{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,13]],"date-time":"2026-05-13T04:35:37Z","timestamp":1778646937638,"version":"3.51.4"},"reference-count":36,"publisher":"American Society for Microbiology","issue":"5","license":[{"start":{"date-parts":[[1998,5,1]],"date-time":"1998-05-01T00:00:00Z","timestamp":893980800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Antimicrob Agents Chemother"],"published-print":{"date-parts":[[1998,5]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Sanfetrinem is a trinem \u03b2-lactam which can be administered orally as a hexatil ester. We examined whether its \u03b2-lactamase interactions resembled those of the available carbapenems, i.e., stable to AmpC and extended-spectrum \u03b2-lactamases but labile to class B and functional group 2f enzymes. The comparator drugs were imipenem, oral cephalosporins, and amoxicillin. MICs were determined for \u03b2-lactamase expression variants, and hydrolysis was examined directly with representative enzymes. Sanfetrinem was a weak inducer of AmpC \u03b2-lactamases below the MIC and had slight lability, with a\n            <jats:italic>k<\/jats:italic>\n            <jats:sub>cat<\/jats:sub>\n            of 0.00033 s\n            <jats:sup>\u22121<\/jats:sup>\n            for the\n            <jats:italic>Enterobacter cloacae<\/jats:italic>\n            enzyme. Its MICs for AmpC-derepressed\n            <jats:italic>E. cloacae<\/jats:italic>\n            and\n            <jats:italic>Citrobacter freundii<\/jats:italic>\n            were 4 to 8 \u03bcg\/ml, compared with MICs of 0.12 to 2 \u03bcg\/ml for AmpC-inducible and -basal strains; MICs for AmpC-derepressed\n            <jats:italic>Serratia marcescens<\/jats:italic>\n            and\n            <jats:italic>Morganella morganii<\/jats:italic>\n            were not raised. Cefixime and cefpodoxime were more labile than sanfetrinem to the\n            <jats:italic>E. cloacae<\/jats:italic>\n            AmpC enzyme, and AmpC-derepressed mutants showed much greater resistance; imipenem was more stable and retained full activity against derepressed mutants. Like imipenem, sanfetrinem was stable to TEM-1 and TEM-10 enzymes and retained full activity against isolates and transconjugants with various extended-spectrum TEM and SHV enzymes, whereas these organisms were resistant to cefixime and cefpodoxime. Sanfetrinem, like imipenem and cefixime but unlike cefpodoxime, also retained activity against\n            <jats:italic>Proteus vulgaris<\/jats:italic>\n            and\n            <jats:italic>Klebsiella oxytoca<\/jats:italic>\n            strains that hyperproduced potent chromosomal class A \u03b2-lactamases. Functional group 2f enzymes, including Sme-1, NMC-A, and an unnamed enzyme from\n            <jats:italic>Acinetobacter<\/jats:italic>\n            spp., increased the sanfetrinem MICs by up to 64-fold. These enzymes also compromised the activities of imipenem and amoxicillin but not those of the cephalosporins. The hydrolysis of sanfetrinem was examined with a purified Sme-1 enzyme, and biphasic kinetics were found. Finally, zinc \u03b2-lactamases, including IMP-1 and the L1 enzyme of\n            <jats:italic>Stenotrophomonas maltophilia<\/jats:italic>\n            , conferred resistance to sanfetrinem and all other \u03b2-lactams tested, and hydrolysis was confirmed with the IMP-1 enzyme. We conclude that sanfetrinem has \u03b2-lactamase interactions similar to those of the available carbapenems except that it is a weaker inducer of AmpC types, with some tendency to select derepressed mutants, unlike imipenem and meropenem.\n          <\/jats:p>","DOI":"10.1128\/aac.42.5.1168","type":"journal-article","created":{"date-parts":[[2018,10,9]],"date-time":"2018-10-09T00:31:56Z","timestamp":1539045116000},"page":"1168-1175","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":17,"title":["Interactions of \u03b2-Lactamases with Sanfetrinem (GV 104326) Compared to Those with Imipenem and with Oral \u03b2-Lactams"],"prefix":"10.1128","volume":"42","author":[{"given":"Gioia S.","family":"Babini","sequence":"first","affiliation":[{"name":"<!--label omitted: 1-->Antibiotic Group, St Bartholomew\u2019s and the Royal London School of Medicine and Dentistry, London E1 2AD, United Kingdom"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Meifang","family":"Yuan","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Antibiotic Group, St Bartholomew\u2019s and the Royal London School of Medicine and Dentistry, London E1 2AD, United Kingdom"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David M.","family":"Livermore","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Antibiotic Group, St Bartholomew\u2019s and the Royal London School of Medicine and Dentistry, London E1 2AD, United Kingdom"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","unstructured":"Afzal-Shah M. 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