{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T01:47:20Z","timestamp":1791942440785,"version":"4.3.4"},"reference-count":114,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2014,7,16]],"date-time":"2014-07-16T00:00:00Z","timestamp":1405468800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01 AI133481"],"award-info":[{"award-number":["R01 AI133481"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2014,8]]},"abstract":"Summary<\/jats:title>\n \n Bacterial pathogens must overcome host sequestration of zinc (\n Zn<\/jats:styled-content>\n 2+<\/jats:sup>\n ), an essential micronutrient, during the infectious disease process. While the mechanisms to acquire chelated\n Zn<\/jats:styled-content>\n 2+<\/jats:sup>\n by bacteria are largely undefined, many pathogens rely upon the\n ZnuABC<\/jats:styled-content>\n family of\n ABC<\/jats:styled-content>\n transporters. Here we show that in\n \n Y<\/jats:italic>\n <\/jats:styled-content>\n ersinia pestis<\/jats:italic>\n ,\n \n irp2<\/jats:italic>\n <\/jats:styled-content>\n , a gene encoding the synthetase (\n HMWP<\/jats:styled-content>\n 2) for the siderophore yersiniabactin (\n Ybt<\/jats:styled-content>\n ) is required for growth under\n Zn<\/jats:styled-content>\n 2+<\/jats:sup>\n \u2010deficient conditions in a strain lacking\n ZnuABC<\/jats:styled-content>\n . Moreover, growth stimulation with exogenous, purified apo\u2010\n Ybt<\/jats:styled-content>\n provides evidence that\n Ybt<\/jats:styled-content>\n may serve as a zincophore for\n Zn<\/jats:styled-content>\n 2+<\/jats:sup>\n acquisition. Studies with the\n Zn<\/jats:styled-content>\n 2+<\/jats:sup>\n \u2010dependent transcriptional reporter\n \n znuA<\/jats:italic>\n <\/jats:styled-content>\n ::<\/jats:italic>\n \n lacZ<\/jats:italic>\n <\/jats:styled-content>\n indicate that the ability to synthesize\n Ybt<\/jats:styled-content>\n affects the levels of intracellular\n Zn<\/jats:styled-content>\n 2+<\/jats:sup>\n . However, the outer membrane receptor\n Psn<\/jats:styled-content>\n and\n TonB<\/jats:styled-content>\n as well as the inner membrane (\n IM<\/jats:styled-content>\n )\n ABC<\/jats:styled-content>\n transporter\n YbtPQ<\/jats:styled-content>\n , which are required for\n Fe<\/jats:styled-content>\n 3+<\/jats:sup>\n acquisition by\n Ybt<\/jats:styled-content>\n , are not needed for\n Ybt<\/jats:styled-content>\n \u2010dependent\n Zn<\/jats:styled-content>\n 2+<\/jats:sup>\n uptake. In contrast, the predicted\n IM<\/jats:styled-content>\n protein\n YbtX<\/jats:styled-content>\n , a member of the\n M<\/jats:styled-content>\n ajor\n F<\/jats:styled-content>\n acilitator\n S<\/jats:styled-content>\n uperfamily, was essential for\n Ybt<\/jats:styled-content>\n \u2010dependent\n Zn<\/jats:styled-content>\n 2+<\/jats:sup>\n uptake. Finally, we show that the\n ZnuABC<\/jats:styled-content>\n system and the\n Ybt<\/jats:styled-content>\n synthetase\n HMWP<\/jats:styled-content>\n 2, presumably by\n Ybt<\/jats:styled-content>\n synthesis, both contribute to the development of a lethal infection in a septicaemic plague mouse model.\n <\/jats:p>","DOI":"10.1111\/mmi.12693","type":"journal-article","created":{"date-parts":[[2014,6,30]],"date-time":"2014-06-30T21:56:54Z","timestamp":1404165414000},"page":"759-775","source":"Crossref","is-referenced-by-count":153,"title":["The\n \n Y<\/i>\n <\/scp>\n ersinia pestis<\/i>\n siderophore, yersiniabactin, and the\n ZnuABC<\/scp>\n system both contribute to zinc acquisition and the development of lethal septicaemic plague in mice"],"prefix":"10.1111","volume":"93","author":[{"given":"Alexander G.","family":"Bobrov","sequence":"first","affiliation":[{"name":"Department of Microbiology, Immunology, and Molecular Genetics University of Kentucky Lexington KY USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Olga","family":"Kirillina","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Immunology, and Molecular Genetics University of Kentucky Lexington KY USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jacqueline D.","family":"Fetherston","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Immunology, and Molecular Genetics University of Kentucky Lexington KY USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M. Clarke","family":"Miller","sequence":"additional","affiliation":[{"name":"James Graham Brown Cancer Center University of Louisville Louisville KY USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joseph A.","family":"Burlison","sequence":"additional","affiliation":[{"name":"James Graham Brown Cancer Center University of Louisville Louisville KY USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert D.","family":"Perry","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Immunology, and Molecular Genetics University of Kentucky Lexington KY 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