Proteomic profile of dormancy within Staphylococcus epidermidis biofilms using iTRAQ and label-free strategies

Detalhes bibliográficos
Autor(a) principal: Carvalhais, Virgínia Maria Dinis
Data de Publicação: 2015
Outros Autores: Cerca, Nuno, Vilanova, Manuel, Vitorino, Rui
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/1822/34591
Resumo: Staphylococcus epidermidis is an important nosocomial bacterium among carriers of indwelling medical devices, since it has a strong ability to form biofilms. The presence of dormant bacteria within a biofilm is one of the factors that contribute to biofilm antibiotic tolerance and immune evasion. Here, we provide a detailed characterization of the quantitative proteomic profile of S. epidermidis biofilms with different proportions of dormant bacteria. A total of 427 and 409 proteins were identified by label-free and label-based quantitative methodologies, respectively. From these, 29 proteins were found to be differentially expressed between S. epidermidis biofilms with prevented and induced dormancy. Proteins overexpressed in S. epidermidis with prevented dormancy were associated with ribosome synthesis pathway, which reflects the metabolic state of dormant bacteria. In the opposite, underexpressed proteins were related to catalytic activity and ion binding, with involvement in purine, arginine, and proline metabolism. Additionally, GTPase activity seems to be enhanced in S. epidermidis biofilm with induced dormancy. The role of magnesium in dormancy modulation was further investigated with bioinformatics tool based in predicted interactions. The main molecular function of proteins, which strongly interact with magnesium, was nucleic acid binding. Different proteomic strategies allowed to obtain similar results and evidenced that prevented dormancy led to an expression of a markedly different repertoire of proteins in comparison to the one of dormant biofilms.
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spelling Proteomic profile of dormancy within Staphylococcus epidermidis biofilms using iTRAQ and label-free strategiesCarbonylationDormancyemPAIiTRAQQuantitative proteomicsStaphylococcus epidermidis biofilmScience & TechnologyStaphylococcus epidermidis is an important nosocomial bacterium among carriers of indwelling medical devices, since it has a strong ability to form biofilms. The presence of dormant bacteria within a biofilm is one of the factors that contribute to biofilm antibiotic tolerance and immune evasion. Here, we provide a detailed characterization of the quantitative proteomic profile of S. epidermidis biofilms with different proportions of dormant bacteria. A total of 427 and 409 proteins were identified by label-free and label-based quantitative methodologies, respectively. From these, 29 proteins were found to be differentially expressed between S. epidermidis biofilms with prevented and induced dormancy. Proteins overexpressed in S. epidermidis with prevented dormancy were associated with ribosome synthesis pathway, which reflects the metabolic state of dormant bacteria. In the opposite, underexpressed proteins were related to catalytic activity and ion binding, with involvement in purine, arginine, and proline metabolism. Additionally, GTPase activity seems to be enhanced in S. epidermidis biofilm with induced dormancy. The role of magnesium in dormancy modulation was further investigated with bioinformatics tool based in predicted interactions. The main molecular function of proteins, which strongly interact with magnesium, was nucleic acid binding. Different proteomic strategies allowed to obtain similar results and evidenced that prevented dormancy led to an expression of a markedly different repertoire of proteins in comparison to the one of dormant biofilms.This work was funded by Fundacao para a Ciencia e a Tecnologia (FCT) and COMPETE grants PTDC/BIA-MIC/113450/2009, FCOMP-01-0124-FEDER-014309, QOPNA research unit (project PEst-C/QUI/UI0062/2013), RNEM (National Mass Spectrometry Network), and CENTRO-07-ST24-FEDER-002034. The authors also thank the FCT Strategic Project PEst-OE/EQB/LA0023/2013, the Project NORTE-07-0124-FEDER-000027, co-funded by the Programa Operacional Regional do Norte (ON.2 - O Novo Norte), QREN, FEDER, and the project RECI/EBB-EBI/0179/2012, FCOMP-01-0124-FEDER-027462. VC has an individual FCT fellowship (SFRH/BD/78235/2011). NC is an Investigator FCT.SpringerUniversidade do MinhoCarvalhais, Virgínia Maria DinisCerca, NunoVilanova, ManuelVitorino, Rui20152015-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/34591engCarvalhais, V.; Cerca, Nuno; Vilanova, Manuel; Vitorino, R., Proteomic profile of dormancy within Staphylococcus epidermidis biofilms using iTRAQ and label-free strategies. Applied Microbiology and Biotechnology, 99(6), 2751-2762, 2016.0175-75981432-061410.1007/s00253-015-6434-325672847http://www.springer.com/chemistry/biotechnology/journal/253info: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:RCAAP2023-07-21T12:02:50Zoai:repositorium.sdum.uminho.pt:1822/34591Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:52:53.675412Repositório 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 profile of dormancy within Staphylococcus epidermidis biofilms using iTRAQ and label-free strategies
title Proteomic profile of dormancy within Staphylococcus epidermidis biofilms using iTRAQ and label-free strategies
spellingShingle Proteomic profile of dormancy within Staphylococcus epidermidis biofilms using iTRAQ and label-free strategies
Carvalhais, Virgínia Maria Dinis
Carbonylation
Dormancy
emPAI
iTRAQ
Quantitative proteomics
Staphylococcus epidermidis biofilm
Science & Technology
title_short Proteomic profile of dormancy within Staphylococcus epidermidis biofilms using iTRAQ and label-free strategies
title_full Proteomic profile of dormancy within Staphylococcus epidermidis biofilms using iTRAQ and label-free strategies
title_fullStr Proteomic profile of dormancy within Staphylococcus epidermidis biofilms using iTRAQ and label-free strategies
title_full_unstemmed Proteomic profile of dormancy within Staphylococcus epidermidis biofilms using iTRAQ and label-free strategies
title_sort Proteomic profile of dormancy within Staphylococcus epidermidis biofilms using iTRAQ and label-free strategies
author Carvalhais, Virgínia Maria Dinis
author_facet Carvalhais, Virgínia Maria Dinis
Cerca, Nuno
Vilanova, Manuel
Vitorino, Rui
author_role author
author2 Cerca, Nuno
Vilanova, Manuel
Vitorino, Rui
author2_role author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Carvalhais, Virgínia Maria Dinis
Cerca, Nuno
Vilanova, Manuel
Vitorino, Rui
dc.subject.por.fl_str_mv Carbonylation
Dormancy
emPAI
iTRAQ
Quantitative proteomics
Staphylococcus epidermidis biofilm
Science & Technology
topic Carbonylation
Dormancy
emPAI
iTRAQ
Quantitative proteomics
Staphylococcus epidermidis biofilm
Science & Technology
description Staphylococcus epidermidis is an important nosocomial bacterium among carriers of indwelling medical devices, since it has a strong ability to form biofilms. The presence of dormant bacteria within a biofilm is one of the factors that contribute to biofilm antibiotic tolerance and immune evasion. Here, we provide a detailed characterization of the quantitative proteomic profile of S. epidermidis biofilms with different proportions of dormant bacteria. A total of 427 and 409 proteins were identified by label-free and label-based quantitative methodologies, respectively. From these, 29 proteins were found to be differentially expressed between S. epidermidis biofilms with prevented and induced dormancy. Proteins overexpressed in S. epidermidis with prevented dormancy were associated with ribosome synthesis pathway, which reflects the metabolic state of dormant bacteria. In the opposite, underexpressed proteins were related to catalytic activity and ion binding, with involvement in purine, arginine, and proline metabolism. Additionally, GTPase activity seems to be enhanced in S. epidermidis biofilm with induced dormancy. The role of magnesium in dormancy modulation was further investigated with bioinformatics tool based in predicted interactions. The main molecular function of proteins, which strongly interact with magnesium, was nucleic acid binding. Different proteomic strategies allowed to obtain similar results and evidenced that prevented dormancy led to an expression of a markedly different repertoire of proteins in comparison to the one of dormant biofilms.
publishDate 2015
dc.date.none.fl_str_mv 2015
2015-01-01T00:00:00Z
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 http://hdl.handle.net/1822/34591
url http://hdl.handle.net/1822/34591
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Carvalhais, V.; Cerca, Nuno; Vilanova, Manuel; Vitorino, R., Proteomic profile of dormancy within Staphylococcus epidermidis biofilms using iTRAQ and label-free strategies. Applied Microbiology and Biotechnology, 99(6), 2751-2762, 2016.
0175-7598
1432-0614
10.1007/s00253-015-6434-3
25672847
http://www.springer.com/chemistry/biotechnology/journal/253
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 Springer
publisher.none.fl_str_mv Springer
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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