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Here, we addressed these questions by using\n            <jats:named-content content-type=\"genus-species\">Acinetobacter baylyi<\/jats:named-content>\n            as a model species and a combination of methodologies aimed to characterize OM channels in their original membrane environment. Kinetic and competition analyses of imipenem (IPM) uptake by\n            <jats:named-content content-type=\"genus-species\">A. baylyi<\/jats:named-content>\n            whole cells allowed us to identify different carbapenem-specific OM uptake sites. Comparative analyses of IPM uptake by\n            <jats:named-content content-type=\"genus-species\">A. baylyi<\/jats:named-content>\n            wild-type (WT) cells and \u0394\n            <jats:italic>carO<\/jats:italic>\n            mutants lacking CarO indicated that this OM protein provided a carbapenem uptake site displaying saturable kinetics and common binding sites for basic amino acids compatible with a specific channel. The kinetic analysis uncovered another carbapenem-specific channel displaying a somewhat lower affinity for IPM than that of CarO and, in addition, common binding sites for basic amino acids as determined by competition studies. The use of\n            <jats:named-content content-type=\"genus-species\">A. baylyi<\/jats:named-content>\n            gene deletion mutants lacking OM proteins proposed to function in carbapenem uptake in\n            <jats:named-content content-type=\"genus-species\">Acinetobacter baumannii<\/jats:named-content>\n            indicated that CarO and OprD\/OccAB1 mutants displayed low but consistent reductions in susceptibility to different carbapenems, including IPM, meropenem, and ertapenem. These two mutants also showed impaired growth on\n            <jats:sc>l<\/jats:sc>\n            -Arg but not on other carbon sources, further supporting a role of CarO and OprD\/OccAB1 in basic amino acid and carbapenem uptake. A multiple-carbapenem-channel scenario may provide clues to our understanding of the contribution of OM channel loss or mutation to the carbapenem-resistant phenotype evolved by pathogenic members of the\n            <jats:named-content content-type=\"genus-species\">Acinetobacter<\/jats:named-content>\n            genus.\n          <\/jats:p>","DOI":"10.1128\/aac.01737-16","type":"journal-article","created":{"date-parts":[[2017,1,10]],"date-time":"2017-01-10T02:30:27Z","timestamp":1484015427000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":29,"title":["The Acinetobacter Outer Membrane Contains Multiple Specific Channels for Carbapenem \u03b2-Lactams as Revealed by Kinetic Characterization Analyses of Imipenem Permeation into Acinetobacter baylyi Cells"],"prefix":"10.1128","volume":"61","author":[{"given":"Jorgelina","family":"Mor\u00e1n-Barrio","sequence":"first","affiliation":[{"name":"Instituto de Biolog\u00eda 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