Penicillin-binding proteins (PBPs) determine antibiotic action in Langmuir monolayers as nanoarchitectonics mimetic membranes of methicillin-resistant Staphylococcus aureus

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dc.contributor.authorMartins, Beatriz Araújo
dc.contributor.authorDeffune, Elenice [UNESP]
dc.contributor.authorOliveira, Osvaldo N.
dc.contributor.authorMoraes, Marli Leite de
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.date.accessioned2022-05-01T15:46:14Z
dc.date.available2022-05-01T15:46:14Z
dc.date.issued2022-06-01
dc.description.abstractThe membrane of methicillin-resistant Staphylococcus aureus (MRSA) contains penicillin-binding proteins (PBPs) in the phospholipidic bilayer, with the protein PBP2a being linked with the resistance mechanism. In this work we confirm the role of PBP2a with molecular-level information obtained with Langmuir monolayers as cell membrane models. The MRSA cell membrane was mimicked with a mixed monolayer of dipalmitoyl phosphatidyl glycerol (DPPG) and cardiolipin (CL), also incorporating PBP2a. The surface pressure-area isotherms and the Brewster angle microscopy (BAM) images for these mixed monolayers were significantly affected by the antibiotic meropenem, which is PBP2a inhibitor. The meropenem effects were associated with the presence of PBP2a, as they were absent in the Langmuir monolayers without PBP2a. The relevance of PBP2a was confirmed with results where the antibiotic methicillin, known to be unsuitable to kill MRSA, had the same effects on mixed DPPG/CL and DPPG/CL-PBP2a monolayers since it prevented PBP2a from incorporating in the monolayer. The biological implication of the findings presented here is that a successful antibiotic against MRSA should be able to interact with PBP2a, but in the membrane.en
dc.description.affiliationFederal University of São Paulo Institute of Science and Technology, São José dos Campos, SP
dc.description.affiliationSão Paulo State University Blood Center Botucatu, SP
dc.description.affiliationSao Carlos Institute of Physics University of Sao Paulo CP 369, SP
dc.description.affiliationUnespSão Paulo State University Blood Center Botucatu, SP
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipInstituto Nacional de Ciência e Tecnologia em Eletrônica Orgânica
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipIdFAPESP: 2018/22214-6
dc.identifierhttp://dx.doi.org/10.1016/j.colsurfb.2022.112447
dc.identifier.citationColloids and Surfaces B: Biointerfaces, v. 214.
dc.identifier.doi10.1016/j.colsurfb.2022.112447
dc.identifier.issn1873-4367
dc.identifier.issn0927-7765
dc.identifier.scopus2-s2.0-85126661809
dc.identifier.urihttp://hdl.handle.net/11449/234287
dc.language.isoeng
dc.relation.ispartofColloids and Surfaces B: Biointerfaces
dc.sourceScopus
dc.subjectAntibiotic
dc.subjectBrewster angle microscope
dc.subjectLangmuir film
dc.subjectMeropenem
dc.subjectMethicillin-resistant Staphylococcus aureus
dc.subjectModel membrane
dc.titlePenicillin-binding proteins (PBPs) determine antibiotic action in Langmuir monolayers as nanoarchitectonics mimetic membranes of methicillin-resistant Staphylococcus aureusen
dc.typeArtigo

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