Publication
Proteomic analyses of the unexplored sea anemone Bunodactis verrucosa
| Summary: | Cnidarian toxic products, particularly peptide toxins, constitute a promising target for biomedicine research. Indeed, cnidarians are considered as the largest phylum of generally toxic animals. However, research on peptides and toxins of sea anemones is still limited. Moreover, most of the toxins from sea anemones have been discovered by classical purification approaches. Recently, high-throughput methodologies have been used for this purpose but in other Phyla. Hence, the present work was focused on the proteomic analyses of whole-body extract from the unexplored sea anemone Bunodactis verrucosa. The proteomic analyses applied were based on two methods: two-dimensional gel electrophoresis combined with MALDI-TOF/TOF and shotgun proteomic approach. In total, 413 proteins were identified, but only eight proteins were identified from gel-based analyses. Such proteins are mainly involved in basal metabolism and biosynthesis of antibiotics as the most relevant pathways. In addition, some putative toxins including metalloproteinases and neurotoxins were also identified. These findings reinforce the significance of the production of antimicrobial compounds and toxins by sea anemones, which play a significant role in defense and feeding. In general, the present study provides the first proteome map of the sea anemone B. verrucosa stablishing a reference for future studies in the discovery of new compounds. © 2018 by the authors. |
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| Subject: | antiinfective agent Sea Anemones animal protein function Animals microbial sensitivity test proteome gene ontology sea anemone biosynthesis toxin analysis Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization biology Computational Biology Neurotoxins marine toxin protein determination neurotoxin Bunodactis verrucosa peptide antibiotic agent nonhuman Tissue Extracts matrix assisted laser desorption ionization time of flight mass spectrometry metalloproteinase protein derivative feeding matrix-assisted laser desorption-ionization mass spectrometry genetics drug synthesis Article chemistry Metalloproteases tissue extract Gene Ontology Microbial Sensitivity Tests two dimensional gel electrophoresis proteomics controlled study Peptides Proteomics |
| Country: | Portugal |
| Document type: | journal article |
| Access type: | Open |
| Associated institution: | Repositório Aberto da Universidade do Porto |
| Language: | English |
| Origin: | Repositório Aberto da Universidade do Porto |
| _version_ | 1850560656890134528 |
|---|---|
| conditionsOfAccess_str | open access |
| country_str | PT |
| description | Cnidarian toxic products, particularly peptide toxins, constitute a promising target for biomedicine research. Indeed, cnidarians are considered as the largest phylum of generally toxic animals. However, research on peptides and toxins of sea anemones is still limited. Moreover, most of the toxins from sea anemones have been discovered by classical purification approaches. Recently, high-throughput methodologies have been used for this purpose but in other Phyla. Hence, the present work was focused on the proteomic analyses of whole-body extract from the unexplored sea anemone Bunodactis verrucosa. The proteomic analyses applied were based on two methods: two-dimensional gel electrophoresis combined with MALDI-TOF/TOF and shotgun proteomic approach. In total, 413 proteins were identified, but only eight proteins were identified from gel-based analyses. Such proteins are mainly involved in basal metabolism and biosynthesis of antibiotics as the most relevant pathways. In addition, some putative toxins including metalloproteinases and neurotoxins were also identified. These findings reinforce the significance of the production of antimicrobial compounds and toxins by sea anemones, which play a significant role in defense and feeding. In general, the present study provides the first proteome map of the sea anemone B. verrucosa stablishing a reference for future studies in the discovery of new compounds. © 2018 by the authors. |
| documentTypeURL_str | http://purl.org/coar/resource_type/c_6501 |
| documentType_str | journal article |
| id | ff10befb-4523-4395-9d0a-724748b34d09 |
| identifierHandle_str | https://hdl.handle.net/10216/120397 |
| language | eng |
| relatedInstitutions_str_mv | Repositório Aberto da Universidade do Porto |
| resourceName_str | Repositório Aberto da Universidade do Porto |
| spellingShingle | Proteomic analyses of the unexplored sea anemone Bunodactis verrucosa antiinfective agent Sea Anemones animal protein function Animals microbial sensitivity test proteome gene ontology sea anemone biosynthesis toxin analysis Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization biology Computational Biology Neurotoxins marine toxin protein determination neurotoxin Bunodactis verrucosa peptide antibiotic agent nonhuman Tissue Extracts matrix assisted laser desorption ionization time of flight mass spectrometry metalloproteinase protein derivative feeding matrix-assisted laser desorption-ionization mass spectrometry genetics drug synthesis Article chemistry Metalloproteases tissue extract Gene Ontology Microbial Sensitivity Tests two dimensional gel electrophoresis proteomics controlled study Peptides Proteomics |
| title | Proteomic analyses of the unexplored sea anemone Bunodactis verrucosa |
| topic | antiinfective agent Sea Anemones animal protein function Animals microbial sensitivity test proteome gene ontology sea anemone biosynthesis toxin analysis Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization biology Computational Biology Neurotoxins marine toxin protein determination neurotoxin Bunodactis verrucosa peptide antibiotic agent nonhuman Tissue Extracts matrix assisted laser desorption ionization time of flight mass spectrometry metalloproteinase protein derivative feeding matrix-assisted laser desorption-ionization mass spectrometry genetics drug synthesis Article chemistry Metalloproteases tissue extract Gene Ontology Microbial Sensitivity Tests two dimensional gel electrophoresis proteomics controlled study Peptides Proteomics |
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