Comparative Proteomics of Methicillin-Resistant Staphylococcus aureus Subjected to Synergistic Effects of the Lantibiotic Nisin and Oxacillin

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dc.contributor.authorBergamo Alves, Fernanda Cristina [UNESP]
dc.contributor.authorAlbano, Mariana [UNESP]
dc.contributor.authorMurbach Teles Andrade, Bruna Fernanda [UNESP]
dc.contributor.authorChechi, Jessica Luana [UNESP]
dc.contributor.authorMarques Pereira, Ana Flavia [UNESP]
dc.contributor.authorFurlanetto, Alessandra [UNESP]
dc.contributor.authorMores Rall, Vera Lucia [UNESP]
dc.contributor.authorHenrique Fernandes, Ana Angelica [UNESP]
dc.contributor.authorSantos, Lucilene Delazari dos [UNESP]
dc.contributor.authorBarbosa, Lidiane Nunes
dc.contributor.authorFernandes Junior, Ary [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniv Paranaense UNIPAR
dc.date.accessioned2019-10-04T12:39:10Z
dc.date.available2019-10-04T12:39:10Z
dc.date.issued2019-06-25
dc.description.abstractWe investigated the responses and mechanisms of action of methicillin-resistant Staphylococcus aureus (MRSA) metabolism when exposed under sublethal concentrations of the synergistic antibacterial combination of nisin + oxacillin (1/4 of maximum sublethal concentration) and sublethal concentrations of oxacillin only and nisin only. A total of 135 proteins were identified, showing an alteration in the expression of 85 proteins when treatment was compared with untreated bacteria (control). When the bacteria were treated using the combination, there was an increase in the expression of proteins related to resistance (e.g., beta-lactamase) and also in the ones involved in protein synthesis, and there was a decrease in the expression of proteins related to stress and alterations in proteins related to bacterial energy metabolism. Bacterial oxidative stress showed that the combination was able to induce oxidative stress (p < 0.05) and increase enzyme activities and lipid hydroperoxide levels compared with individual treatments. The analysis of cell ultrastructure showed damage in MRSA, especially on the bacterial wall and the plasma membrane, with cell lysis and death. Thus, the changes caused by these treatments affected different proteins related to the bacterial biological processes and signaling pathways such as cell division, structure, stress, regulation, bacterial resistance, protein synthesis, gene expression, energetic metabolism, and virulence. It was observed that synergism among antimicrobials has high potential in therapeutic use and may reduce the required amounts of antibacterial substances in addition to being effective on different targets in bacterial cells.en
dc.description.affiliationSao Paulo State Univ UNESP, IBB, Dept Microbiol & Immunol, BR-18618691 Botucatu, SP, Brazil
dc.description.affiliationSao Paulo State Univ UNESP, IBB, Dept Chem & Biochem, Botucatu, SP, Brazil
dc.description.affiliationSao Paulo State Univ UNESP, Botucatu Med Sch FMB, Grad Program Trop Dis, Botucatu, SP, Brazil
dc.description.affiliationSao Paulo State Univ UNESP, Ctr Study Venom & Venomous Anim CEVAP, Botucatu, SP, Brazil
dc.description.affiliationUniv Paranaense UNIPAR, Grad Program Anim Sci Emphasis Bioact Prod, Umuarama, Brazil
dc.description.affiliationSao Paulo State Univ UNESP, IBB, Elect Microscopy Ctr, Botucatu, SP, Brazil
dc.description.affiliationUnespSao Paulo State Univ UNESP, IBB, Dept Microbiol & Immunol, BR-18618691 Botucatu, SP, Brazil
dc.description.affiliationUnespSao Paulo State Univ UNESP, IBB, Dept Chem & Biochem, Botucatu, SP, Brazil
dc.description.affiliationUnespSao Paulo State Univ UNESP, Botucatu Med Sch FMB, Grad Program Trop Dis, Botucatu, SP, Brazil
dc.description.affiliationUnespSao Paulo State Univ UNESP, Ctr Study Venom & Venomous Anim CEVAP, Botucatu, SP, Brazil
dc.description.affiliationUnespSao Paulo State Univ UNESP, IBB, Elect Microscopy Ctr, Botucatu, SP, Brazil
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipIdFAPESP: 2015/14278-6
dc.format.extent11
dc.identifierhttp://dx.doi.org/10.1089/mdr.2019.0038
dc.identifier.citationMicrobial Drug Resistance. New Rochelle: Mary Ann Liebert, Inc, 11 p., 2019.
dc.identifier.doi10.1089/mdr.2019.0038
dc.identifier.issn1076-6294
dc.identifier.lattes3368404126695911
dc.identifier.urihttp://hdl.handle.net/11449/185854
dc.identifier.wosWOS:000473305100001
dc.language.isoeng
dc.publisherMary Ann Liebert, Inc
dc.relation.ispartofMicrobial Drug Resistance
dc.rights.accessRightsAcesso aberto
dc.sourceWeb of Science
dc.subjectantimicrobial peptide
dc.subjectbacterial resistance
dc.subjectsynergism
dc.subjectLC-MS/MS
dc.subjectoxidative stress
dc.subjecttransmission electron microscopy
dc.titleComparative Proteomics of Methicillin-Resistant Staphylococcus aureus Subjected to Synergistic Effects of the Lantibiotic Nisin and Oxacillinen
dc.typeArtigo
dcterms.rightsHolderMary Ann Liebert, Inc
unesp.advisor.lattes3368404126695911
unesp.author.lattes8310835825824360[11]
unesp.author.orcid0000-0002-4640-5332[1]
unesp.author.orcid0000-0002-2744-2824[11]

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Coleções

Artigos - Microbiologia e Imunologia - IBB
Artigos - Doenças Tropicais e Diagnósticos por Imagem - FMB
Artigos - Química e Bioquímica - IBB
Botucatu - CEVAP - Centro de Estudos de Venenos e Animais Peçonhentos
Botucatu - CME - Centro de Microscopia Eletrônica