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Acontia, a Specialised Defensive Structure, Has Low Venom Complexity in Calliactis polypus
Phylum Cnidaria represents a unique group among venomous taxa, with its delivery system organised as individual organelles, known as nematocysts, heterogeneously distributed across morphological structures rather than packaged as a specialised organ. Acontia are packed with large nematocysts that ar...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10051995/ https://www.ncbi.nlm.nih.gov/pubmed/36977109 http://dx.doi.org/10.3390/toxins15030218 |
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author | Smith, Hayden L. Prentis, Peter J. Bryan, Scott E. Norton, Raymond S. Broszczak, Daniel A. |
author_facet | Smith, Hayden L. Prentis, Peter J. Bryan, Scott E. Norton, Raymond S. Broszczak, Daniel A. |
author_sort | Smith, Hayden L. |
collection | PubMed |
description | Phylum Cnidaria represents a unique group among venomous taxa, with its delivery system organised as individual organelles, known as nematocysts, heterogeneously distributed across morphological structures rather than packaged as a specialised organ. Acontia are packed with large nematocysts that are expelled from sea anemones during aggressive encounters with predatory species and are found in a limited number of species in the superfamily Metridioidea. Little is known about this specialised structure other than the commonly accepted hypothesis of its role in defence and a rudimentary understanding of its toxin content and activity. This study utilised previously published transcriptomic data and new proteomic analyses to expand this knowledge by identifying the venom profile of acontia in Calliactis polypus. Using mass spectrometry, we found limited toxin diversity in the proteome of acontia, with an abundance of a sodium channel toxin type I, and a novel toxin with two ShK-like domains. Additionally, genomic evidence suggests that the proposed novel toxin is ubiquitous across sea anemone lineages. Overall, the venom profile of acontia in Calliactis polypus and the novel toxin identified here provide the basis for future research to define the function of acontial toxins in sea anemones. |
format | Online Article Text |
id | pubmed-10051995 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-100519952023-03-30 Acontia, a Specialised Defensive Structure, Has Low Venom Complexity in Calliactis polypus Smith, Hayden L. Prentis, Peter J. Bryan, Scott E. Norton, Raymond S. Broszczak, Daniel A. Toxins (Basel) Article Phylum Cnidaria represents a unique group among venomous taxa, with its delivery system organised as individual organelles, known as nematocysts, heterogeneously distributed across morphological structures rather than packaged as a specialised organ. Acontia are packed with large nematocysts that are expelled from sea anemones during aggressive encounters with predatory species and are found in a limited number of species in the superfamily Metridioidea. Little is known about this specialised structure other than the commonly accepted hypothesis of its role in defence and a rudimentary understanding of its toxin content and activity. This study utilised previously published transcriptomic data and new proteomic analyses to expand this knowledge by identifying the venom profile of acontia in Calliactis polypus. Using mass spectrometry, we found limited toxin diversity in the proteome of acontia, with an abundance of a sodium channel toxin type I, and a novel toxin with two ShK-like domains. Additionally, genomic evidence suggests that the proposed novel toxin is ubiquitous across sea anemone lineages. Overall, the venom profile of acontia in Calliactis polypus and the novel toxin identified here provide the basis for future research to define the function of acontial toxins in sea anemones. MDPI 2023-03-12 /pmc/articles/PMC10051995/ /pubmed/36977109 http://dx.doi.org/10.3390/toxins15030218 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Smith, Hayden L. Prentis, Peter J. Bryan, Scott E. Norton, Raymond S. Broszczak, Daniel A. Acontia, a Specialised Defensive Structure, Has Low Venom Complexity in Calliactis polypus |
title | Acontia, a Specialised Defensive Structure, Has Low Venom Complexity in Calliactis polypus |
title_full | Acontia, a Specialised Defensive Structure, Has Low Venom Complexity in Calliactis polypus |
title_fullStr | Acontia, a Specialised Defensive Structure, Has Low Venom Complexity in Calliactis polypus |
title_full_unstemmed | Acontia, a Specialised Defensive Structure, Has Low Venom Complexity in Calliactis polypus |
title_short | Acontia, a Specialised Defensive Structure, Has Low Venom Complexity in Calliactis polypus |
title_sort | acontia, a specialised defensive structure, has low venom complexity in calliactis polypus |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10051995/ https://www.ncbi.nlm.nih.gov/pubmed/36977109 http://dx.doi.org/10.3390/toxins15030218 |
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