{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T01:13:12Z","timestamp":1790817192322,"version":"4.1.0"},"reference-count":37,"publisher":"American Society for Microbiology","issue":"3","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J. Bacteriol."],"published-print":{"date-parts":[[2015,2,1]]},"abstract":"<jats:p>The use of hemin iron by<jats:named-content content-type=\"genus-species\">Corynebacterium diphtheriae<\/jats:named-content>requires the DtxR- and iron-regulated ABC hemin transporter HmuTUV and the secreted Hb-binding protein HtaA. We recently described two surface anchored proteins, ChtA and ChtC, which also bind hemin and Hb. ChtA and ChtC share structural similarities to HtaA; however, a function for ChtA and ChtC was not determined. In this study, we identified additional host iron sources that are utilized by<jats:named-content content-type=\"genus-species\">C. diphtheriae<\/jats:named-content>. We show that several<jats:named-content content-type=\"genus-species\">C. diphtheriae<\/jats:named-content>strains use the hemoglobin-haptoglobin (Hb-Hp) complex as an iron source. We report that an<jats:italic>htaA<\/jats:italic>deletion mutant of<jats:named-content content-type=\"genus-species\">C. diphtheriae<\/jats:named-content>strain 1737 is unable to use the Hb-Hp complex as an iron source, and we further demonstrate that a<jats:italic>chtA-chtC<\/jats:italic>double mutant is also unable to use Hb-Hp iron. Single-deletion mutants of<jats:italic>chtA<\/jats:italic>or<jats:italic>chtC<\/jats:italic>use Hb-Hp iron in a manner similar to that of the wild type. These findings suggest that both HtaA and either ChtA or ChtC are essential for the use of Hb-Hp iron. Enzyme-linked immunosorbent assay (ELISA) studies show that HtaA binds the Hb-Hp complex, and the substitution of a conserved tyrosine (Y361) for alanine in HtaA results in significantly reduced binding.<jats:named-content content-type=\"genus-species\">C. diphtheriae<\/jats:named-content>was also able to use human serum albumin (HSA) and myoglobin (Mb) but not hemopexin as iron sources. These studies identify a biological function for the ChtA and ChtC proteins and demonstrate that the use of the Hb-Hp complex as an iron source by<jats:named-content content-type=\"genus-species\">C. diphtheriae<\/jats:named-content>requires multiple iron-regulated surface components.<\/jats:p>","DOI":"10.1128\/jb.02413-14","type":"journal-article","created":{"date-parts":[[2014,11,18]],"date-time":"2014-11-18T04:46:14Z","timestamp":1416285974000},"page":"553-562","source":"Crossref","is-referenced-by-count":42,"title":["Utilization of Host Iron Sources by Corynebacterium diphtheriae: Multiple Hemoglobin-Binding Proteins Are Essential for the Use of Iron from the Hemoglobin-Haptoglobin Complex"],"prefix":"10.1128","volume":"197","author":[{"given":"Courtni E.","family":"Allen","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael 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