Proteomic analyses of the unexplored sea anemone Bunodactis verrucosa
Autor(a) principal: | |
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Data de Publicação: | 2018 |
Outros Autores: | , , , , , , |
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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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 |
eu_rights_str_mv |
openAccess |
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 instacron:RCAAP |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
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RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799135526267125760 |