{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,28]],"date-time":"2026-10-28T02:03:34Z","timestamp":1793153014764,"version":"4.5.0"},"reference-count":34,"publisher":"American Society for Microbiology","issue":"9","license":[{"start":{"date-parts":[[2017,9,1]],"date-time":"2017-09-01T00:00:00Z","timestamp":1504224000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/100000057","name":"HHS | NIH | National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["GM79465"],"award-info":[{"award-number":["GM79465"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000062","name":"HHS | NIH | National Institute of Diabetes and Digestive and Kidney Diseases","doi-asserted-by":"publisher","award":["DK093386"],"award-info":[{"award-number":["DK093386"]}],"id":[{"id":"10.13039\/100000062","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2017,9]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Copper is an essential yet potentially toxic trace element that is required by all aerobic organisms. A key regulator of copper homeostasis in mammalian cells is the copper-transporting P-type ATPase ATP7A, which mediates copper transport from the cytoplasm into the secretory pathway, as well as copper export across the plasma membrane. Previous studies have shown that ATP7A-dependent copper transport is required for killing phagocytosed\n            <jats:named-content content-type=\"genus-species\">Escherichia coli<\/jats:named-content>\n            in a cultured macrophage cell line. In this investigation, we expanded on these studies by generating\n            <jats:italic>Atp7a<\/jats:italic>\n            <jats:sup>\n              <jats:italic>LysMcre<\/jats:italic>\n            <\/jats:sup>\n            mice, in which the\n            <jats:italic>Atp7a<\/jats:italic>\n            gene was specifically deleted in cells of the myeloid lineage, including macrophages. Primary macrophages isolated from\n            <jats:italic>Atp7a<\/jats:italic>\n            <jats:sup>\n              <jats:italic>LysMcre<\/jats:italic>\n            <\/jats:sup>\n            mice exhibit decreased copper transport into phagosomal compartments and a reduced ability to kill\n            <jats:named-content content-type=\"genus-species\">Salmonella enterica<\/jats:named-content>\n            serovar Typhimurium compared to that of macrophages isolated from wild-type mice. The\n            <jats:italic>Atp7a<\/jats:italic>\n            <jats:sup>\n              <jats:italic>LysMcre<\/jats:italic>\n            <\/jats:sup>\n            mice were also more susceptible to systemic infection by\n            <jats:italic>S<\/jats:italic>\n            . Typhimurium than wild-type mice. Deletion of the\n            <jats:italic>S<\/jats:italic>\n            . Typhimurium copper exporters, CopA and GolT, was found to decrease infection in wild-type mice but not in the\n            <jats:italic>Atp7a<\/jats:italic>\n            <jats:sup>\n              <jats:italic>LysMcre<\/jats:italic>\n            <\/jats:sup>\n            mice. These studies suggest that ATP7A-dependent copper transport into the phagosome mediates host defense against\n            <jats:italic>S<\/jats:italic>\n            . Typhimurium, which is counteracted by copper export from the bacteria via CopA and GolT. These findings reveal unique and opposing functions for copper transporters of the host and pathogen during infection.\n          <\/jats:p>","DOI":"10.1128\/iai.00351-17","type":"journal-article","created":{"date-parts":[[2017,6,27]],"date-time":"2017-06-27T00:20:22Z","timestamp":1498522822000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":67,"title":["Host and Pathogen Copper-Transporting P-Type ATPases Function Antagonistically during Salmonella Infection"],"prefix":"10.1128","volume":"85","author":[{"given":"Erik","family":"Ladomersky","sequence":"first","affiliation":[{"name":"Department of Biochemistry, University of Missouri, Columbia, Missouri, USA"},{"name":"Christopher S. 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