Biosynthesis and IroC‐dependent export of the siderophore salmochelin are essential for virulence of Salmonella enterica serovar Typhimurium

Crouch, Marie‐Laure V.; Castor, Margaret; Karlinsey, Joyce E.; Kalhorn, Thomas; Fang, Ferric C.

doi:10.1111/j.1365-2958.2007.06089.x

Cited by 189Bacterial Genetics and BiotechnologySalmonella and Campylobacter epidemiologyEscherichia coli research studies

Biosynthesis and IroC‐dependent export of the siderophore salmochelin are essential for virulence of Salmonella enterica serovar Typhimurium

Crouch, Marie‐Laure V., Castor, Margaret, Karlinsey, Joyce E., Kalhorn, Thomas, Fang, Ferric C.·2008·Molecular Microbiology

DOI 10.1111/j.1365-2958.2007.06089.x

Open this paper in CoChat — free account

Abstract

In response to iron deprivation, Salmonella enterica serovar Typhimurium secretes two catecholate-type siderophores, enterobactin and its glucosylated derivative salmochelin. Although the systems responsible for enterobactin synthesis and acquisition are well characterized, the mechanisms of salmochelin secretion and acquisition, as well as its role in Salmonella virulence, are incompletely understood. Herein we show by liquid chromatography-mass spectrometry analysis of culture supernatants from wild type and isogenic mutant bacterial strains that the Major Facilitator Superfamily pump EntS is the major exporter of enterobactin and the ABC transporter IroC exports both salmochelin and enterobactin. Growth promotion experiments demonstrate that IroC is not required for utilization of Fe-enterobactin or Fe-salmochelin, as had been previously suggested, but the ABC transporter protein FepD is required for utilization of both siderophores. Salmonella mutants deficient in salmochelin synthesis or secretion exhibit reduced virulence during systemic infection of mice.

Integrity signals

Registry

Crossref · 10.1111/j.1365-2958.2007.06089.x

Cites

46 of 46 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Activation and expression of microbial iron acquisition systems is linked to their pathogenicity and proliferation.
“The activation and expression of such microbial iron acquisition systems is linked to their pathogenicity and proliferation (Rabsch et al., 1999; Schrettl et al., 2004; Crouch et al., 2008; Andrews-Polymenis et al., 2010; Cassat and Skaar, 2013).”
From Iron at the interface of immunity and infection (2014) · cites this paper as Crouch et al., 2008
The triple sit feo entC S.Tm mutant lacks the three main iron acquisition pathways.
“we infected macrophages with a triple sit feo entC mutant strain of S.Tm defective for the three main iron acquisition pathways (Crouch et al, 2008).”
From Iron Regulatory Proteins Mediate Host Resistance to Salmonella Infection (2015) · cites this paper as Crouch et al, 2008
Intramacrophage numbers of an iron-uptake-deficient Salmonella mutant were still significantly lower upon hmox silencing than in control macrophages, although the difference was less prominent than with wild-type Salmonella.
“Although, the differences in bacterial counts between ctrl.sh and hmox.sh macrophages were less prominent than during infection with wt Salmonella, intramacrophage numbers of mutant Salmonella were still significantly lower upon hmox silencing than in wt macrophages.”
From Heme oxygenase 1 controls early innate immune response of macrophages toSalmonellaTyphimurium infection: Heme oxygenase 1 expression affects Salmonellainfection (2016) · cites this paper as Crouch et al., 2008
The Salmonella triple mutant ΔentCΔsitΔfeo lacks the ability to synthesize enterobactin and to take up iron via SitABCD and Feo.
“The mutant strain, deficient in enterobactin synthesis, SitABCD- and Feo-mediated iron uptake (ΔentCΔsitΔfeo) was constructed and grown as previously described (Crouch et al., 2008).”
From Heme oxygenase 1 controls early innate immune response of macrophages toSalmonellaTyphimurium infection: Heme oxygenase 1 expression affects Salmonellainfection (2016) · cites this paper as Crouch et al., 2008

One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products.
Datsenko, K., & Wanner, B. (2000) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.120163297 · Cited by 15,902 · see citing works
Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
Guzman, L., Belin, D., Carson, M. J., & Beckwith, J. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.14.4121-4130.1995 · Cited by 4,942 · see citing works
Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant
Cherepanov, P., & Wackernagel, W. (1995) · Gene · doi:10.1016/0378-1119(95)00193-a · Cited by 1,952 · see citing works
Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron
Flo, T. H., Smith, K. D., Sato, S., Rodriguez, D. J., Holmes, M. A., Strong, R. K., Akira, S., & Aderem, A. (2004) · Nature · doi:10.1038/nature03104 · Cited by 1,877 · see citing works
Balancing Acts
Hentze, M. W., Muckenthaler, M. U., & Andrews, N. C. (2004) · Cell · doi:10.1016/s0092-8674(04)00343-5 · Cited by 1,736 · see citing works
Natural resistance to infection with intracellular parasites: isolation of a candidate for Bcg
Vidal, S. M., Malo, D., Vogan, K., Skamene, E., & Gros, P. (1993) · Cell · doi:10.1016/0092-8674(93)90135-d · Cited by 1,104 · see citing works
P-glycoprotein: from genomics to mechanism
Ambudkar, S. V., Kimchi‐Sarfaty, C., Sauna, Z. E., & Gottesman, M. M. (2003) · Oncogene · doi:10.1038/sj.onc.1206948 · Cited by 1,076 · see citing works
Iron and microbial infection
Schaible, U. E., & Kaufmann, S. H. E. (2004) · Nature Reviews Microbiology · doi:10.1038/nrmicro1046 · Cited by 945 · see citing works
Characterization of the ferrous iron uptake system of Escherichia coli
Kammler, M., Schön, C., & Hantke, K. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.19.6212-6219.1993 · Cited by 460 · see citing works
GeneChip ® expression analysis of the iron starvation response in Pseudomonas aeruginosa : identification of novel pyoverdine biosynthesis genes
Ochsner, U. A., Wilderman, P. J., Vasil, A. I., & Vasil, M. L. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03084.x · Cited by 406 · see citing works
Iron Transport in Bacteria
(2004) · ASM Press eBooks · doi:10.1128/9781555816544 · Cited by 368 · see citing works
Salmochelins, siderophores of Salmonella enterica and uropathogenic Escherichia coli strains, are recognized by the outer membrane receptor IroN
Hantke, K., Nicholson, G., Rabsch, W., & Winkelmann, G. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0737682100 · Cited by 359 · see citing works
Iron Storage in Bacteria
Andrews, S. C. (1998) · Advances in Microbial Physiology · doi:10.1016/s0065-2911(08)60134-4 · Cited by 353 · see citing works
The pathogen-associated iroA gene cluster mediates bacterial evasion of lipocalin 2
Fischbach, M. A., Lin, H., Zhou, L., Yu, Y., Abergel, R. J., Liu, D. R., Raymond, K. N., Wanner, B. L., Strong, R. K., Walsh, C. T., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604636103 · Cited by 319 · see citing works
Iron, manganese, and cobalt transport by Nramp1 (Slc11a1) and Nramp2 (Slc11a2) expressed at the plasma membrane
Forbes, J. R., & Gros, P. (2003) · Blood · doi:10.1182/blood-2003-02-0425 · Cited by 288 · see citing works
The structure of salmochelins: C-glucosylated enterobactins of Salmonella enterica §
Bister, B., Bischoff, D., NICHOLSON, G. J., Valdebenito, M., Schneider, K., Winkelmann, G., Hantke, K., & Süßmuth, R. D. (2004) · BioMetals · doi:10.1023/b:biom.0000029432.69418.6a · Cited by 188 · see citing works
Salmonella typhimuriumEncodes a Putative Iron Transport System within the Centisome 63 Pathogenicity Island
Zhou, D., Hardt, W.-D., & Galán, J. E. (1999) · Infection and Immunity · doi:10.1128/iai.67.4.1974-1981.1999 · Cited by 182 · see citing works
Export of the siderophore enterobactin in Escherichia coli: involvement of a 43 kDa membrane exporter
Furrer, J. L., Sanders, D. N., Hook-Barnard, I. G., & McIntosh, M. A. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02885.x · Cited by 180 · see citing works
TolC Is Involved in Enterobactin Efflux across the Outer Membrane of Escherichia coli
Bleuel, C., Große, C., Taudte, N., Scherer, J., Wesenberg, D., Krauss, G.-J., Nies, D. H., & Grass, G. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.19.6701-6707.2005 · Cited by 180 · see citing works
Contribution of TonB- and Feo-mediated iron uptake to growth of Salmonella typhimurium in the mouse
Tsolis, R. M., Bäumler, A. J., Heffron, F., & Stojiljkovic, I. (1996) · Infection and Immunity · doi:10.1128/iai.64.11.4549-4556.1996 · Cited by 174 · see citing works
In vitro characterization of IroB, a pathogen-associated C -glycosyltransferase
Fischbach, M. A., Lin, H., Liu, D. R., & Walsh, C. T. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408463102 · Cited by 169 · see citing works
IroN, a Novel Outer Membrane Siderophore Receptor Characteristic of Salmonella enterica
Bäumler, A. J., Norris, T. L., Lasco, T., Voigt, W., Reissbrodt, R., Rabsch, W., & Heffron, F. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.6.1446-1453.1998 · Cited by 147 · see citing works
Essential PchG-Dependent Reduction in Pyochelin Biosynthesis of Pseudomonas aeruginosa
Reimmann, C., Patel, H. M., Serino, L., Barone, M., Walsh, C. T., & Haas, D. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.3.813-820.2001 · Cited by 136 · see citing works
Mechanisms of Cellular Iron Acquisition
Kaplan, J. (2002) · Cell · doi:10.1016/s0092-8674(02)01164-9 · Cited by 128 · see citing works
Enterochelin (enterobactin): virulence factor for Salmonella typhimurium
Yancey, R. J., Breeding, S. A., & Lankford, C. E. (1979) · Infection and Immunity · doi:10.1128/iai.24.1.174-180.1979 · Cited by 127 · see citing works
The Salmonella enterica Serovar Typhimurium Divalent Cation Transport Systems MntH and SitABCD Are Essential for Virulence in an Nramp1 G169 Murine Typhoid Model
Zaharik, M. L., Cullen, V. L., Fung, A. M., Libby, S. J., Choy, S. L. K., Coburn, B. A., Kehres, D. G., Maguire, M. E., Fang, F. C., & Finlay, B. B. (2004) · Infection and Immunity · doi:10.1128/iai.72.9.5522-5525.2004 · Cited by 119 · see citing works
Self-citation
Functions of the siderophore esterases IroD and IroE in iron-salmochelin utilization
Zhu, M., Valdebenito, M., Winkelmann, G., & Hantke, K. (2005) · Microbiology · doi:10.1099/mic.0.27888-0 · Cited by 111 · see citing works
Ferrioxamine-Mediated Iron(III) Utilization by Salmonella enterica
Kingsley, R. A., Reissbrodt, R., Rabsch, W., Ketley, J. M., Tsolis, R. M., Everest, P. H., Gordon Dougan, B., Bäumler, A. J., Roberts, M., & WILLIAMS, P. H. (1999) · Applied and Environmental Microbiology · doi:10.1128/aem.65.4.1610-1618.1999 · Cited by 105 · see citing works
Iron transport by Nramp2/DMT1: pH regulation of transport by 2 histidines in transmembrane domain 6
Lam-Yuk-Tseung, S., Govoni, G. R., Forbes, J., & Gros, P. (2003) · Blood · doi:10.1182/blood-2002-07-2108 · Cited by 103 · see citing works
The effects of mutations in the ant promoter of phage P22 depend on context.
Graña, D., Gardella, T. J., & Susskind, M. M. (1988) · Genetics · doi:10.1093/genetics/120.2.319 · Cited by 99 · see citing works
The ability of Salmonella typhimurium to produce the siderophore enterobactin is not a virulence factor in mouse typhoid
Benjamin, W. H., Turnbough, C. L., Posey, B. S., & Briles, D. E. (1985) · Infection and Immunity · doi:10.1128/iai.50.2.392-397.1985 · Cited by 90 · see citing works
Binding of Ferric Enterobactin by theEscherichia coliPeriplasmic Protein FepB
Sprencel, C., Cao, Z., Qi, Z., Scott, D. C., Montague, M. A., Ivanoff, N., Xu, J., Raymond, K., Newton, S. M. C., & Klebba, P. E. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.19.5359-5364.2000 · Cited by 82 · see citing works
Role of Receptor Proteins for Enterobactin and 2,3-Dihydroxybenzoylserine in Virulence of Salmonella enterica
Rabsch, W., Methner, U., Voigt, W., Tschäpe, H., Reissbrodt, R., & Williams, P. H. (2003) · Infection and Immunity · doi:10.1128/iai.71.12.6953-6961.2003 · Cited by 81 · see citing works
Catecholate receptor proteins in Salmonella enterica: role in virulence and implications for vaccine development
Williams, P. H., Rabsch, W., Methner, U., Voigt, W., Tschäpe, H., & Reissbrodt, R. (2005) · Vaccine · doi:10.1016/j.vaccine.2005.07.020 · Cited by 78 · see citing works
Exochelin genes in Mycobacterium smegmatis: identification of an ABC transporter and two non‐ribosomal peptide synthetase genes
Zhu, W., Arceneaux, J. E. L., Beggs, M. L., Byers, B. R., Eisenach, K. D., & Lundrigan, M. D. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.00961.x · Cited by 70 · see citing works
Microbial Evasion of the Immune System: Structural Modifications of Enterobactin Impair Siderocalin Recognition
Abergel, R. J., Moore, E. G., Strong, R. K., & Raymond, K. N. (2006) · Journal of the American Chemical Society · doi:10.1021/ja062476+ · Cited by 65 · see citing works
Molecular and clinical aspects of iron homeostasis: from anemia to hemochromatosis
Nairz, M., & Weiß, G. (2006) · Wiener klinische Wochenschrift · doi:10.1007/s00508-006-0653-7 · Cited by 54 · see citing works
Enzymatic Tailoring of Enterobactin Alters Membrane Partitioning and Iron Acquisition
Luo, M., Lin, H., Fischbach, M. A., Liu, D. R., Walsh, C. T., & Groves, J. T. (2006) · ACS Chemical Biology · doi:10.1021/cb0500034 · Cited by 52 · see citing works
BordetellaAlcS Transporter Functions in Alcaligin Siderophore Export and Is Central to Inducer Sensing in Positive Regulation of Alcaligin System Gene Expression
Brickman, T. J., & Armstrong, S. K. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.11.3650-3661.2005 · Cited by 48 · see citing works
ThecsbXgene ofAzotobacter vinelandiiencodes an MFS efflux pump required for catecholate siderophore export
Page, W. J., Kwon, E. N., Cornish, A. S., & Tindale, A. E. (2003) · FEMS Microbiology Letters · doi:10.1016/s0378-1097(03)00753-5 · Cited by 35 · see citing works
Iron-regulated excretion of alpha-keto acids by Salmonella typhimurium
Reissbrodt, R., Kingsley, R. A., Rabsch, W., Beer, W., Roberts, M., & WILLIAMS, P. H. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.14.4538-4544.1997 · Cited by 34 · see citing works
Involvement of the Vibrio parahaemolyticus pvsC gene in export of the siderophore vibrioferrin.
Tanabe, T., Nakao, H., Kuroda, T., Tsuchiya, T., & Yamamoto, S. (2006) · PubMed · Cited by 23 · see citing works
TonB-dependent iron supply inSalmonellaby α-ketoacids and α-hydroxyacids
Kingsley, R. A., Rabsch, W., Roberts, M., Reissbrodt, R., & WILLIAMS, P. H. (1996) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1996.tb08316.x · Cited by 23 · see citing works
Pathogenic Escherichia coli, Shigella , and Salmonella
Payne, S. M., & Mey, A. R. (2014) · ASM Press eBooks · doi:10.1128/9781555816544.ch14 · Cited by 16 · see citing works
A new hydroxamate siderophore for iron supply of Salmonella.
Rabsch, W., Paul, P., & Reissbrodt, R. (1987) · PubMed · Cited by 15 · see citing works
Uptake of Iron by Isolated Rat Hepatocytes from a Hydrophilic Impermeant Ferric Chelate, Fe(III)-DTPA
Scheiber‐Mojdehkar, B., & Goldenberg, H. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0064 · Cited by 14 · see citing works

Flagged first, then by citations

Research works printed but not linked: 1

10.1021/ja062476 · DOI

Sorted by citations

Structure, Function, and Evolution of Bacterial ATP-Binding Cassette Systems
Davidson, A. L., Dassa, E., Orelle, C., & Chen, J. (2008) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00031-07 · Cited by 1,422 · see citing works
Probiotic Bacteria Reduce Salmonella Typhimurium Intestinal Colonization by Competing for Iron
Deriu, E., Liu, J. Z., Pezeshki, M., Edwards, R. A., Ochoa, R. J., Contreras, H., Libby, S. J., Fang, F. C., & Raffatellu, M. (2013) · Cell Host & Microbe · doi:10.1016/j.chom.2013.06.007 · Cited by 550 · see citing works
Self-citation
Lipocalin-2 Resistance Confers an Advantage to Salmonella enterica Serotype Typhimurium for Growth and Survival in the Inflamed Intestine
Raffatellu, M., George, M. D., Akiyama, Y., Hornsby, M. J., Nuccio, S.-P., Paixao, T. A., Butler, B. P., Chu, H., Santos, R. L., Berger, T., et al. (2009) · Cell Host & Microbe · doi:10.1016/j.chom.2009.03.011 · Cited by 525 · see citing works
Immunometabolism at the interface between macrophages and pathogens
Russell, D. G., Huang, L., & VanderVen, B. C. (2019) · Nature reviews. Immunology · doi:10.1038/s41577-019-0124-9 · Cited by 460 · see citing works
Microbial siderophores: a mini review
Saha, R., Saha, N., Donofrio, R. S., & Bestervelt, L. L. (2012) · Journal of Basic Microbiology · doi:10.1002/jobm.201100552 · Cited by 438 · see citing works
The struggle for iron - a metal at the host-pathogen interface: Iron at the host-pathogen interface
Nairz, M., Schroll, A., Sonnweber, T., & Weiss, G. (2010) · Cellular Microbiology · doi:10.1111/j.1462-5822.2010.01529.x · Cited by 398 · see citing works
Iron, copper, zinc, and manganese transport and regulation in pathogenic Enterobacteria: correlations between strains, site of infection and the relative importance of the different metal transport systems for virulence
Porcheron, G., Garénaux, A., Proulx, J., Sabri, M., & Dozois, C. M. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00090 · Cited by 367 · see citing works
Iron at the interface of immunity and infection
Nairz, M., Haschka, D., Demetz, E., & Weiss, G. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00152 · Cited by 325 · see citing works
“The activation and expression of such microbial iron acquisition systems is linked to their pathogenicity and proliferation (Rabsch et al., 1999; Schrettl et al., 2004; Crouch et al., 2008; Andrews-Polymenis et al., 2010; Cassat and Skaar, 2013).”
Background
Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humans
Caza, M., & Kronstad, J. W. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00080 · Cited by 306 · see citing works
The siderophore yersiniabactin binds copper to protect pathogens during infection
Chaturvedi, K. S., Hung, C. S., Crowley, J. R., Stapleton, A. E., & Henderson, J. P. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1020 · Cited by 301 · see citing works
The Cytokine IL-22 Promotes Pathogen Colonization by Suppressing Related Commensal Bacteria
Behnsen, J., Jellbauer, S., Wong, C. P., Edwards, R. A., George, M. D., Ouyang, W., & Raffatellu, M. (2014) · Immunity · doi:10.1016/j.immuni.2014.01.003 · Cited by 279 · see citing works
Resistance and survival strategies of Salmonella enterica to environmental stresses
Spector, M. P., & Kenyon, W. J. (2011) · Food Research International · doi:10.1016/j.foodres.2011.06.056 · Cited by 268 · see citing works
Th17 Cytokines and the Gut Mucosal Barrier
Blaschitz, C., & Raffatellu, M. (2010) · Journal of Clinical Immunology · doi:10.1007/s10875-010-9368-7 · Cited by 247 · see citing works
Trace metals and animal health: Interplay of the gut microbiota with iron, manganese, zinc, and copper
Pajarillo, E. A. B., Lee, E.-S., & Kang, D. (2021) · Animal nutrition · doi:10.1016/j.aninu.2021.03.005 · Cited by 227 · see citing works
Metal limitation and toxicity at the interface between host and pathogen
Becker, K. W., & Skaar, E. P. (2014) · FEMS Microbiology Reviews · doi:10.1111/1574-6976.12087 · Cited by 223 · see citing works
The ins and outs of bacterial iron metabolism
Frawley, E. R., & Fang, F. C. (2014) · Molecular Microbiology · doi:10.1111/mmi.12709 · Cited by 222 · see citing works
Self-citation
Iron acquisition strategies of bacterial pathogens
Sheldon, J. R., Laakso, H. A., & Heinrichs, D. E. (2016) · Microbiology Spectrum · doi:10.1128/microbiolspec.vmbf-0010-2015 · Cited by 219 · see citing works
Nitric oxide–mediated regulation of ferroportin-1 controls macrophage iron homeostasis and immune function in Salmonella infection
Nairz, M., Schleicher, U., Schroll, A., Sonnweber, T., Theurl, I., Ludwiczek, S., Talasz, H., Brandacher, G., Moser, P. L., Muckenthaler, M. U., et al. (2013) · Journal of Experimental Medicine · doi:10.1084/jem.20121946 · Cited by 204 · see citing works
Self-citation
Life in the inflamed intestine, Salmonella style
Santos, R. L., Raffatellu, M., Bevins, C. L., Adams, L. G., Tükel, Ç., Tsolis, R. M., & Bäumler, A. J. (2009) · Trends in Microbiology · doi:10.1016/j.tim.2009.08.008 · Cited by 197 · see citing works
Mucosal lipocalin 2 has pro-inflammatory and iron-sequestering effects in response to bacterial enterobactin
Bachman, M. A., Miller, V. L., & Weiser, J. N. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000622 · Cited by 186 · see citing works
Salicylic Acid Biosynthesis and Metabolism: A Divergent Pathway for Plants and Bacteria
Mishra, A. K., & Baek, K.-H. (2021) · Biomolecules · doi:10.3390/biom11050705 · Cited by 184 · see citing works
Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT)
Ud-Din, A. I. M. S., Tikhomirova, A., & Roujeinikova, A. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17071018 · Cited by 176 · see citing works
Enterobactin-Mediated Delivery of β-Lactam Antibiotics Enhances Antibacterial Activity against Pathogenic Escherichia coli
Zheng, T., & Nolan, E. M. (2014) · Journal of the American Chemical Society · doi:10.1021/ja503911p · Cited by 167 · see citing works
Interferon‐γ limits the availability of iron for intramacrophage Salmonella typhimurium
Nairz, M., Fritsche, G., Brunner, P., Talasz, H., Hantke, K., & Weiss, G. (2008) · European Journal of Immunology · doi:10.1002/eji.200738056 · Cited by 151 · see citing works
The <scp> Y </scp> ersinia pestis siderophore, yersiniabactin, and the <scp>ZnuABC</scp> system both contribute to zinc acquisition and the development of lethal septicaemic plague in mice
Bobrov, A. G., Kirillina, O., Fetherston, J. D., Miller, M. C., Burlison, J. A., & Perry, R. D. (2014) · Molecular Microbiology · doi:10.1111/mmi.12693 · Cited by 149 · see citing works
Absence of functional Hfe protects mice from invasive Salmonella enterica Serovar Typhimurium infection via induction of lipocalin-2
Nairz, M., Theurl, I., Schroll, A., Theurl, M., Fritsche, G., Lindner, E., Seifert, M., Crouch, M.-L. V., Hantke, K., Akira, S., et al. (2009) · Blood · doi:10.1182/blood-2009-05-223354 · Cited by 146 · see citing works
Self-citation
The Pyromaniac Inside You: Salmonella Metabolism in the Host Gut
Rivera-Chávez, F., & Bäumler, A. J. (2015) · Annual Review of Microbiology · doi:10.1146/annurev-micro-091014-104108 · Cited by 143 · see citing works
Bacterial Metabolism Shapes the Host–Pathogen Interface
Passalacqua, K. D., Charbonneau, M., & O’Riordan, M. X. (2016) · Microbiology Spectrum · doi:10.1128/microbiolspec.vmbf-0027-2015 · Cited by 143 · see citing works
The ins and outs of siderophore mediated iron uptake by extra-intestinal pathogenic Escherichia coli
Garénaux, A., Caza, M., & Dozois, C. M. (2011) · Veterinary Microbiology · doi:10.1016/j.vetmic.2011.05.023 · Cited by 141 · see citing works
Salmochelin, the long-overlooked catecholate siderophore of Salmonella
Müller, S. I., Valdebenito, M., & Hantke, K. (2009) · BioMetals · doi:10.1007/s10534-009-9217-4 · Cited by 141 · see citing works
Transition metal ions at the crossroads of mucosal immunity and microbial pathogenesis
Diaz-Ochoa, V. E., Jellbauer, S., Klaus, S., & Raffatellu, M. (2014) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2014.00002 · Cited by 129 · see citing works
Inhibition of Siderophore Biosynthesis in Mycobacterium tuberculosis with Nucleoside Bisubstrate Analogues: Structure−Activity Relationships of the Nucleobase Domain of 5′-O-[N-(Salicyl)sulfamoyl]adenosine
Neres, J., Labello, N. P., Somu, R. V., Boshoff, H. I., Wilson, D. J., Vannada, J., Chen, L., Barry, C. E., Bennett, E. M., & Aldrich, C. C. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm800567v · Cited by 129 · see citing works
High-Affinity Manganese Coordination by Human Calprotectin Is Calcium-Dependent and Requires the Histidine-Rich Site Formed at the Dimer Interface
Hayden, J. A., Brophy, M. B., Cunden, L. S., & Nolan, E. M. (2012) · Journal of the American Chemical Society · doi:10.1021/ja3096416 · Cited by 128 · see citing works
Disruption of Mycobactin Biosynthesis Leads to Attenuation of Mycobacterium tuberculosis for Growth and Virulence
Reddy, P. V., Puri, R. V., Chauhan, P., Kar, R., Rohilla, A., Khera, A., & Tyagi, A. K. (2013) · The Journal of Infectious Diseases · doi:10.1093/infdis/jit250 · Cited by 127 · see citing works
Specific Roles of the iroBCDEN Genes in Virulence of an Avian Pathogenic Escherichia coli O78 Strain and in Production of Salmochelins
Caza, M., Lepine, F. L., Milot, S. M., & Dozois, C. M. (2008) · Infection and Immunity · doi:10.1128/iai.00455-08 · Cited by 126 · see citing works
Polymicrobial–Host Interactions during Infection
Tay, W. H., Chong, K. K. L., & Kline, K. A. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.05.006 · Cited by 126 · see citing works
AcrB, AcrD, and MdtABC Multidrug Efflux Systems Are Involved in Enterobactin Export in Escherichia coli
Horiyama, T., & Nishino, K. (2014) · PLoS ONE · doi:10.1371/journal.pone.0108642 · Cited by 125 · see citing works
Iron and innate antimicrobial immunity-depriving the pathogen, defending the host
Nairz, M., Dichtl, S., Schroll, A., Haschka, D., Tymoszuk, P., Theurl, I., & Weiss, G. (2018) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2018.03.007 · Cited by 123 · see citing works
Role of divalent metals in infectious disease susceptibility and outcome
Weiss, G., & Carver, P. L. (2018) · Clinical Microbiology and Infection · doi:10.1016/j.cmi.2017.01.018 · Cited by 123 · see citing works
Molecular strategies of microbial iron assimilation: from high-affinity complexes to cofactor assembly systems
Miethke, M. (2012) · Metallomics · doi:10.1039/c2mt20193c · Cited by 121 · see citing works
Contribution of Siderophore Systems to Growth and Urinary Tract Colonization of Asymptomatic Bacteriuria Escherichia coli
Watts, R. E., Totsika, M., Challinor, V. L., Mabbett, A. N., Ulett, G. C., Voss, J. J. D., & Schembri, M. A. (2011) · Infection and Immunity · doi:10.1128/iai.05594-11 · Cited by 116 · see citing works
Interplay between enterobactin, myeloperoxidase and lipocalin 2 regulates E. coli survival in the inflamed gut
Singh, V., Yeoh, B. S., Xiao, X., Kumar, M., Bachman, M. A., Borregaard, N., Joe, B., & Vijay–Kumar, M. (2015) · Nature Communications · doi:10.1038/ncomms8113 · Cited by 115 · see citing works
The role of metal ions in the virulence and viability of bacterial pathogens
Neville, S. L. (2019) · Biochemical Society Transactions · doi:10.1042/bst20180275 · Cited by 114 · see citing works
Salmonella enterica Serovar Typhimurium Strategies for Host Adaptation
Anderson, C. J., & Kendall, M. M. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.01983 · Cited by 106 · see citing works
Iron Regulatory Proteins Mediate Host Resistance to Salmonella Infection
Nairz, M., Ferring-Appel, D., Casarrubea, D., Sonnweber, T., Viatte, L., Schroll, A., Haschka, D., Fang, F. C., Hentze, M. W., Weiss, G., et al. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.06.017 · Cited by 103 · see citing works
Self-citation
The phage shock protein PspA facilitates divalent metal transport and is required for virulence of Salmonella enterica sv. Typhimurium
Karlinsey, J. E., Maguire, M. E., Becker, L. A., Crouch, M. V., & Fang, F. C. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07357.x · Cited by 102 · see citing works
Self-citation
Iron and citrate export by a major facilitator superfamily pump regulates metabolism and stress resistance in Salmonella Typhimurium
Frawley, E. R., Crouch, M.-L. V., Bingham-Ramos, L. K., Robbins, H. F., Wang, W., Wright, G. D., & Fang, F. C. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218274110 · Cited by 101 · see citing works
Self-citation
Slc11a1 limits intracellular growth ofSalmonella entericasv. Typhimurium by promoting macrophage immune effector functions and impairing bacterial iron acquisition
Nairz, M., Fritsche, G., Crouch, M.-L. V., Barton, H. C., Fang, F. C., & Weiss, G. (2009) · Cellular Microbiology · doi:10.1111/j.1462-5822.2009.01337.x · Cited by 100 · see citing works
Self-citation
Xenosiderophore Utilization Promotes Bacteroides thetaiotaomicron Resilience during Colitis
Zhu, W., Winter, M. G., Spiga, L., Hughes, E. R., Chanin, R. B., Mulgaonkar, A., Pennington, J., Maas, M., Behrendt, C. L., Kim, J., et al. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.01.010 · Cited by 100 · see citing works
The Iron hand of Uropathogenic Escherichia Coli : The Role of Transition Metal Control in Virulence
Robinson, A. E., Heffernan, J. R., & Henderson, J. P. (2018) · Future Microbiology · doi:10.2217/fmb-2017-0295 · Cited by 95 · see citing works
The impact of intestinal inflammation on the nutritional environment of the gut microbiota
Faber, F., & Bäumler, A. J. (2014) · Immunology Letters · doi:10.1016/j.imlet.2014.04.014 · Cited by 92 · see citing works
Understanding How Minerals Contribute to Optimal Immune Function
Ştefanache, A., Lungu, I. I., Butnariu, I.-A., Călin, G., Guțu, C., Marcu, C., Grierosu, C., Goroftei, E. R. B., Duceac, L.-D., Dabija, M. G., et al. (2023) · Journal of Immunology Research · doi:10.1155/2023/3355733 · Cited by 91 · see citing works
‘Ride on the ferrous wheel’ – The cycle of iron in macrophages in health and disease
Nairz, M., Schroll, A., Demetz, E., Tancevski, I., Theurl, I., & Weiss, G. (2015) · Immunobiology · doi:10.1016/j.imbio.2014.09.010 · Cited by 89 · see citing works
Invasive Non-typhoidal Salmonella (iNTS) Infections
Fierer, J. (2022) · Clinical Infectious Diseases · doi:10.1093/cid/ciac035 · Cited by 87 · see citing works
Targeting iron assimilation to develop new antibacterials
Foley, T. L., & Simeonov, A. M. (2012) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2012.708335 · Cited by 82 · see citing works
Th17 cytokines and host-pathogen interactions at the mucosa: Dichotomies of help and harm
Liu, J. Z., Pezeshki, M., & Raffatellu, M. (2009) · Cytokine · doi:10.1016/j.cyto.2009.07.005 · Cited by 80 · see citing works
Proteomic Analyses of Intracellular Salmonella enterica Serovar Typhimurium Reveal Extensive Bacterial Adaptations to Infected Host Epithelial Cells
Liu, Y., Zhang, Q., Hu, M., Yu, K., Fu, J., Zhou, F., & Liu, X. (2015) · Infection and Immunity · doi:10.1128/iai.02882-14 · Cited by 77 · see citing works
Discovery and Characterization of New Hydroxamate Siderophores, Baumannoferrin A and B, produced by Acinetobacter baumannii
Penwell, W. F., DeGrace, N., Tentarelli, S., Gauthier, L., Gilbert, C. M., Arivett, B. A., Miller, A. A., Durand-Réville, T. F., Joubran, C., & Actis, L. A. (2015) · ChemBioChem · doi:10.1002/cbic.201500147 · Cited by 73 · see citing works
Slc11a1 (Nramp1) impairs growth of Salmonella enterica serovar typhimurium in macrophages via stimulation of lipocalin-2 expression
Fritsche, G., Nairz, M., Libby, S. J., Fang, F. C., & Weiss, G. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.1111554 · Cited by 72 · see citing works
Self-citation
The ferric enterobactin transporter Fep is required for persistent Salmonella enterica serovar Typhimurium infection
Nagy, T. A., Moreland, S. M., Andrews-Polymenis, H., & Detweiler, C. S. (2013) · Infection and Immunity · doi:10.1128/iai.00412-13 · Cited by 72 · see citing works
The interplay between siderophore secretion and coupled iron and copper transport in the heterocyst-forming cyanobacterium Anabaena sp. PCC 7120
Nicolaisen, K., Hahn, A. S., Valdebenito, M., Moslavac, S., Samborski, A., Maldener, I., Wilken, C., Valladares, A., Flores, E., Hantke, K., et al. (2010) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2010.07.008 · Cited by 71 · see citing works
Iron Transport and Metabolism in Escherichia, Shigella, and Salmonella
Mey, A. R., Gómez-Garzón, C., & Payne, S. M. (2021) · EcoSal Plus · doi:10.1128/ecosalplus.esp-0034-2020 · Cited by 70 · see citing works
Siderophore-based detection of Fe(iii) and microbial pathogens
Zheng, T., & Nolan, E. M. (2012) · Metallomics · doi:10.1039/c2mt20082a · Cited by 70 · see citing works
Secretion, but not overall synthesis, of catecholate siderophores contributes to virulence of extraintestinal pathogenic Escherichia coli
Caza, M., Lepine, F. L., & Dozois, C. M. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07570.x · Cited by 69 · see citing works
Lipocalin‐2 ensures host defense against Salmonella Typhimurium by controlling macrophage iron homeostasis and immune response
Nairz, M., Schroll, A., Haschka, D., Dichtl, S., Sonnweber, T., Theurl, I., Theurl, M., Lindner, E., Demetz, E., Aßhoff, M., et al. (2015) · European Journal of Immunology · doi:10.1002/eji.201545569 · Cited by 67 · see citing works
Self-citation
An efflux pump is required for siderophore recycling by Pseudomonas aeruginosa
Yeterian, E., Martin, L. W., Lamont, I. L., & Schalk, I. J. (2009) · Environmental Microbiology Reports · doi:10.1111/j.1758-2229.2009.00115.x · Cited by 64 · see citing works
Heme oxygenase 1 controls early innate immune response of macrophages toSalmonellaTyphimurium infection: Heme oxygenase 1 expression affects Salmonellainfection
Mitterstiller, A.-M., Haschka, D., Dichtl, S., Nairz, M., Demetz, E., Talasz, H., Soares, M. P., Einwallner, E., Esterbauer, H., Fang, F. C., et al. (2016) · Cellular Microbiology · doi:10.1111/cmi.12578 · Cited by 62 · see citing works
Self-citation
An overview of recent progress in siderophore-antibiotic conjugates
Kong, H., Cheng, W., Han, W., Yuan, Y., Yang, Z., & Zhang, X. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.111615 · Cited by 62 · see citing works
G.I. pros: Antimicrobial defense in the gastrointestinal tract
Chung, L. K., & Raffatellu, M. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.02.001 · Cited by 60 · see citing works
Intracellular niche-specific profiling reveals transcriptional adaptations required for the cytosolic lifestyle of Salmonella enterica
Powers, T. R., Haeberle, A. L., Predeus, A. V., Hammarlöf, D. L., Cundiff, J. A., Saldaña‐Ahuactzi, Z., Hokamp, K., Hinton, J. C. D., & Knodler, L. A. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009280 · Cited by 59 · see citing works
An antioxidant role for catecholate siderophores in Salmonella
Achard, M. E. S., Chen, K. W., Sweet, M. J., Watts, R. E., Schroder, K., Schembri, M. A., & McEwan, A. G. (2013) · Biochemical Journal · doi:10.1042/bj20121771 · Cited by 57 · see citing works
Genome-wide Analysis of Salmonella enterica serovar Typhi in Humanized Mice Reveals Key Virulence Features
Karlinsey, J. E., Stepien, T. A., Mayho, M., Singletary, L. A., Bingham-Ramos, L. K., Brehm, M. A., Greiner, D. L., Shultz, L. D., Gallagher, L. A., Bawn, M., et al. (2019) · Cell Host & Microbe · doi:10.1016/j.chom.2019.08.001 · Cited by 56 · see citing works
Self-citation
Detection and Molecular Identification of Salmonella Virulence Genes in Livestock Production Systems in South Africa
Mthembu, T. P., Zishiri, O. T., & El Zowalaty, M. E. (2019) · Pathogens · doi:10.3390/pathogens8030124 · Cited by 56 · see citing works
Role of Catecholate Siderophores in Gram-Negative Bacterial Colonization of the Mouse Gut
Pi, H., Jones, S. A., Mercer, L. E., Meador, J. P., Caughron, J. E., Jordan, L., Newton, S. M., Conway, T., & Klebba, P. E. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050020 · Cited by 53 · see citing works
Gastrointestinal host-pathogen interaction in the age of microbiome research
Tsolis, R. M., & Bäumler, A. J. (2020) · Current Opinion in Microbiology · doi:10.1016/j.mib.2020.03.002 · Cited by 53 · see citing works
The Major Facilitator Superfamily-Type Transporter YmfE and the Multidrug-Efflux Activator Mta Mediate Bacillibactin Secretion inBacillus subtilis
Miethke, M., Schmidt, S., & Marahiel, M. A. (2008) · Journal of Bacteriology · doi:10.1128/jb.00464-08 · Cited by 53 · see citing works
Stenotrophomonas maltophilia produces an EntC-dependent catecholate siderophore that is distinct from enterobactin
Nas, M. Y., & Cianciotto, N. P. (2017) · Microbiology · doi:10.1099/mic.0.000545 · Cited by 51 · see citing works
Purification of Legiobactin and Importance of This Siderophore in Lung Infection byLegionella pneumophila
Allard, K. A., Dao, J., Sanjeevaiah, P., McCoy-Simandle, K., Chatfield, C. H., Crumrine, D. S., Castignetti, D., & Cianciotto, N. P. (2009) · Infection and Immunity · doi:10.1128/iai.00087-09 · Cited by 51 · see citing works
Microbial siderophore-based iron assimilation and therapeutic applications
Li, K., Chen, W., & Bruner, S. D. (2016) · BioMetals · doi:10.1007/s10534-016-9935-3 · Cited by 51 · see citing works
Dopamine Is a Siderophore-Like Iron Chelator That Promotes Salmonella enterica Serovar Typhimurium Virulence in Mice
Dichtl, S., Demetz, E., Haschka, D., Tymoszuk, P., Petzer, V., Nairz, M., Seifert, M., Hoffmann, A., Brigo, N., Würzner, R., et al. (2019) · mBio · doi:10.1128/mbio.02624-18 · Cited by 50 · see citing works
Self-citation
Virulence Factors in Klebsiella pneumoniae: A Literature Review
Monteiro, A. D. S. S., Cordeiro, S. M., & Pedreira, J. N. R. (2024) · Indian Journal of Microbiology · doi:10.1007/s12088-024-01247-0 · Cited by 49 · see citing works
Genetic and Dietary Iron Overload Differentially Affect the Course of Salmonella Typhimurium Infection
Nairz, M., Schroll, A., Haschka, D., Dichtl, S., Tymoszuk, P., Demetz, E., Moser, P., Haas, H., Fang, F. C., Theurl, I., et al. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00110 · Cited by 46 · see citing works
Self-citation
Strategies adopted by Salmonella to survive in host: a review
Li, W., Ren, Q., Ni, T., Zhao, Y., Sang, Z., Luo, R., Li, Z., & Li, S. (2023) · Archives of Microbiology · doi:10.1007/s00203-023-03702-w · Cited by 46 · see citing works
Genome-Wide Transposon Mutagenesis Identifies a Role for Host Neuroendocrine Stress Hormones in Regulating the Expression of Virulence Genes inSalmonella
Spencer, H., Karavolos, M. H., Bulmer, D. M., Aldridge, P. D., Chhabra, S. R., Winzer, K., Williams, P. M., & Khan, C. M. A. (2009) · Journal of Bacteriology · doi:10.1128/jb.01329-09 · Cited by 45 · see citing works
Microcins and urovirulence in Escherichia coli
Azpiroz, M. F., Poey, M. E., & Laviña, M. D. (2009) · Microbial Pathogenesis · doi:10.1016/j.micpath.2009.09.003 · Cited by 44 · see citing works
Whole Genome Sequencing detects Inter-Facility Transmission of Carbapenem-resistant Klebsiella pneumoniae
Spencer, M., Winglee, K., Passaretti, C. L., Earl, A. M., Manson, A. L., Mulder, H. P., Sautter, R. L., & Fodor, A. A. (2018) · Journal of Infection · doi:10.1016/j.jinf.2018.11.003 · Cited by 44 · see citing works
Linearized Siderophore Products Secreted via MacAB Efflux Pump Protect Salmonella enterica Serovar Typhimurium from Oxidative Stress
Bogomolnaya, L. M., Tilvawala, R. R., Elfenbein, J. R., Cirillo, J. D., & Andrews‐Polymenis, H. L. (2020) · mBio · doi:10.1128/mbio.00528-20 · Cited by 44 · see citing works
ZIPCO, a putative metal ion transporter, is crucial for Plasmodium liver‐stage development
Sahu, T., Boisson, B., Lacroix, C., Bischoff, E., Richier, Q., Formaglio, P., Thiberge, S., Dobrescu, I., Ménard, R., & Baldacci, P. A. (2014) · EMBO Molecular Medicine · doi:10.15252/emmm.201403868 · Cited by 43 · see citing works
Iron Efflux by PmtA Is Critical for Oxidative Stress Resistance and Contributes Significantly to Group A Streptococcus Virulence
VanderWal, A. R., Makthal, N., Pinochet‐Barros, A., Helmann, J. D., Olsen, R. J., & Kumaraswami, M. (2017) · Infection and Immunity · doi:10.1128/iai.00091-17 · Cited by 43 · see citing works
System-level analysis of Salmonella metabolism during infection
Bumann, D. (2009) · Current Opinion in Microbiology · doi:10.1016/j.mib.2009.08.004 · Cited by 42 · see citing works
A Salmochelin S4-Inspired Ciprofloxacin Trojan Horse Conjugate
Sanderson, T. J., Black, C. M., Southwell, J. W., Wilde, E. J., Pandey, A. K., Herman, R., Thomas, G. H., Boros, E., Duhme‐Klair, A., & Routledge, A. (2020) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.0c00568 · Cited by 41 · see citing works
Biosynthetic considerations of triscatechol siderophores framed on serine and threonine macrolactone scaffolds
Reitz, Z. L., Sandy, M., & Butler, A. (2017) · Metallomics · doi:10.1039/c7mt00111h · Cited by 40 · see citing works
Requirement of Siderophore Biosynthesis for Plant Colonization by Salmonella enterica
Hao, L., Willis, D. K., Andrews‐Polymenis, H. L., McClelland, M., & Barak, J. D. (2012) · Applied and Environmental Microbiology · doi:10.1128/aem.07867-11 · Cited by 39 · see citing works
Interplay between ferric uptake regulator Fur and horizontally acquired virulence regulator EsrB coordinates virulence gene expression in Edwardsiella piscicida
Shao, S., Li, C., Zhao, L., Zhang, Y., Yin, K., & Wang, Q. (2021) · Microbiological Research · doi:10.1016/j.micres.2021.126892 · Cited by 39 · see citing works
Acquisition of regulator on virulence plasmid of hypervirulent Klebsiella allows bacterial lifestyle switch in response to iron
Chu, W. H. W., Tan, Y. H., Tan, S. Y., Chen, Y., Yong, M., Lye, D. C., Kalimuddin, S., Archuleta, S., & Gan, Y. (2023) · mBio · doi:10.1128/mbio.01297-23 · Cited by 37 · see citing works
Salmonella proteomics under oxidative stress reveals coordinated regulation of antioxidant defense with iron metabolism and bacterial virulence
Fu, J., Qi, L., Hu, M., Liu, Y., Yu, K., Liu, Q. S., & Liu, X. (2017) · Journal of Proteomics · doi:10.1016/j.jprot.2017.02.004 · Cited by 36 · see citing works
Facile synthesis of salmochelin S1, S2, MGE, DGE, and TGE
Yu, X., Dai, Y., Yang, T., Gagné, M. R., & Gong, H. (2010) · Tetrahedron · doi:10.1016/j.tet.2010.11.007 · Cited by 36 · see citing works
Expression of IroN, the salmochelin siderophore receptor, requires mRNA activation by RyhB small RNA homologues
Balbontín, R., Villagra, N. A., de la Gándara, M. P., Mora, G. C., Figueroa‐Bossi, N., & Bossi, L. (2015) · Molecular Microbiology · doi:10.1111/mmi.13307 · Cited by 35 · see citing works
Nifedipine Affects the Course of Salmonella enterica Serovar Typhimurium Infection by Modulating Macrophage Iron Homeostasis
Mair, S. M., Nairz, M., Bellmann-Weiler, R., Muehlbacher, T., Schroll, A., Theurl, I., Moser, P. L., Talasz, H., Fang, F. C., & Weiss, G. (2011) · The Journal of Infectious Diseases · doi:10.1093/infdis/jir395 · Cited by 33 · see citing works
Self-citation
<scp>S</scp>almonellaacquires ferrous iron from haemophagocytic macrophages
Nagy, T. A., Moreland, S. M., & Detweiler, C. S. (2014) · Molecular Microbiology · doi:10.1111/mmi.12739 · Cited by 33 · see citing works

The ferric enterobactin transporter Fep is required for persistent Salmonella enterica serovar Typhimurium infection
Nagy, T. A., Moreland, S. M., Andrews-Polymenis, H., & Detweiler, C. S. (2013) · Infection and Immunity · doi:10.1128/iai.00412-13 · Cited by 72 · see citing works
Correspondence
Zhu, M., Valdebenito, M., Winkelmann, G., Hantke, K., & Hantke, K. (2005)
Salmochelins, siderophores of Salmonella enterica and uropathogenic Escherichia coli strains, are recognized by the outer membrane receptor IroN
Hantke, K., Nicholson, G., Rabsch, W., & Winkelmann, G. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0737682100 · Cited by 359 · see citing works
The ability of Salmonella typhimurium to produce the siderophore enterobactin is not a virulence factor in mouse typhoid
Benjamin, W. H., Turnbough, C. L., Posey, B. S., & Briles, D. E. (1985) · Infection and Immunity · doi:10.1128/iai.50.2.392-397.1985 · Cited by 90 · see citing works
Catecholate siderophore esterases Fes, IroD and IroE are required for salmochelins secretion following utilization, but only IroD contributes to virulence of extra‐intestinal pathogenic E scherichia coli
Caza, M., Garénaux, A., Lepine, F. L., & Dozois, C. M. (2015) · Molecular Microbiology · doi:10.1111/mmi.13059 · Cited by 32 · see citing works

Authors: Crouch, M. V., Castor, M., Karlinsey, J. E., Kalhorn, T., & Fang, F. C.
Affiliations: University of Washington (US)
Corresponding author: Fang, Ferric C.
ORCID: Karlinsey, Joyce E.
Fang, Ferric C.
Venue: Molecular Microbiology
Publisher: Wiley
Published: 2008-01-14
Volume: 67
Issue: 5
Pages: 971-983
ISSN: 0950-382X (ISSN-L)
1365-2958
DOI: 10.1111/j.1365-2958.2007.06089.x
OpenAlex: W2087509245
Cited by: 187
References: 46
Citations by year: 2026: 8 · 2025: 4 · 2024: 6 · 2023: 8 · 2022: 13 · 2021: 10 · 2020: 14 · 2019: 10 · 2018: 6 · 2017: 9 · 2016: 14 · 2015: 12 · 2014: 14 · 2013: 12 · 2012: 11
FWCI: 6.33
Type: journal article
Language: en
Open access: closed
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: Molecular Microbiology (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of Allergy and Infectious Diseases (AI54052, AI 39557, R01AI050660, AI50660, F32AI054052)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Life Sciences › Agricultural and Biological Sciences › Food Science › Salmonella and Campylobacter epidemiology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Escherichia coli research studies
Keywords: salmochelin, enterobactin, siderophore biosynthesis, iron acquisition, iron starvation, Salmonella typhimurium, bacterial virulence, catecholate siderophores, systemic infection
MeSH terms: Animals, Bacterial Proteins, Biological Transport, Chromatography, Liquid, Enterobactin, Iron, Membrane Proteins, Salmonella Infections, Animal, Salmonella typhimurium, Mass Spectrometry, Virulence, Siderophores, Sequence Deletion, ATP-Binding Cassette Transporters, Mice

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Biosynthesis and IroC‐dependent export of the siderophore salmochelin are essential for virulence of Salmonella enterica serovar Typhimurium

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Cites

Cited by

Related

Record

About these checks