Proteomic Diversity of the Sea Anemone : Comparative Analysis of Nematocyst Venom, Mucus, and Tissue-Specific Profiles.
Fuente:
PubMed
Saved in:
| Main Authors: | , , , , , , |
|---|---|
| Format: | Artículo científico |
| Language: | en |
| Published: |
Marine drugs
2025
|
| Subjects: | |
| Online Access: | |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1868266239811387393 |
|---|---|
| author | Barroso, Ricardo Alexandre Rodrigues, Tomás Campos, Alexandre Almeida, Daniela Guardiola, Francisco A Turkina, Maria V Antunes, Agostinho |
| author_facet | Barroso, Ricardo Alexandre Rodrigues, Tomás Campos, Alexandre Almeida, Daniela Guardiola, Francisco A Turkina, Maria V Antunes, Agostinho Barroso, Ricardo Alexandre Rodrigues, Tomás Campos, Alexandre Almeida, Daniela Guardiola, Francisco A Turkina, Maria V Antunes, Agostinho |
| collection | PubMed - marine biology |
| contents | Proteomic Diversity of the Sea Anemone : Comparative Analysis of Nematocyst Venom, Mucus, and Tissue-Specific Profiles. Barroso, Ricardo Alexandre Rodrigues, Tomás Campos, Alexandre Almeida, Daniela Guardiola, Francisco A Turkina, Maria V Antunes, Agostinho Animals Sea Anemones Proteomics Nematocyst Cnidarian Venoms Mucus Proteome Antimicrobial Peptides 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 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 , offering a critical foundation for exploring novel bioactive compounds and valuable insights into its molecular complexity. |
| format | Artículo científico |
| id | pubmed_39997203 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Marine drugs |
| record_format | pubmed |
| spellingShingle | Proteomic Diversity of the Sea Anemone : Comparative Analysis of Nematocyst Venom, Mucus, and Tissue-Specific Profiles. Barroso, Ricardo Alexandre Rodrigues, Tomás Campos, Alexandre Almeida, Daniela Guardiola, Francisco A Turkina, Maria V Antunes, Agostinho Animals Sea Anemones Proteomics Nematocyst Cnidarian Venoms Mucus Proteome Antimicrobial Peptides Proteomic Diversity of the Sea Anemone : Comparative Analysis of Nematocyst Venom, Mucus, and Tissue-Specific Profiles. Barroso, Ricardo Alexandre Rodrigues, Tomás Campos, Alexandre Almeida, Daniela Guardiola, Francisco A Turkina, Maria V Antunes, Agostinho Animals Sea Anemones Proteomics Nematocyst Cnidarian Venoms Mucus Proteome Antimicrobial Peptides 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 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 , offering a critical foundation for exploring novel bioactive compounds and valuable insights into its molecular complexity. |
| title | Proteomic Diversity of the Sea Anemone : Comparative Analysis of Nematocyst Venom, Mucus, and Tissue-Specific Profiles. |
| topic | Animals Sea Anemones Proteomics Nematocyst Cnidarian Venoms Mucus Proteome Antimicrobial Peptides |
| url | https://pubmed.ncbi.nlm.nih.gov/39997203/ |