Proteomic analyses of the unexplored sea anemone Bunodactis verrucosa

Detalhes bibliográficos
Autor(a) principal: Domínguez-Pérez D.
Data de Publicação: 2018
Outros Autores: Campos A., Rodríguez A.A., Turkina M.V., Ribeiro T., Osorio H., Vasconcelos V., Antunes A.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: https://hdl.handle.net/10216/120397
Resumo: 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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spelling Proteomic analyses of the unexplored sea anemone Bunodactis verrucosaantibiotic agentantiinfective agentmarine toxinmetalloproteinaseneurotoxinprotein derivativeproteomepeptidetissue extractArticlebiosynthesisBunodactis verrucosacontrolled studydrug synthesisfeedingmatrix assisted laser desorption ionization time of flight mass spectrometrynonhumanprotein determinationprotein functionproteomicssea anemonetoxin analysistwo dimensional gel electrophoresisanimalbiologychemistrygene ontologygeneticsmatrix-assisted laser desorption-ionization mass spectrometrymicrobial sensitivity testsea anemoneAnimalsComputational BiologyGene OntologyMetalloproteasesMicrobial Sensitivity TestsNeurotoxinsPeptidesProteomicsSea AnemonesSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationTissue ExtractsCnidarian 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.MDPI20182018-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/10216/120397eng1660339710.3390/md16020042Domínguez-Pérez D.Campos A.Rodríguez A.A.Turkina M.V.Ribeiro T.Osorio H.Vasconcelos V.Antunes A.info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-11-29T12:33:35Zoai:repositorio-aberto.up.pt:10216/120397Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T23:22:35.084725Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Proteomic analyses of the unexplored sea anemone Bunodactis verrucosa
title Proteomic analyses of the unexplored sea anemone Bunodactis verrucosa
spellingShingle Proteomic analyses of the unexplored sea anemone Bunodactis verrucosa
Domínguez-Pérez D.
antibiotic agent
antiinfective agent
marine toxin
metalloproteinase
neurotoxin
protein derivative
proteome
peptide
tissue extract
Article
biosynthesis
Bunodactis verrucosa
controlled study
drug synthesis
feeding
matrix assisted laser desorption ionization time of flight mass spectrometry
nonhuman
protein determination
protein function
proteomics
sea anemone
toxin analysis
two dimensional gel electrophoresis
animal
biology
chemistry
gene ontology
genetics
matrix-assisted laser desorption-ionization mass spectrometry
microbial sensitivity test
sea anemone
Animals
Computational Biology
Gene Ontology
Metalloproteases
Microbial Sensitivity Tests
Neurotoxins
Peptides
Proteomics
Sea Anemones
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Tissue Extracts
title_short Proteomic analyses of the unexplored sea anemone Bunodactis verrucosa
title_full Proteomic analyses of the unexplored sea anemone Bunodactis verrucosa
title_fullStr Proteomic analyses of the unexplored sea anemone Bunodactis verrucosa
title_full_unstemmed Proteomic analyses of the unexplored sea anemone Bunodactis verrucosa
title_sort Proteomic analyses of the unexplored sea anemone Bunodactis verrucosa
author Domínguez-Pérez D.
author_facet Domínguez-Pérez D.
Campos A.
Rodríguez A.A.
Turkina M.V.
Ribeiro T.
Osorio H.
Vasconcelos V.
Antunes A.
author_role author
author2 Campos A.
Rodríguez A.A.
Turkina M.V.
Ribeiro T.
Osorio H.
Vasconcelos V.
Antunes A.
author2_role author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Domínguez-Pérez D.
Campos A.
Rodríguez A.A.
Turkina M.V.
Ribeiro T.
Osorio H.
Vasconcelos V.
Antunes A.
dc.subject.por.fl_str_mv antibiotic agent
antiinfective agent
marine toxin
metalloproteinase
neurotoxin
protein derivative
proteome
peptide
tissue extract
Article
biosynthesis
Bunodactis verrucosa
controlled study
drug synthesis
feeding
matrix assisted laser desorption ionization time of flight mass spectrometry
nonhuman
protein determination
protein function
proteomics
sea anemone
toxin analysis
two dimensional gel electrophoresis
animal
biology
chemistry
gene ontology
genetics
matrix-assisted laser desorption-ionization mass spectrometry
microbial sensitivity test
sea anemone
Animals
Computational Biology
Gene Ontology
Metalloproteases
Microbial Sensitivity Tests
Neurotoxins
Peptides
Proteomics
Sea Anemones
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Tissue Extracts
topic antibiotic agent
antiinfective agent
marine toxin
metalloproteinase
neurotoxin
protein derivative
proteome
peptide
tissue extract
Article
biosynthesis
Bunodactis verrucosa
controlled study
drug synthesis
feeding
matrix assisted laser desorption ionization time of flight mass spectrometry
nonhuman
protein determination
protein function
proteomics
sea anemone
toxin analysis
two dimensional gel electrophoresis
animal
biology
chemistry
gene ontology
genetics
matrix-assisted laser desorption-ionization mass spectrometry
microbial sensitivity test
sea anemone
Animals
Computational Biology
Gene Ontology
Metalloproteases
Microbial Sensitivity Tests
Neurotoxins
Peptides
Proteomics
Sea Anemones
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Tissue Extracts
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.
publishDate 2018
dc.date.none.fl_str_mv 2018
2018-01-01T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv https://hdl.handle.net/10216/120397
url https://hdl.handle.net/10216/120397
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 16603397
10.3390/md16020042
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
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dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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