Using New Approaches to Understand Their Composition, Distribution, and Function)
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24 pages, 3877 KiB  
Article
Transcriptomic Analysis of Four Cerianthid (Cnidaria, Ceriantharia) Venoms
by Anna M. L. Klompen, Jason Macrander, Adam M. Reitzel and Sérgio N. Stampar
Mar. Drugs 2020, 18(8), 413; https://doi.org/10.3390/md18080413 - 05 Aug 2020
Cited by 21 | Viewed by 6664
Abstract
Tube anemones, or cerianthids, are a phylogenetically informative group of cnidarians with complex life histories, including a pelagic larval stage and tube-dwelling adult stage, both known to utilize venom in stinging-cell rich tentacles. Cnidarians are an entirely venomous group that utilize their proteinaceous-dominated [...] Read more.
Tube anemones, or cerianthids, are a phylogenetically informative group of cnidarians with complex life histories, including a pelagic larval stage and tube-dwelling adult stage, both known to utilize venom in stinging-cell rich tentacles. Cnidarians are an entirely venomous group that utilize their proteinaceous-dominated toxins to capture prey and defend against predators, in addition to several other ecological functions, including intraspecific interactions. At present there are no studies describing the venom for any species within cerianthids. Given their unique development, ecology, and distinct phylogenetic-placement within Cnidaria, our objective is to evaluate the venom-like gene diversity of four species of cerianthids from newly collected transcriptomic data. We identified 525 venom-like genes between all four species. The venom-gene profile for each species was dominated by enzymatic protein and peptide families, which is consistent with previous findings in other cnidarian venoms. However, we found few toxins that are typical of sea anemones and corals, and furthermore, three of the four species express toxin-like genes closely related to potent pore-forming toxins in box jellyfish. Our study is the first to provide a survey of the putative venom composition of cerianthids and contributes to our general understanding of the diversity of cnidarian toxins. Full article
(This article belongs to the Special Issue Anthozoan Toxins: Using New Approaches to Understand Their Composition, Distribution, and Function)
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21 pages, 4581 KiB  
Article
A Versatile and Robust Serine Protease Inhibitor Scaffold from Actinia tenebrosa
by Xingchen Chen, Darren Leahy, Jessica Van Haeften, Perry Hartfield, Peter J. Prentis, Chloé A. van der Burg, Joachim M. Surm, Ana Pavasovic, Bruno Madio, Brett R. Hamilton, Glenn F. King, Eivind A. B. Undheim, Maria Brattsand and Jonathan M. Harris
Mar. Drugs 2019, 17(12), 701; https://doi.org/10.3390/md17120701 - 12 Dec 2019
Cited by 9 | Viewed by 3984
Abstract
Serine proteases play pivotal roles in normal physiology and a spectrum of patho-physiological processes. Accordingly, there is considerable interest in the discovery and design of potent serine protease inhibitors for therapeutic applications. This led to concerted efforts to discover versatile and robust molecular [...] Read more.
Serine proteases play pivotal roles in normal physiology and a spectrum of patho-physiological processes. Accordingly, there is considerable interest in the discovery and design of potent serine protease inhibitors for therapeutic applications. This led to concerted efforts to discover versatile and robust molecular scaffolds for inhibitor design. This investigation is a bioprospecting study that aims to isolate and identify protease inhibitors from the cnidarian Actinia tenebrosa. The study isolated two Kunitz-type protease inhibitors with very similar sequences but quite divergent inhibitory potencies when assayed against bovine trypsin, chymostrypsin, and a selection of human sequence-related peptidases. Homology modeling and molecular dynamics simulations of these inhibitors in complex with their targets were carried out and, collectively, these methodologies enabled the definition of a versatile scaffold for inhibitor design. Thermal denaturation studies showed that the inhibitors were remarkably robust. To gain a fine-grained map of the residues responsible for this stability, we conducted in silico alanine scanning and quantified individual residue contributions to the inhibitor’s stability. Sequences of these inhibitors were then used to search for Kunitz homologs in an A. tenebrosa transcriptome library, resulting in the discovery of a further 14 related sequences. Consensus analysis of these variants identified a rich molecular diversity of Kunitz domains and expanded the palette of potential residue substitutions for rational inhibitor design using this domain. Full article
(This article belongs to the Special Issue Anthozoan Toxins: Using New Approaches to Understand Their Composition, Distribution, and Function)
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23 pages, 1918 KiB  
Article
Transcriptomic and Proteomic Analysis of the Tentacles and Mucus of Anthopleura dowii Verrill, 1869
by Santos Ramírez-Carreto, Rosario Vera-Estrella, Tobías Portillo-Bobadilla, Alexei Licea-Navarro, Johanna Bernaldez-Sarabia, Enrique Rudiño-Piñera, Jerome J. Verleyen, Estefanía Rodríguez and Claudia Rodríguez-Almazán
Mar. Drugs 2019, 17(8), 436; https://doi.org/10.3390/md17080436 - 25 Jul 2019
Cited by 26 | Viewed by 4056
Abstract
Sea anemone venom contains a complex and diverse arsenal of peptides and proteins of pharmacological and biotechnological interest, however, only venom from a few species has been explored from a global perspective to date. In the present study, we identified the polypeptides present [...] Read more.
Sea anemone venom contains a complex and diverse arsenal of peptides and proteins of pharmacological and biotechnological interest, however, only venom from a few species has been explored from a global perspective to date. In the present study, we identified the polypeptides present in the venom of the sea anemone Anthopleura dowii Verrill, 1869 through a transcriptomic and proteomic analysis of the tentacles and the proteomic profile of the secreted mucus. In our transcriptomic results, we identified 261 polypeptides related to or predicted to be secreted in the venom, including proteases, neurotoxins that could act as either potassium (K+) or sodium (Na+) channels inhibitors, protease inhibitors, phospholipases A2, and other polypeptides. Our proteomic data allowed the identification of 156 polypeptides—48 exclusively identified in the mucus, 20 in the tentacles, and 88 in both protein samples. Only 23 polypeptides identified by tandem mass spectrometry (MS/MS) were related to the venom and 21 exclusively identified in the mucus, most corresponding to neurotoxins and hydrolases. Our data contribute to the knowledge of evolutionary and venomic analyses of cnidarians, particularly of sea anemones. Full article
(This article belongs to the Special Issue Anthozoan Toxins: Using New Approaches to Understand Their Composition, Distribution, and Function)
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Review

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19 pages, 3319 KiB  
Review
Characterising Functional Venom Profiles of Anthozoans and Medusozoans within Their Ecological Context
by Lauren M. Ashwood, Raymond S. Norton, Eivind A. B. Undheim, David A. Hurwood and Peter J. Prentis
Mar. Drugs 2020, 18(4), 202; https://doi.org/10.3390/md18040202 - 09 Apr 2020
Cited by 30 | Viewed by 6985
Abstract
This review examines the current state of knowledge regarding toxins from anthozoans (sea anemones, coral, zoanthids, corallimorphs, sea pens and tube anemones). We provide an overview of venom from phylum Cnidaria and review the diversity of venom composition between the two major clades [...] Read more.
This review examines the current state of knowledge regarding toxins from anthozoans (sea anemones, coral, zoanthids, corallimorphs, sea pens and tube anemones). We provide an overview of venom from phylum Cnidaria and review the diversity of venom composition between the two major clades (Medusozoa and Anthozoa). We highlight that the functional and ecological context of venom has implications for the temporal and spatial expression of protein and peptide toxins within class Anthozoa. Understanding the nuances in the regulation of venom arsenals has been made possible by recent advances in analytical technologies that allow characterisation of the spatial distributions of toxins. Furthermore, anthozoans are unique in that ecological roles can be assigned using tissue expression data, thereby circumventing some of the challenges related to pharmacological screening. Full article
(This article belongs to the Special Issue Anthozoan Toxins: Using New Approaches to Understand Their Composition, Distribution, and Function)
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26 pages, 6529 KiB  
Review
Sea Anemone Toxins: A Structural Overview
by Bruno Madio, Glenn F. King and Eivind A. B. Undheim
Mar. Drugs 2019, 17(6), 325; https://doi.org/10.3390/md17060325 - 01 Jun 2019
Cited by 54 | Viewed by 7756
Abstract
Sea anemones produce venoms of exceptional molecular diversity, with at least 17 different molecular scaffolds reported to date. These venom components have traditionally been classified according to pharmacological activity and amino acid sequence. However, this classification system suffers from vulnerabilities due to functional [...] Read more.
Sea anemones produce venoms of exceptional molecular diversity, with at least 17 different molecular scaffolds reported to date. These venom components have traditionally been classified according to pharmacological activity and amino acid sequence. However, this classification system suffers from vulnerabilities due to functional convergence and functional promiscuity. Furthermore, for most known sea anemone toxins, the exact receptors they target are either unknown, or at best incomplete. In this review, we first provide an overview of the sea anemone venom system and then focus on the venom components. We have organised the venom components by distinguishing firstly between proteins and non-proteinaceous compounds, secondly between enzymes and other proteins without enzymatic activity, then according to the structural scaffold, and finally according to molecular target. Full article
(This article belongs to the Special Issue Anthozoan Toxins: Using New Approaches to Understand Their Composition, Distribution, and Function)
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