{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,4]],"date-time":"2026-09-04T13:10:49Z","timestamp":1788527449273,"version":"build-2803163510"},"reference-count":12,"publisher":"SAGE Publications","issue":"8","license":[{"start":{"date-parts":[[2022,8,1]],"date-time":"2022-08-01T00:00:00Z","timestamp":1659312000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.sagepub.com\/page\/policies\/text-and-data-mining-license"}],"content-domain":{"domain":["journals.sagepub.com"],"crossmark-restriction":true},"short-container-title":["Microbial Drug Resistance"],"published-print":{"date-parts":[[2022,8]]},"abstract":"<jats:p>\n                    <jats:italic toggle=\"yes\">Pseudomonas aeruginosa<\/jats:italic>\n                    is an opportunist pathogen usually associated with life threatening infections and exhibits a set of intrinsic and acquired antimicrobial mechanisms. Although resistance to penicillins-like compounds is commonly associated with the chromosomal\n                    <jats:italic toggle=\"yes\">Pseudomonas<\/jats:italic>\n                    -derived cephalosporinases \u03b2-lactamase, the real contribution of OXA-50, a second chromosomally encoded \u03b2-lactamase, remains unclear. In this study, we characterized the biochemical properties of OXA-50, OXA-488, and OXA-494. Both oxacilinases differ from OXA-50 in two amino acids each. The\n                    <jats:italic toggle=\"yes\">bla<\/jats:italic>\n                    <jats:sub>OXA-50<\/jats:sub>\n                    ,\n                    <jats:italic toggle=\"yes\">bla<\/jats:italic>\n                    <jats:sub>OXA-488<\/jats:sub>\n                    , and\n                    <jats:italic toggle=\"yes\">bla<\/jats:italic>\n                    <jats:sub>OXA-494<\/jats:sub>\n                    were cloned into pET26b\n                    <jats:sup>+<\/jats:sup>\n                    that was transformed into\n                    <jats:italic toggle=\"yes\">Escherichia coli<\/jats:italic>\n                    DH5\u03b1 strain, expressed in\n                    <jats:italic toggle=\"yes\">E. coli<\/jats:italic>\n                    BL21 strain, and then purified for obtaining the hydrolytic parameters. Benzylpenicillin was the preferential substrate instead of oxacillin. Besides, OXA-488 showed a threefold increase in catalytic efficiency for benzylpenicillin, and it was twofold more efficient in hydrolyzing imipenem, compared with OXA-50, although such carbapenemase activity was considered weak. In addition, OXA-488 and OXA-494 showed an increased affinity for penicillins, which contributed to the increased catalytic efficiency against ampicillin, especially OXA-488. Chromosomally encoded resistance mechanisms are usually overshadowed by acquired mechanisms. However, understanding their real contribution is essential to comprehend the versatile profiles verified in\n                    <jats:italic toggle=\"yes\">P. aeruginosa<\/jats:italic>\n                    isolates. Such information can help to choose the best therapy in a scenario of limited options.\n                  <\/jats:p>","DOI":"10.1089\/mdr.2021.0405","type":"journal-article","created":{"date-parts":[[2022,7,14]],"date-time":"2022-07-14T10:22:31Z","timestamp":1657794151000},"page":"849-852","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":12,"title":["Kinetics Analysis of \u03b2-Lactams Hydrolysis by OXA-50 Variants of\n                    <i>Pseudomonas aeruginosa<\/i>"],"prefix":"10.1177","volume":"28","author":[{"given":"Ana Paula","family":"Streling","sequence":"first","affiliation":[{"name":"Laborat\u00f3rio ALERTA, Division of Infectious Diseases, Department of Internal Medicine, Escola Paulista de Medicina (EPM), Universidade Federal de S\u00e3o Paulo (UNIFESP), S\u00e3o Paulo, S\u00e3o Paulo, Brazil."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rodrigo","family":"Cay\u00f4","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio ALERTA, Division of Infectious Diseases, Department of Internal Medicine, Escola Paulista de Medicina (EPM), Universidade Federal de S\u00e3o Paulo (UNIFESP), S\u00e3o Paulo, S\u00e3o Paulo, Brazil."},{"name":"Laborat\u00f3rio de Imunologia e Microbiologia (LIB), Setor de Biologia Molecular, Microbiologia e Imunologia, Departamento de Ci\u00eancias Biol\u00f3gicas (DCB), Instituto de Ci\u00eancias Ambientais, Qu\u00edmicas e Farmac\u00eauticas (ICAQF), Universidade Federal de S\u00e3o Paulo (UNIFESP), Diadema, S\u00e3o Paulo, Brazil."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carolina S.","family":"Nodari","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio ALERTA, Division of Infectious Diseases, Department of Internal Medicine, Escola Paulista de Medicina (EPM), Universidade Federal de S\u00e3o Paulo (UNIFESP), S\u00e3o Paulo, S\u00e3o Paulo, Brazil."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luiz G.P.","family":"Almeida","sequence":"additional","affiliation":[{"name":"National Laboratory for Scientific Computing (LNCC), Petr\u00f3polis, Rio de Janeiro, Brazil."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Felipe","family":"Bronze","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Enzimologia, Department of Biophysics, Escola Paulista de Medicina (EPM), Universidade Federal de S\u00e3o Paulo (UNIFESP), S\u00e3o Paulo, S\u00e3o Paulo, Brazil."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andr\u00e9 Val\u00eancio","family":"Siqueira","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio ALERTA, Division of Infectious Diseases, Department of Internal Medicine, Escola Paulista de Medicina (EPM), Universidade Federal de S\u00e3o Paulo (UNIFESP), S\u00e3o Paulo, S\u00e3o Paulo, Brazil."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Adriana P.","family":"Matos","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio ALERTA, Division of Infectious Diseases, Department of Internal Medicine, Escola Paulista de Medicina (EPM), Universidade Federal de S\u00e3o Paulo (UNIFESP), S\u00e3o Paulo, S\u00e3o Paulo, Brazil."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vitor","family":"Oliveira","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Enzimologia, Department of Biophysics, Escola Paulista de Medicina (EPM), Universidade Federal de S\u00e3o Paulo (UNIFESP), S\u00e3o Paulo, S\u00e3o Paulo, Brazil."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ana Tereza R.","family":"Vasconcelos","sequence":"additional","affiliation":[{"name":"National Laboratory for Scientific Computing (LNCC), Petr\u00f3polis, Rio de Janeiro, Brazil."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marcelo F.M.","family":"Marcondes","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Enzimologia, Department of Biophysics, Escola Paulista de Medicina (EPM), Universidade Federal de S\u00e3o Paulo (UNIFESP), S\u00e3o Paulo, S\u00e3o Paulo, Brazil."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0913-768X","authenticated-orcid":false,"given":"Ana Cristina","family":"Gales","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio ALERTA, Division of Infectious Diseases, Department of Internal Medicine, Escola Paulista de Medicina (EPM), Universidade Federal de S\u00e3o Paulo (UNIFESP), S\u00e3o Paulo, S\u00e3o Paulo, Brazil."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"179","published-online":{"date-parts":[[2022,8,16]]},"reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.drup.2015.08.002"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijantimicag.2015.03.001"},{"key":"e_1_3_2_4_2","doi-asserted-by":"crossref","first-page":"2043","DOI":"10.1128\/AAC.48.6.2043-2048.2004","article-title":"Biochemical characterization of the naturally occurring oxacillinase OXA-50 of Pseudomonas aeruginosa","volume":"48","author":"Girlich D.","year":"2004","unstructured":"Girlich D., , Naas T., , and Nordmann P.. 2004. 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Chemother"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.01807-15"},{"key":"e_1_3_2_8_2","doi-asserted-by":"crossref","first-page":"4567","DOI":"10.1128\/AAC.49.11.4567-4575.2005","article-title":"Pseudomonas aeruginosa AmpR is a global transcriptional factor that regulates expression of AmpC and PoxB beta-lactamases, proteases, quorum sensing, and other virulence factors","volume":"49","author":"Kong K.F.","year":"2005","unstructured":"Kong K.F., , Jayawardena S.R, , Indulkar S.D, et al. 2005. Pseudomonas aeruginosa AmpR is a global transcriptional factor that regulates expression of AmpC and PoxB beta-lactamases, proteases, quorum sensing, and other virulence factors. Antimicrob. Agents Chemother. 49:4567\u20134575.","journal-title":"Antimicrob. Agents Chemother"},{"key":"e_1_3_2_9_2","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1093\/jac\/dkf210","article-title":"Molecular characterization of SPM-1, a novel metallo-beta-lactamase isolated in Latin America: report from the SENTRY antimicrobial surveillance programme","volume":"50","author":"Toleman M.A.","year":"2002","unstructured":"Toleman M.A., , Simm A.M, , Murphy T.A, et al. 2002. Molecular characterization of SPM-1, a novel metallo-beta-lactamase isolated in Latin America: report from the SENTRY antimicrobial surveillance programme. J. Antimicrob. Chemother. 50:673\u2013679.","journal-title":"J. Antimicrob. Chemother"},{"key":"e_1_3_2_10_2","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.bjid.2016.10.008","article-title":"Carbapenem-resistant and cephalosporin-susceptible: a worrisome phenotype among Pseudomonas aeruginosa clinical isolates in Brazil","volume":"21","author":"Campana E.H.","year":"2017","unstructured":"Campana E.H., , Xavier D.E, , Petrolini F.V, , Cordeiro-Moura J.R, , Araujo M.R, , and Gales A.C.. 2017. Carbapenem-resistant and cephalosporin-susceptible: a worrisome phenotype among Pseudomonas aeruginosa clinical isolates in Brazil. Braz. J. Infect. Dis. 21:57\u201362.","journal-title":"Braz. J. Infect. Dis"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1038\/35023079"},{"key":"e_1_3_2_12_2","author":"Nascimento A.P.","year":"1946","unstructured":"Nascimento A.P., , Ortiz M.F, , Martins W.M, et al. 2016. Intraclonal genome stability of the metallo-\u03b2-lactamase SPM-1-producing Pseudomonas aeruginosa ST277, an endemic clone disseminated in Brazilian Hospitals. Front. Microbiol. 7:1946.","journal-title":"et al"},{"key":"e_1_3_2_13_2","doi-asserted-by":"crossref","first-page":"5159","DOI":"10.1128\/AAC.00158-15","article-title":"Characterization of BKC-1 class A carbapenemase from Klebsiella pneumoniae clinical isolates in Brazil","volume":"59","author":"Nicoletti A.G.","year":"2015","unstructured":"Nicoletti A.G., , Marcondes M.F, , Martins W.M, et al. 2015. Characterization of BKC-1 class A carbapenemase from Klebsiella pneumoniae clinical isolates in Brazil. Antimicrob. Agents Chemother. 59:5159\u20135164.","journal-title":"Antimicrob. 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