caa a22 4500 605499071 CHVBK 20210128100549.0 cr unu---uuuuu 210128e20150301xx s 000 0 eng 10.1007/s00253-015-6434-3 doi (NATIONALLICENCE)springer-10.1007/s00253-015-6434-3 Proteomic profile of dormancy within Staphylococcus epidermidis biofilms using iTRAQ and label-free strategies [Elektronische Daten] [Virginia Carvalhais, Nuno Cerca, Manuel Vilanova, Rui Vitorino] 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. Springer-Verlag Berlin Heidelberg, 2015 Carbonylation nationallicence Dormancy nationallicence emPAI nationallicence iTRAQ nationallicence Quantitative proteomics nationallicence Staphylococcus epidermidis biofilm nationallicence Carvalhais Virginia Centre of Biological Engineering (CEB), Laboratory of Research in Biofilms Rosário Oliveira (LIBRO), University of Minho, Campus de Gualtar, 4710-057, Braga, Portugal aut Cerca Nuno Centre of Biological Engineering (CEB), Laboratory of Research in Biofilms Rosário Oliveira (LIBRO), University of Minho, Campus de Gualtar, 4710-057, Braga, Portugal aut Vilanova Manuel Instituto de Biologia Molecular e Celular (IBMC), Rua do Campo Alegre 83, Porto, Portugal aut Vitorino Rui QOPNA, Mass Spectrometry Center, Department of Chemistry, University of Aveiro, 3810-193, Aveiro, Portugal aut Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/6(2015-03-01), 2751-2762 0175-7598 99:6<2751 2015 99 253 https://doi.org/10.1007/s00253-015-6434-3 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00253-015-6434-3 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Carvalhais Virginia Centre of Biological Engineering (CEB), Laboratory of Research in Biofilms Rosário Oliveira (LIBRO), University of Minho, Campus de Gualtar, 4710-057, Braga, Portugal aut NATIONALLICENCE 700 1- Cerca Nuno Centre of Biological Engineering (CEB), Laboratory of Research in Biofilms Rosário Oliveira (LIBRO), University of Minho, Campus de Gualtar, 4710-057, Braga, Portugal aut NATIONALLICENCE 700 1- Vilanova Manuel Instituto de Biologia Molecular e Celular (IBMC), Rua do Campo Alegre 83, Porto, Portugal aut NATIONALLICENCE 700 1- Vitorino Rui QOPNA, Mass Spectrometry Center, Department of Chemistry, University of Aveiro, 3810-193, Aveiro, Portugal aut NATIONALLICENCE 773 0- Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/6(2015-03-01), 2751-2762 0175-7598 99:6<2751 2015 99 253