{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T16:48:36Z","timestamp":1792082916461,"version":"4.4.0"},"reference-count":31,"publisher":"American Society for Microbiology","issue":"7","license":[{"start":{"date-parts":[[2015,7,1]],"date-time":"2015-07-01T00:00:00Z","timestamp":1435708800000},"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":[[2015,7]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Aminoglycosides (AGs) are clinically relevant antibiotics used to treat infections caused by both Gram-negative and Gram-positive bacteria, as well as\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Mycobacteria<\/jats:named-content>\n            . As with all current antibacterial agents, resistance to AGs is an increasing problem. The most common mechanism of resistance to AGs is the presence of AG-modifying enzymes (AMEs) in bacterial cells, with AG acetyltransferases (AACs) being the most prevalent. Recently, it was discovered that Zn\n            <jats:sup>2+<\/jats:sup>\n            metal ions displayed an inhibitory effect on the resistance enzyme AAC(6\u2032)-Ib in\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Acinetobacter baumannii<\/jats:named-content>\n            and\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Escherichia coli<\/jats:named-content>\n            . In this study, we explore a wide array of metal salts (Mg\n            <jats:sup>2+<\/jats:sup>\n            , Cr\n            <jats:sup>3+<\/jats:sup>\n            , Cr\n            <jats:sup>6+<\/jats:sup>\n            , Mn\n            <jats:sup>2+<\/jats:sup>\n            , Co\n            <jats:sup>2+<\/jats:sup>\n            , Ni\n            <jats:sup>2+<\/jats:sup>\n            , Cu\n            <jats:sup>2+<\/jats:sup>\n            , Zn\n            <jats:sup>2+<\/jats:sup>\n            , Cd\n            <jats:sup>2+<\/jats:sup>\n            , and Au\n            <jats:sup>3+<\/jats:sup>\n            with different counter ions) and their inhibitory effect on a large repertoire of AACs [AAC(2\u2032)-Ic, AAC(3)-Ia, AAC(3)-Ib, AAC(3)-IV, AAC(6\u2032)-Ib\u2032, AAC(6\u2032)-Ie, AAC(6\u2032)-IId, and Eis]. In addition, we determine the MIC values for amikacin and tobramycin in combination with a zinc pyrithione complex in clinical isolates of various bacterial strains (two strains of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">A. baumannii<\/jats:named-content>\n            , three of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Enterobacter cloacae<\/jats:named-content>\n            , and four of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Klebsiella pneumoniae<\/jats:named-content>\n            ) and one representative of each species purchased from the American Type Culture Collection.\n          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