{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T05:24:19Z","timestamp":1790832259148,"version":"4.1.0"},"reference-count":61,"publisher":"American Society for Microbiology","issue":"5","license":[{"start":{"date-parts":[[2024,5,23]],"date-time":"2024-05-23T00:00:00Z","timestamp":1716422400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/doi.org\/10.1128\/ASMCopyrightv2"},{"start":{"date-parts":[[2024,5,23]],"date-time":"2024-05-23T00:00:00Z","timestamp":1716422400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"name":"NIH","award":["R21 AI123558-01 and 1R21AI141826-01A1"],"award-info":[{"award-number":["R21 AI123558-01 and 1R21AI141826-01A1"]}]},{"name":"The Department of Veterans Affairs VA Merit Review","award":["I01 BX004677-01"],"award-info":[{"award-number":["I01 BX004677-01"]}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2024,5,23]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:sec>\n                    <jats:title\/>\n                    <jats:p>\n                      Microbes synthesize and secrete siderophores, that bind and solubilize precipitated or otherwise unavailable iron in their microenvironments. Gram (\u2212) bacterial TonB-dependent outer membrane receptors capture the resulting ferric siderophores to begin the uptake process. From their similarity to\n                      <jats:italic>fepA,<\/jats:italic>\n                      the structural gene for the\n                      <jats:italic>Escherichia coli<\/jats:italic>\n                      ferric enterobactin (FeEnt) receptor, we identified four homologous genes in the human and animal ESKAPE pathogen\n                      <jats:italic>Klebsiella pneumoniae<\/jats:italic>\n                      (strain Kp52.145). One locus encodes IroN (locus\n                      <jats:italic>0027<\/jats:italic>\n                      on plasmid pII), and three other loci encode other FepA orthologs\/paralogs (chromosomal loci\n                      <jats:italic>1658, 2380,<\/jats:italic>\n                      and\n                      <jats:italic>4984<\/jats:italic>\n                      ). Based on the crystal structure of\n                      <jats:italic>E. coli<\/jats:italic>\n                      FepA (1FEP), we modeled the tertiary structures of the\n                      <jats:italic>K. pneumoniae<\/jats:italic>\n                      FepA homologs and genetically engineered individual Cys substitutions in their predicted surface loops. We subjected bacteria expressing the Cys mutant proteins to modification with extrinsic fluorescein maleimide (FM) and used the resulting fluorescently labeled cells to spectroscopically monitor the binding and transport of catecholate ferric siderophores by the four different receptors. The FM-modified FepA homologs were nanosensors that defined the ferric catecholate uptake pathways in pathogenic strains of\n                      <jats:italic>K. pneumoniae<\/jats:italic>\n                      . In Kp52.145, loci\n                      <jats:italic>1658<\/jats:italic>\n                      and\n                      <jats:italic>4984<\/jats:italic>\n                      encoded receptors that primarily recognized and transported FeEnt; locus\n                      <jats:italic>0027<\/jats:italic>\n                      produced a receptor that principally bound and transported FeEnt and glucosylated FeEnt (FeGEnt); locus 2380 encoded a protein that bound ferric catecholate compounds but did not detectably transport them. The sensors also characterized the uptake of iron complexes, including FeGEnt, by the hypervirulent, hypermucoviscous\n                      <jats:italic>K. pneumoniae<\/jats:italic>\n                      strain hvKp1.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>IMPORTANCE<\/jats:title>\n                    <jats:p>\n                      Both commensal and pathogenic bacteria produce small organic chelators, called siderophores, that avidly bind iron and increase its bioavailability.\n                      <jats:italic>Klebsiella pneumoniae<\/jats:italic>\n                      variably produces four siderophores that antagonize host iron sequestration: enterobactin, glucosylated enterobactin (also termed salmochelin), aerobactin, and yersiniabactin, which promote colonization of different host tissues. Abundant evidence links bacterial iron acquisition to virulence and infectious diseases. The data we report explain the recognition and transport of ferric catecholates and other siderophores, which are crucial to iron acquisition by\n                      <jats:italic>K. pneumoniae<\/jats:italic>\n                      .\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1128\/jb.00024-24","type":"journal-article","created":{"date-parts":[[2024,4,9]],"date-time":"2024-04-09T09:04:30Z","timestamp":1712653470000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":46,"title":["Siderophore-mediated iron acquisition by\n                    <i>Klebsiella pneumoniae<\/i>"],"prefix":"10.1128","volume":"206","author":[{"given":"Ashish","family":"Kumar","sequence":"first","affiliation":[{"name":"Department of Biochemistry &amp; Molecular Biophysics, Kansas State University, Manhattan, Kansas, USA"},{"name":"Department of Rare Blood and Musculoskeletal Disorders, Sanofi, Cambridge, Massachusetts, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Somnath","family":"Chakravorty","sequence":"additional","affiliation":[{"name":"Department of Biochemistry &amp; Molecular Biophysics, Kansas State University, Manhattan, Kansas, USA"},{"name":"Jacobs School of Medicine, University at Buffalo, Buffalo, New York, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Taihao","family":"Yang","sequence":"additional","affiliation":[{"name":"Department of Biochemistry &amp; Molecular Biophysics, Kansas State University, Manhattan, Kansas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4566-7442","authenticated-orcid":false,"given":"Thomas A.","family":"Russo","sequence":"additional","affiliation":[{"name":"Jacobs School of Medicine, University at Buffalo, Buffalo, New York, USA"},{"name":"Veterans Administration, Western New York Healthcare System, Buffalo, New York, 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