{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,20]],"date-time":"2026-06-20T00:29:43Z","timestamp":1781915383850,"version":"3.54.5"},"reference-count":46,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2012,11,1]],"date-time":"2012-11-01T00:00:00Z","timestamp":1351728000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2012,12]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>Iron and copper are transition metals that can be toxic to cells due to their abilities to react with peroxide to generate hydroxyl radical. Ferritins and metallothioneins are known to sequester intracellular iron and copper respectively. The <jats:styled-content style=\"fixed-case\">L<\/jats:styled-content>yme disease pathogen <jats:italic><jats:styled-content style=\"fixed-case\">B<\/jats:styled-content>orrelia burgdorferi<\/jats:italic> does not require iron, but its genome encodes a ferritin\u2010like <jats:styled-content style=\"fixed-case\">D<\/jats:styled-content>ps (<jats:styled-content style=\"fixed-case\"><jats:styled-content>D<\/jats:styled-content>NA<\/jats:styled-content>\u2010binding <jats:styled-content>p<\/jats:styled-content>rotein from <jats:styled-content>s<\/jats:styled-content>tarved bacteria) molecule, which has been shown to be important for the spirochaete's persistence in the tick and subsequent transmission to a new host. Here, we show that the <jats:styled-content>c<\/jats:styled-content>arboxyl\u2010terminal <jats:styled-content>c<\/jats:styled-content>ysteine\u2010<jats:styled-content>r<\/jats:styled-content>ich (<jats:styled-content style=\"fixed-case\">CCR<\/jats:styled-content>) domain of this protein functions as a copper\u2010binding metallothionein. This novel fusion between <jats:styled-content style=\"fixed-case\">D<\/jats:styled-content>ps and metallothionein is unique to and conserved in all <jats:italic><jats:styled-content style=\"fixed-case\">B<\/jats:styled-content>orrelia<\/jats:italic> species. We term this molecule <jats:styled-content style=\"fixed-case\">BicA<\/jats:styled-content> for <jats:italic><jats:styled-content><jats:styled-content style=\"fixed-case\">B<\/jats:styled-content><\/jats:styled-content>orrelia<\/jats:italic> <jats:styled-content>i<\/jats:styled-content>ron\u2010 and <jats:styled-content>c<\/jats:styled-content>opper\u2010binding protein <jats:styled-content><jats:styled-content style=\"fixed-case\">A<\/jats:styled-content><\/jats:styled-content>. An isogenic mutant lacking <jats:styled-content style=\"fixed-case\">BicA<\/jats:styled-content> had significantly reduced levels of iron and copper and was more sensitive to iron and copper toxicity than its parental strain. Supplementation of the medium with iron or copper rendered the spirochaete more susceptible to peroxide killing. These data suggest that an important function of <jats:styled-content style=\"fixed-case\">BicA<\/jats:styled-content> is to detoxify excess iron and copper the spirochaete may encounter during its natural life cycle through a tick vector and a vertebrate host.<\/jats:p>","DOI":"10.1111\/mmi.12068","type":"journal-article","created":{"date-parts":[[2012,10,15]],"date-time":"2012-10-15T06:36:52Z","timestamp":1350283012000},"page":"1441-1451","source":"Crossref","is-referenced-by-count":34,"title":["A novel iron\u2010 and copper\u2010binding protein in the <scp>L<\/scp>yme disease spirochaete"],"prefix":"10.1111","volume":"86","author":[{"given":"Peng","family":"Wang","sequence":"first","affiliation":[{"name":"Department of Veterinary Biosciences The Ohio State University  1900 Coffey Road Columbus OH 43210 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anthony","family":"Lutton","sequence":"additional","affiliation":[{"name":"Trace Element Research Laboratory The Ohio State University  125 South Oval Mall Columbus OH 43210 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John","family":"Olesik","sequence":"additional","affiliation":[{"name":"Trace Element Research Laboratory The Ohio State University  125 South Oval Mall Columbus OH 43210 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hojatollah","family":"Vali","sequence":"additional","affiliation":[{"name":"Department of Anatomy and Cell Biology McGill University  3640 University Street Montreal Quebec Canada H3A\u20090C7"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xin","family":"Li","sequence":"additional","affiliation":[{"name":"Department of Veterinary Biosciences The Ohio State University  1900 Coffey Road Columbus OH 43210 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