{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T18:04:37Z","timestamp":1791137077991,"version":"4.1.0"},"reference-count":47,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2022,4,27]],"date-time":"2022-04-27T00:00:00Z","timestamp":1651017600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2022,4,27]],"date-time":"2022-04-27T00:00:00Z","timestamp":1651017600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/501100004663","name":"Ministry of Science and Technology, Taiwan","doi-asserted-by":"publisher","award":["MOST 108-2320-B-010-032-MY3"],"award-info":[{"award-number":["MOST 108-2320-B-010-032-MY3"]}],"id":[{"id":"10.13039\/501100004663","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100005866","name":"Far Eastern Memorial Hospital","doi-asserted-by":"publisher","award":["111DN28"],"award-info":[{"award-number":["111DN28"]}],"id":[{"id":"10.13039\/501100005866","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["J Biomed Sci"],"published-print":{"date-parts":[[2022,12]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:sec><jats:title>Background<\/jats:title><jats:p><jats:italic>Stenotrophomonas maltophilia<\/jats:italic>, a member of \u03b3-proteobacteria, is a ubiquitous environmental bacterium that is recognized as an opportunistic nosocomial pathogen. FecABCD system contributes to ferric citrate acquisition in<jats:italic>Escherichia coli<\/jats:italic>. FeoABC system, consisting of an inner membrane transporter (FeoB) and two cytoplasmic proteins (FeoA and FeoC), is a well-known ferrous iron transporter system in \u03b3-proteobacteria. As revealed by the sequenced genome,<jats:italic>S. maltophilia<\/jats:italic>appears to be equipped with several iron acquisition systems; however, the understanding of these systems is limited. In this study, we aimed to elucidate the ferric citrate acquisition system of<jats:italic>S. maltophilia<\/jats:italic>.<\/jats:p><\/jats:sec><jats:sec><jats:title>Methods<\/jats:title><jats:p>Candidate genes searching and function validation are the strategy for elucidating the genes involved in ferric citrate acquisition. The candidate genes responsible for ferric citrate acquisition were firstly selected using FecABCD of<jats:italic>E. coli<\/jats:italic>as a reference, and then revealed by transcriptome analysis of<jats:italic>S. maltophilia<\/jats:italic>KJ with and without 2,2\u2032-dipyridyl (DIP) treatment. Function validation was carried out by deletion mutant construction and ferric citrate utilization assay. The bacterial adenylate cyclase two-hybrid system was used to verify intra-membrane protein\u2013protein interaction.<\/jats:p><\/jats:sec><jats:sec><jats:title>Results<\/jats:title><jats:p>Smlt2858 and Smlt2356, the homologues of FecA and FecC\/D of<jats:italic>E. coli<\/jats:italic>, were first considered; however, deletion mutant construction and functional validation ruled out their involvement in ferric citrate acquisition.<jats:italic>FciA<\/jats:italic>(Smlt1148), revealed by its upregulation in DIP-treated KJ cells, was the outer membrane receptor for ferric citrate uptake. The<jats:italic>fciA<\/jats:italic>gene is a member of the<jats:italic>fciTABC<\/jats:italic>operon, in which<jats:italic>fciT, fciA,<\/jats:italic>and<jats:italic>fciC<\/jats:italic>participated in ferric citrate acquisition. Uniquely, the Feo system of<jats:italic>S. maltophilia<\/jats:italic>is composed of a cytoplasmic protein FeoA, an inner membrane transporter FeoB, and a predicted inner membrane protein FeoI. The intra-membrane protein\u2013protein interaction between FeoB and FeoI may extend the substrate profile of FeoB to ferric citrate. FeoABI system functioned as an inner membrane transporter of ferric citrate.<\/jats:p><\/jats:sec><jats:sec><jats:title>Conclusions<\/jats:title><jats:p>The FciTABC and FeoABI systems contribute to ferric citrate acquisition in<jats:italic>S. maltophilia<\/jats:italic>.<\/jats:p><\/jats:sec>","DOI":"10.1186\/s12929-022-00809-y","type":"journal-article","created":{"date-parts":[[2022,4,27]],"date-time":"2022-04-27T15:07:19Z","timestamp":1651072039000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":15,"title":["The fciTABC and feoABI systems contribute to ferric citrate acquisition in Stenotrophomonas maltophilia"],"prefix":"10.1186","volume":"29","author":[{"given":"Chun-Hsing","family":"Liao","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hsu-Feng","family":"Lu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hsin-Hui","family":"Huang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yu","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Li-Hua","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yi-Tsung","family":"Lin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tsuey-Ching","family":"Yang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2022,4,27]]},"reference":[{"key":"809_CR1","doi-asserted-by":"publisher","first-page":"653","DOI":"10.1126\/science.277.5326.653","volume":"277","author":"H Beinert","year":"1997","unstructured":"Beinert H, Holm RH, M\u00fcnck E. Iron-sulfur clusters: nature\u2019s modular, multipurpose structures. Science. 1997;277:653\u20139.","journal-title":"Science"},{"key":"809_CR2","doi-asserted-by":"publisher","unstructured":"Sheldon JR, Laakso HA, Heinrichs DE. Iron\u00a0acquisition strategies of bacterial pathogens. Microbiol Spectr. 2016;4(2). doi:https:\/\/doi.org\/10.1128\/microbiolspec. VMBF-0010\u20132015.","DOI":"10.1128\/microbiolspec"},{"key":"809_CR3","doi-asserted-by":"publisher","first-page":"318","DOI":"10.1016\/S0005-2736(02)00578-3","volume":"1565","author":"AD Ferguson","year":"2002","unstructured":"Ferguson AD, Deisenhofer J. TonB-dependent receptors-structural perspectives. Biochim Biophys Acta. 2002;1565:318\u201332.","journal-title":"Biochim Biophys Acta"},{"key":"809_CR4","doi-asserted-by":"publisher","first-page":"431","DOI":"10.1111\/j.1432-1033.1981.tb06357.x","volume":"117","author":"S Hussein","year":"1981","unstructured":"Hussein S, Hantke K, Braun V. Citrate-dependent iron transport system in Escherichia coli K-12. Eur J Biochem. 1981;117:431\u20137.","journal-title":"Eur J Biochem"},{"key":"809_CR5","doi-asserted-by":"publisher","first-page":"3298","DOI":"10.1128\/jb.172.6.3298-3303.1990","volume":"172","author":"ML Guerinot","year":"1990","unstructured":"Guerinot ML, Meidl EJ, Plessner O. Citrate as a siderophore in Bradyrhizobium japonicum. J Bacteriol. 1990;172:3298\u2013303.","journal-title":"J Bacteriol"},{"key":"809_CR6","doi-asserted-by":"publisher","first-page":"2767","DOI":"10.1128\/JB.00069-10","volume":"193","author":"AM Jones","year":"2011","unstructured":"Jones AM, Wildermuth MC. The phytopathogen Pseudomonas syringae pv. tomato DC3000 has three high-affinity iron-scavenging systems functional under iron limitation conditions but dispensable for pathogenesis. J Bacteriol. 2011;193:2767\u201375.","journal-title":"J Bacteriol"},{"key":"809_CR7","doi-asserted-by":"publisher","first-page":"361","DOI":"10.3389\/fcimb.2017.00361","volume":"7","author":"M Balado","year":"2017","unstructured":"Balado M, Puentes B, Couceiro L, Fuentes-Monteverde JC, Rodriguez J, Osorio CR, et al. Secreted citrate serves as iron carrier for the marine pathogen photobacterium damselae subsp. damselae. Front Cell Infect Microbiol. 2017;7:361.","journal-title":"Front Cell Infect Microbiol"},{"key":"809_CR8","doi-asserted-by":"publisher","first-page":"2716","DOI":"10.1128\/jb.170.6.2716-2724.1988","volume":"170","author":"U Pressler","year":"1988","unstructured":"Pressler U, Staudenmaier H, Zimmermann L, Braun V. Genetics of the iron dicitrate transport system of Escherichia coli. J Bacteriol. 1988;170:2716\u201324.","journal-title":"J Bacteriol"},{"key":"809_CR9","doi-asserted-by":"publisher","first-page":"305","DOI":"10.1099\/mic.0.023531-0","volume":"155","author":"B Marshall","year":"2009","unstructured":"Marshall B, Stintzi A, Gilmour C, Meyer JM, Poole K. Citrate mediated iron uptake in Pseudomonas aeruginosa: involvement of the citrate inducible FecA receptor and the FeoB ferrous iron transporter. Microbiology. 2009;155:305\u201315.","journal-title":"Microbiology"},{"key":"809_CR10","doi-asserted-by":"publisher","first-page":"2626","DOI":"10.1128\/jb.171.5.2626-2633.1989","volume":"171","author":"H Staudenmaier","year":"1989","unstructured":"Staudenmaier H, Van Hove B, Yaraghi Z, Braun V. Nucleotide sequences of the fecBCDE genes and locations of the proteins suggest a periplasmic-binding-protein-dependent transport mechanism for iron(III) dicitrate in Escherichia coli. J Bacteriol. 1989;171:2626\u201333.","journal-title":"J Bacteriol"},{"key":"809_CR11","doi-asserted-by":"publisher","first-page":"1430","DOI":"10.1002\/j.1460-2075.1995.tb07129.x","volume":"17","author":"C Harle","year":"1995","unstructured":"Harle C, Kim I, Angerer A, Braun V. Signal transfer through three compartments: transcription initiation of the Escherichia coli ferric citrate transport system from the cell surface. EMBO J. 1995;17:1430\u20138.","journal-title":"EMBO J"},{"key":"809_CR12","doi-asserted-by":"publisher","first-page":"1146","DOI":"10.1046\/j.1365-2958.2000.01783.x","volume":"35","author":"A Janakiraman","year":"2000","unstructured":"Janakiraman A, Slauch JM. The putative iron transport system SitABCD encoded on SPI1 is required for full virulence of Salmonella typhimurium. Mol Microbiol. 2000;35:1146\u201355.","journal-title":"Mol Microbiol"},{"key":"809_CR13","doi-asserted-by":"publisher","first-page":"25317","DOI":"10.1074\/jbc.M111.222745","volume":"286","author":"D Koch","year":"2011","unstructured":"Koch D, Chan AC, Murphy ME, Lilie H, Grass G, Nies DH. Characterization of a dipartite iron uptake system from uropathogenic Escherichia coli strain F11. J Biol Chem. 2011;286:25317\u201330.","journal-title":"J Biol Chem"},{"key":"809_CR14","doi-asserted-by":"publisher","first-page":"6032","DOI":"10.1128\/IAI.70.11.6032-6042.2002","volume":"70","author":"E Boyer","year":"2002","unstructured":"Boyer E, Bergevin I, Malo D, Gros P, Cellier MF. Acquisition of Mn(II) in addition to Fe(II) is required for full virulence of Salmonella enterica serovar Typhimurium. Infect Immun. 2002;70:6032\u201342.","journal-title":"Infect Immun"},{"key":"809_CR15","doi-asserted-by":"publisher","first-page":"6212","DOI":"10.1128\/jb.175.19.6212-6219.1993","volume":"175","author":"M Kammler","year":"1993","unstructured":"Kammler M, Schon C, Hantke K. Characterization of the ferrous iron uptake system of Escherichia coli. J Bacteriol. 1993;175:6212\u20139.","journal-title":"J Bacteriol"},{"key":"809_CR16","doi-asserted-by":"publisher","first-page":"274","DOI":"10.1046\/j.1365-2958.2000.01987.x","volume":"37","author":"J Velayudhan","year":"2000","unstructured":"Velayudhan J, Hughes NJ, McColm AA, Bagshaw J, Clayton CL, Andrews SC, et al. Iron acquisition and virulence in Helicobacter pylori: a major role for FeoB, a high-affinity ferrous iron transporter. Mol Microbiol. 2000;37:274\u201386.","journal-title":"Mol Microbiol"},{"key":"809_CR17","doi-asserted-by":"publisher","first-page":"2779","DOI":"10.1128\/JB.183.9.2779-2784.2001","volume":"183","author":"H Katoh","year":"2001","unstructured":"Katoh H, Hagino N, Grossman AR, Ogawa T. Genes essential to iron transport in the cyanobacterium Synechocystis sp. strain PCC 6803. J Bacteriol. 2001;183:2779\u201384.","journal-title":"J Bacteriol"},{"key":"809_CR18","doi-asserted-by":"publisher","first-page":"5659","DOI":"10.1128\/IAI.70.10.5659-5669.2002","volume":"70","author":"M Robey","year":"2002","unstructured":"Robey M, Cianciotto NP. Legionella pneumophila feoAB promotes ferrous iron uptake and intracellular infection. Infect Immun. 2002;70:5659\u201369.","journal-title":"Infect Immun"},{"key":"809_CR19","doi-asserted-by":"publisher","first-page":"5433","DOI":"10.1128\/IAI.00052-06","volume":"74","author":"H Naikare","year":"2006","unstructured":"Naikare H, Palyada K, Panciera R, Marlow D, Stintzi A. Major role for FeoB in Campylobacter jejuni ferrous iron acquisition, gut colonization, and intracellular survival. Infect Immun. 2006;74:5433\u201344.","journal-title":"Infect Immun"},{"key":"809_CR20","doi-asserted-by":"publisher","first-page":"6515","DOI":"10.1128\/JB.00626-06","volume":"188","author":"EE Wyckoff","year":"2006","unstructured":"Wyckoff EE, Mey AR, Leimbach A, Fisher CF, Payne SM. Characterization of ferric and ferrous iron transport systems in Vibrio cholerae. J Bacteriol. 2006;188:6515\u201323.","journal-title":"J Bacteriol"},{"key":"809_CR21","doi-asserted-by":"publisher","first-page":"3249","DOI":"10.1128\/JB.187.9.3249-3254.2005","volume":"187","author":"H Louvel","year":"2005","unstructured":"Louvel H, Girons IS, Picardeau M. Isolation and characterization of FecA- and FeoB-mediated iron acquisition systems of the spirochete Leptospira biflexa by random insertional mutagenesis. J Bacteriol. 2005;187:3249\u201354.","journal-title":"J Bacteriol"},{"key":"809_CR22","doi-asserted-by":"publisher","first-page":"733","DOI":"10.1016\/j.bbrc.2012.06.027","volume":"423","author":"H Kim","year":"2012","unstructured":"Kim H, Lee H, Shin D. The FeoA protein is necessary for the FeoB transporter to import ferrous iron. Biochem Biophys Res Commun. 2012;423:733\u20138.","journal-title":"Biochem Biophys Res Commun"},{"key":"809_CR23","doi-asserted-by":"publisher","first-page":"1160","DOI":"10.1128\/JB.00930-15","volume":"198","author":"B Stevenson","year":"2016","unstructured":"Stevenson B, Wyckoff EE, Payne SM. Vibrio cholera FeoA, FeoB, and FeoC interact to form a complex. J Bacteriol. 2016;198:1160\u201370.","journal-title":"J Bacteriol"},{"key":"809_CR24","first-page":"59","volume":"3","author":"B Troxell","year":"2013","unstructured":"Troxell B, Hassan HM. Transcriptional regulation by ferric uptake regulator (Fur) in pathogenic bacteria. Front Cell Infect Microbiol. 2013;3:59.","journal-title":"Front Cell Infect Microbiol"},{"key":"809_CR25","doi-asserted-by":"publisher","first-page":"1177","DOI":"10.1046\/j.1365-2958.2002.03088.x","volume":"45","author":"P Visca","year":"2002","unstructured":"Visca P, Leoni L, Wilson MJ, Lamont IL. Iron transport and regulation, cell signalling and genomics: lessons from Escherichia coli and Pseudomonas. Mol Microbiol. 2002;45:1177\u201390.","journal-title":"Mol Microbiol"},{"key":"809_CR26","doi-asserted-by":"publisher","DOI":"10.1098\/rsob.180023","volume":"8","author":"K Jung","year":"2018","unstructured":"Jung K, Fabiani F, Hoyer E, Lassak J. Bacterial transmembrane signaling systems and their engineering for biosensing. Open Biol. 2018;8: 180023.","journal-title":"Open Biol"},{"key":"809_CR27","doi-asserted-by":"publisher","first-page":"673","DOI":"10.1016\/j.femsre.2004.10.001","volume":"29","author":"V Braun","year":"2005","unstructured":"Braun V, Mahren S. Transmembrane transcriptional control (surface signaling) of the Escherichia coli Fec type. FEMS Microbiol Rev. 2005;29:673\u201384.","journal-title":"FEMS Microbiol Rev"},{"key":"809_CR28","doi-asserted-by":"publisher","first-page":"103","DOI":"10.1007\/s10534-005-8253-y","volume":"19","author":"V Braun","year":"2006","unstructured":"Braun V, Mahren S, Sauter A. Gene regulation by transmembrane signaling. Biometals. 2006;19:103\u201313.","journal-title":"Biometals"},{"key":"809_CR29","doi-asserted-by":"publisher","first-page":"482","DOI":"10.1186\/1471-2164-15-482","volume":"15","author":"P Alavi","year":"2014","unstructured":"Alavi P, Starcher MR, Thallinger GG, Zachow C, M\u00fcller H, Berg G. Stenotrophomonas comparative genomics reveals genes and functions that differentiate beneficial and pathogenic bacteria. BMC Genomics. 2014;15:482.","journal-title":"BMC Genomics"},{"key":"809_CR30","doi-asserted-by":"publisher","DOI":"10.1128\/CMR.00030-19","volume":"34","author":"JS Brooke","year":"2021","unstructured":"Brooke JS. Advances in the microbiology of Stenotrophomonas maltophilia. Clin Microbiol Rev. 2021;34: e0003019.","journal-title":"Clin Microbiol Rev"},{"key":"809_CR31","doi-asserted-by":"publisher","first-page":"1590","DOI":"10.1099\/mic.0.000545","volume":"163","author":"MY Nas","year":"2017","unstructured":"Nas MY, Cianciotto NP. Stenotrophomonas maltophilia produces an EntC-dependent catecholate siderophore that is distinct from enterobactin. Microbiology. 2017;163:1590\u2013603.","journal-title":"Microbiology"},{"key":"809_CR32","unstructured":"Pan SY, Shih YL, Huang HH, Li LH, Lin YT,\u00a0Yang TC. The involvement of PacIRA system of Stenotrophomonas maltophilia in the uptake of Pseudomonas aeruginosa pyochelin and intraspecies competition for iron acquisition. J Microbiol Immunol Infect. 2021;23:S1684\u20131182(21)00052\u20139."},{"issue":"4","key":"809_CR33","first-page":"e02467","volume":"63","author":"YW Huang","year":"2019","unstructured":"Huang YW, Huang HH, Huang KH, Chen WC, Lin YT, Hsu CC, et al. AmpI functions as an iron Exporter to alleviate \u03b2-Lactam-mediated reactive oxygen species stress in Stenotrophomonas maltophilia. Antimicrob Agents Chemother. 2019;63(4):e02467-e2518.","journal-title":"Antimicrob Agents Chemother"},{"issue":"4","key":"809_CR34","doi-asserted-by":"publisher","first-page":"R74","DOI":"10.1186\/gb-2008-9-4-r74","volume":"9","author":"LC Crossman","year":"2008","unstructured":"Crossman LC, Gould VC, Dow JM, Vernikos GS, Okazaki A, Sebaihia M, Saunders D, Arrowsmith C, Carver T, Peters N, Adlem E, Kerhornou A, Lord A, Murphy L, Seeger K, Squares R, Rutter S, Quail MA, Rajandream MA, Harris D, Churcher C, Bentley SD, Parkhill J, Thomson NR, Avison MB. The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants. Genome Biol. 2008;9(4):R74.","journal-title":"Genome Biol"},{"key":"809_CR35","doi-asserted-by":"publisher","first-page":"2902","DOI":"10.1128\/AAC.01513-08","volume":"3","author":"TC Yang","year":"2009","unstructured":"Yang TC, Huang YW, Hu RM, Huang SC, Lin YT. AmpDI is involved in expression of the chromosomal L1 and L2 \u03b2-lactamases of Stenotrophomonas maltophilia. Antimicrob Agents Chemother. 2009;3:2902\u20137.","journal-title":"Antimicrob Agents Chemother"},{"key":"809_CR36","doi-asserted-by":"publisher","first-page":"5826","DOI":"10.1128\/AAC.00317-11","volume":"55","author":"CH Chen","year":"2011","unstructured":"Chen CH, Huang CC, Chung TC, Hu RM, Huang YW, Yang TC. Contribution of resistance-nodulation-division efflux pump operon smeU1-V-W-U2-X to multidrug resistance of Stenotrophomonas maltophilia. Antimicrob Agents Chemother. 2011;55:5826\u201333.","journal-title":"Antimicrob Agents Chemother"},{"key":"809_CR37","unstructured":"Miller JH. 1972. Experiments in molecular genetics, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY. p 352\u2013355."},{"issue":"45","key":"809_CR38","doi-asserted-by":"publisher","first-page":"2761","DOI":"10.1128\/JCM.01228-07","volume":"2007","author":"JM Janda","year":"2007","unstructured":"Janda JM, Abbott SL. 16S rRNA gene sequencing for bacterial identification in the diagnostic laboratory: pluses, perils, and pitfalls. J Clin Microbiol. 2007;2007(45):2761\u20134.","journal-title":"J Clin Microbiol"},{"key":"809_CR39","doi-asserted-by":"publisher","first-page":"3544","DOI":"10.1093\/jac\/dkaa358","volume":"75","author":"CH Liao","year":"2020","unstructured":"Liao CH, Chen WC, Li LH, Lin YT, Pan SY, Yang TC. AmpR of Stenotrophomonas maltophilia is involved in stenobactin synthesis and enhanced \u03b2-lactam resistance in an iron-depleted condition. J Antimicrob Chemother. 2020;75:3544\u201351.","journal-title":"J Antimicrob Chemother"},{"issue":"136","key":"809_CR40","doi-asserted-by":"publisher","first-page":"1859","DOI":"10.1099\/00221287-136-9-1859","volume":"1990","author":"RA Harding","year":"1990","unstructured":"Harding RA, Royt PW. Acquisition of iron from citrate by Pseudomonas aeruginosa. J Gen Microbiol. 1990;1990(136):1859\u201367.","journal-title":"J Gen Microbiol"},{"key":"809_CR41","doi-asserted-by":"crossref","unstructured":"Wu CJ, Chen Y, Li LH, Wu CM, Lin YT, Ma CH, Yang TC. Roles of SmeYZ, SbiAB, and SmeDEF efflux systems in iron homeostasis of Stenotrophomonas maltophilia. Microbiol Spec. 2022. In revision.","DOI":"10.1128\/spectrum.02448-21"},{"key":"809_CR42","doi-asserted-by":"publisher","first-page":"926","DOI":"10.3389\/fmicb.2015.00926","volume":"6","author":"CA Garc\u00eda","year":"2015","unstructured":"Garc\u00eda CA, Alcaraz ES, Franco MA, Passerini de Rossi BN. Iron is a signal for\u00a0Stenotrophomonas\u00a0maltophilia\u00a0biofilm formation, oxidative stress response, OMPs expression, and virulence. Front Microbiol. 2015;6:926.","journal-title":"Front Microbiol"},{"key":"809_CR43","doi-asserted-by":"publisher","first-page":"3364","DOI":"10.1128\/JB.00343-13","volume":"195","author":"H Kim","year":"2013","unstructured":"Kim H, Lee H, Shin D. The FeoC protein leads to high cellular levels of the Fe(II) transporter FeoB by preventing FtsH protease regulation of FeoB in Salmonella enterica. J Bacteriol. 2013;195:3364\u201370.","journal-title":"J Bacteriol"},{"key":"809_CR44","doi-asserted-by":"publisher","first-page":"4826","DOI":"10.1128\/JB.00738-13","volume":"195","author":"EA Weaver","year":"2013","unstructured":"Weaver EA, Wyckoff EE, Mey AR, Morrison R, Payne SM. FeoA and FeoC are essential components of the Vibrio cholerae ferrous iron uptake system, and FeoC interacts with FeoB. J Bacteriol. 2013;195:4826\u201335.","journal-title":"J Bacteriol"},{"key":"809_CR45","doi-asserted-by":"publisher","first-page":"273","DOI":"10.1093\/femsre\/fuv049","volume":"40","author":"CKY Lau","year":"2015","unstructured":"Lau CKY, Krewulak KD, Vogel HJ. Bacterial ferrous iron transport: the Feo system. FEMS Microbiol Rev. 2015;40:273\u201398.","journal-title":"FEMS Microbiol Rev"},{"key":"809_CR46","doi-asserted-by":"publisher","first-page":"5752","DOI":"10.1073\/pnas.95.10.5752","volume":"95","author":"G Karimova","year":"1998","unstructured":"Karimova G, Pidoux J, Ullmann A, Ladant D. A bacterial two-hybrid system based on a reconstituted signal transduction pathway. Proc Natl Acad Sci USA. 1998;95:5752\u20136.","journal-title":"Proc Natl Acad Sci USA"},{"key":"809_CR47","doi-asserted-by":"publisher","first-page":"92","DOI":"10.1128\/JB.01826-14","volume":"197","author":"H Kim","year":"2015","unstructured":"Kim H, Lee H, Shin D. Lon-mediated proteolysis of the FeoC protein prevents Salmonella enterica from accumulating the Fe(II) transporter FeoB under high-oxygen conditions. J Bacteriol. 2015;197:92\u20138.","journal-title":"J Bacteriol"}],"container-title":["Journal of Biomedical Science"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1186\/s12929-022-00809-y.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1186\/s12929-022-00809-y\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1186\/s12929-022-00809-y.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,2,3]],"date-time":"2023-02-03T19:14:16Z","timestamp":1675451656000},"score":1,"resource":{"primary":{"URL":"https:\/\/jbiomedsci.biomedcentral.com\/articles\/10.1186\/s12929-022-00809-y"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,4,27]]},"references-count":47,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2022,12]]}},"alternative-id":["809"],"URL":"https:\/\/doi.org\/10.1186\/s12929-022-00809-y","relation":{},"ISSN":["1423-0127"],"issn-type":[{"value":"1423-0127","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,4,27]]},"assertion":[{"value":"10 February 2022","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"19 April 2022","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"27 April 2022","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"Not applicable.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics approval and consent to participate"}},{"value":"Not applicable.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent for publication"}},{"value":"The authors declare that they have no competing interests.","order":4,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"26"}}