Proteomic Diversity of the Sea Anemone <i>Actinia fragacea</i>: Comparative Analysis of Nematocyst Venom, Mucus, and Tissue-Specific Profiles
Sea anemones (Actiniaria, Cnidaria) are promising targets for biomedical research, as they produce unique bioactive compounds, including toxins and antimicrobial peptides (AMPs). However, the diversity and mechanisms underlying their chemical defenses remain poorly understood. In this study, we inve...
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2025-02-01
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| Series: | Marine Drugs |
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| author | Ricardo Alexandre Barroso Tomás Rodrigues Alexandre Campos Daniela Almeida Francisco A. Guardiola Maria V. Turkina Agostinho Antunes |
| author_facet | Ricardo Alexandre Barroso Tomás Rodrigues Alexandre Campos Daniela Almeida Francisco A. Guardiola Maria V. Turkina Agostinho Antunes |
| author_sort | Ricardo Alexandre Barroso |
| collection | DOAJ |
| description | Sea anemones (Actiniaria, Cnidaria) are promising targets for biomedical research, as they produce unique bioactive compounds, including toxins and antimicrobial peptides (AMPs). However, the diversity and mechanisms underlying their chemical defenses remain poorly understood. In this study, we investigate the proteomic profiles of the unexplored sea anemone <i>Actinia fragacea</i> by analyzing its venom nematocyst extract, tissues, and mucus secretion. A total of 4011 different proteins were identified, clustered into 3383 protein groups. Among the 83 putative toxins detected, actinoporins, neurotoxins, and phospholipase A2 were uncovered, as well as two novel zinc metalloproteinases with two specific domains (ShK) associated with potassium channel inhibition. Common Gene Ontology (GO) terms were related to immune responses, cell adhesion, protease inhibition, and tissue regeneration. Furthermore, 1406 of the 13,276 distinct peptides identified were predicted as potential AMPs, including a putative Aurelin-like AMP localized within the nematocysts. This discovery highlights and strengthens the evidence for a cnidarian-exclusive Aurelin peptide family. Several other bioactive compounds with distinctive defense functions were also detected, including enzymes, pattern recognition proteins (PRPs), and neuropeptides. This study provides the first proteome map of <i>A. fragacea</i>, offering a critical foundation for exploring novel bioactive compounds and valuable insights into its molecular complexity. |
| format | Article |
| id | doaj-art-b6da8d159fee48599f9c52db0400b1f6 |
| institution | DOAJ |
| issn | 1660-3397 |
| language | English |
| publishDate | 2025-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Marine Drugs |
| spelling | doaj-art-b6da8d159fee48599f9c52db0400b1f62025-08-20T02:45:00ZengMDPI AGMarine Drugs1660-33972025-02-012327910.3390/md23020079Proteomic Diversity of the Sea Anemone <i>Actinia fragacea</i>: Comparative Analysis of Nematocyst Venom, Mucus, and Tissue-Specific ProfilesRicardo Alexandre Barroso0Tomás Rodrigues1Alexandre Campos2Daniela Almeida3Francisco A. Guardiola4Maria V. Turkina5Agostinho Antunes6CIIMAR/CIMAR—Interdisciplinary Centre of Marine and Environmental Research, University of Porto, Terminal de Cruzeiros do Porto de Leixões, Av. General Norton de Matos, s/n, 4450-208 Porto, PortugalCIIMAR/CIMAR—Interdisciplinary Centre of Marine and Environmental Research, University of Porto, Terminal de Cruzeiros do Porto de Leixões, Av. General Norton de Matos, s/n, 4450-208 Porto, PortugalCIIMAR/CIMAR—Interdisciplinary Centre of Marine and Environmental Research, University of Porto, Terminal de Cruzeiros do Porto de Leixões, Av. General Norton de Matos, s/n, 4450-208 Porto, PortugalDepartment of Zoology and Physical Anthropology, Faculty of Biology, University of Murcia, Campus of International Excellence, Campus Mare Nostrum, 30100 Murcia, SpainImmunobiology for Aquaculture Group, Department of Cell Biology and Histology, Faculty of Biology, Regional Campus of International Excellence “Campus Mare Nostrum”, University of Murcia, 30100 Murcia, SpainDepartment of Biomedical and Clinical Sciences, Faculty of Medicine and Clinical Sciences, Linköping University, 581 83 Linköping, SwedenCIIMAR/CIMAR—Interdisciplinary Centre of Marine and Environmental Research, University of Porto, Terminal de Cruzeiros do Porto de Leixões, Av. General Norton de Matos, s/n, 4450-208 Porto, PortugalSea anemones (Actiniaria, Cnidaria) are promising targets for biomedical research, as they produce unique bioactive compounds, including toxins and antimicrobial peptides (AMPs). However, the diversity and mechanisms underlying their chemical defenses remain poorly understood. In this study, we investigate the proteomic profiles of the unexplored sea anemone <i>Actinia fragacea</i> by analyzing its venom nematocyst extract, tissues, and mucus secretion. A total of 4011 different proteins were identified, clustered into 3383 protein groups. Among the 83 putative toxins detected, actinoporins, neurotoxins, and phospholipase A2 were uncovered, as well as two novel zinc metalloproteinases with two specific domains (ShK) associated with potassium channel inhibition. Common Gene Ontology (GO) terms were related to immune responses, cell adhesion, protease inhibition, and tissue regeneration. Furthermore, 1406 of the 13,276 distinct peptides identified were predicted as potential AMPs, including a putative Aurelin-like AMP localized within the nematocysts. This discovery highlights and strengthens the evidence for a cnidarian-exclusive Aurelin peptide family. Several other bioactive compounds with distinctive defense functions were also detected, including enzymes, pattern recognition proteins (PRPs), and neuropeptides. This study provides the first proteome map of <i>A. fragacea</i>, offering a critical foundation for exploring novel bioactive compounds and valuable insights into its molecular complexity.https://www.mdpi.com/1660-3397/23/2/79sea anemonesCnidariaproteomicstoxinsantimicrobial peptides (AMPs) |
| spellingShingle | Ricardo Alexandre Barroso Tomás Rodrigues Alexandre Campos Daniela Almeida Francisco A. Guardiola Maria V. Turkina Agostinho Antunes Proteomic Diversity of the Sea Anemone <i>Actinia fragacea</i>: Comparative Analysis of Nematocyst Venom, Mucus, and Tissue-Specific Profiles Marine Drugs sea anemones Cnidaria proteomics toxins antimicrobial peptides (AMPs) |
| title | Proteomic Diversity of the Sea Anemone <i>Actinia fragacea</i>: Comparative Analysis of Nematocyst Venom, Mucus, and Tissue-Specific Profiles |
| title_full | Proteomic Diversity of the Sea Anemone <i>Actinia fragacea</i>: Comparative Analysis of Nematocyst Venom, Mucus, and Tissue-Specific Profiles |
| title_fullStr | Proteomic Diversity of the Sea Anemone <i>Actinia fragacea</i>: Comparative Analysis of Nematocyst Venom, Mucus, and Tissue-Specific Profiles |
| title_full_unstemmed | Proteomic Diversity of the Sea Anemone <i>Actinia fragacea</i>: Comparative Analysis of Nematocyst Venom, Mucus, and Tissue-Specific Profiles |
| title_short | Proteomic Diversity of the Sea Anemone <i>Actinia fragacea</i>: Comparative Analysis of Nematocyst Venom, Mucus, and Tissue-Specific Profiles |
| title_sort | proteomic diversity of the sea anemone i actinia fragacea i comparative analysis of nematocyst venom mucus and tissue specific profiles |
| topic | sea anemones Cnidaria proteomics toxins antimicrobial peptides (AMPs) |
| url | https://www.mdpi.com/1660-3397/23/2/79 |
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