Acontia, a Specialised Defensive Structure, Has Low Venom Complexity in <i>Calliactis polypus</i>
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...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-03-01
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| Series: | Toxins |
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| Online Access: | https://www.mdpi.com/2072-6651/15/3/218 |
| _version_ | 1797608762468466688 |
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| author | Hayden L. Smith Peter J. Prentis Scott E. Bryan Raymond S. Norton Daniel A. Broszczak |
| author_facet | Hayden L. Smith Peter J. Prentis Scott E. Bryan Raymond S. Norton Daniel A. Broszczak |
| author_sort | Hayden L. Smith |
| collection | DOAJ |
| 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 <i>Calliactis polypus</i>. 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 <i>Calliactis polypus</i> and the novel toxin identified here provide the basis for future research to define the function of acontial toxins in sea anemones. |
| first_indexed | 2024-03-11T05:49:10Z |
| format | Article |
| id | doaj.art-4a42fe5d9ae241b483da0f848ae0f232 |
| institution | Directory Open Access Journal |
| issn | 2072-6651 |
| language | English |
| last_indexed | 2024-03-11T05:49:10Z |
| publishDate | 2023-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Toxins |
| spelling | doaj.art-4a42fe5d9ae241b483da0f848ae0f2322023-11-17T14:14:31ZengMDPI AGToxins2072-66512023-03-0115321810.3390/toxins15030218Acontia, a Specialised Defensive Structure, Has Low Venom Complexity in <i>Calliactis polypus</i>Hayden L. Smith0Peter J. Prentis1Scott E. Bryan2Raymond S. Norton3Daniel A. Broszczak4School of Biology and Environmental Sciences, Faculty of Science, Queensland University of Technology, Brisbane, QLD 4001, AustraliaSchool of Biology and Environmental Sciences, Faculty of Science, Queensland University of Technology, Brisbane, QLD 4001, AustraliaSchool of Earth and Atmospheric Sciences, Faculty of Science, Queensland University of Technology, Brisbane, QLD 4001, AustraliaMedicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, VIC 3052, AustraliaSchool of Biomedical Sciences, Faculty of Health, Queensland University of Technology, Brisbane, QLD 4001, AustraliaPhylum 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 <i>Calliactis polypus</i>. 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 <i>Calliactis polypus</i> and the novel toxin identified here provide the basis for future research to define the function of acontial toxins in sea anemones.https://www.mdpi.com/2072-6651/15/3/218Actiniariaacontiaphylogeneticsproteomicstoxinvenom |
| spellingShingle | Hayden L. Smith Peter J. Prentis Scott E. Bryan Raymond S. Norton Daniel A. Broszczak Acontia, a Specialised Defensive Structure, Has Low Venom Complexity in <i>Calliactis polypus</i> Toxins Actiniaria acontia phylogenetics proteomics toxin venom |
| title | Acontia, a Specialised Defensive Structure, Has Low Venom Complexity in <i>Calliactis polypus</i> |
| title_full | Acontia, a Specialised Defensive Structure, Has Low Venom Complexity in <i>Calliactis polypus</i> |
| title_fullStr | Acontia, a Specialised Defensive Structure, Has Low Venom Complexity in <i>Calliactis polypus</i> |
| title_full_unstemmed | Acontia, a Specialised Defensive Structure, Has Low Venom Complexity in <i>Calliactis polypus</i> |
| title_short | Acontia, a Specialised Defensive Structure, Has Low Venom Complexity in <i>Calliactis polypus</i> |
| title_sort | acontia a specialised defensive structure has low venom complexity in i calliactis polypus i |
| topic | Actiniaria acontia phylogenetics proteomics toxin venom |
| url | https://www.mdpi.com/2072-6651/15/3/218 |
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