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MntR modulates expression of the PerR regulon and superoxide resistance in Staphylococcus aureus through control of manganese uptake
Open accessAbstract
Summary: The Staphylococcus aureus DtxR‐like protein, MntR, controls expression of the mntABC and mntH genes, which encode putative manganese transporters. Mutation of mntABC produced a growth defect in metal‐depleted medium and increased sensitivity to intracellularly generated superoxide radicals. These phenotypes resulted from diminished uptake of manganese and were rescued by the addition of excess Mn(II). Resistance to superoxide was incompletely rescued by Mn(II) for STE035 ( mntA mntH ), and the strain had reduced virulence in a murine abscess model of infection. Expression of mntABC was repressed by Mn(II) in an MntR‐dependent manner, which contrasts with the expression of mntH that was not repressed in elevated Mn(II) and was decreased in an mntR mutant. This demonstrates that MntR acts as a negative and positive regulator of these loci re‐spectively. PerR, the peroxide resistance regulon repressor, acts with MntR to control the expression of mntABC and manganese uptake. The expression of the PerR‐regulated genes, katA (catalase), ftn (ferritin) and fur (ferric uptake regulator), was diminished in STE031 ( mntR ) when grown in excess Mn(II). Therefore, the control of Mn(II)‐regulated members of the PerR regulon and the Fur protein is modulated by MntR through its control of Mn(II) uptake. The co‐ordinated regulation of metal ion homeostasis and oxidative stress resistance via the regulators MntR, PerR and Fur of S. aureus is discussed.
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In the citing paper
“In addition to regulation by MntR, mntABC is negatively regulated by PerR, a manganese and iron-dependent Fur homologue that controls responses to oxidative stress [144, 145].”
From Metal ion acquisition in Staphylococcus aureus: overcoming nutritional immunity (2012) · cites this paper as [144]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Deletion of mntR leads to constitutive transcription of mntABC irrespective of manganese levels.”
From Metal ion acquisition in Staphylococcus aureus: overcoming nutritional immunity (2012) · cites this paper as [144]
In the citing paper
“In contrast, mutation of mntH does not lead to an appreciable growth defect in metal-depleted media”
From Metal ion acquisition in Staphylococcus aureus: overcoming nutritional immunity (2012) · cites this paper as [144]
In the citing paper
“The S. aureus genome encodes MntABC-type (mntABC) and Nramp-type (mntH) manganese transporters, both of which have been functionally characterized.”
From Metal ion acquisition in Staphylococcus aureus: overcoming nutritional immunity (2012) · cites this paper as [144]
In the citing paper
“In manganese-replete conditions, transcription of mntABC is repressed by MntR.”
From Metal ion acquisition in Staphylococcus aureus: overcoming nutritional immunity (2012) · cites this paper as [144]
In the citing paper
“Mutation of mntA in S. aureus results in a reduced growth rate in metal-depleted minimal media, a phenotype that is reversible upon addition of manganese.”
From Metal ion acquisition in Staphylococcus aureus: overcoming nutritional immunity (2012) · cites this paper as [144]
In the citing paper
“suggesting that MntABC may be the dominant manganese transporter in S. aureus under in vitro conditions [144].”
From Metal ion acquisition in Staphylococcus aureus: overcoming nutritional immunity (2012) · cites this paper as [144]
In the citing paper
“The transcriptional regulator MntR affects expression of both mntABC and mntH.”
From Metal ion acquisition in Staphylococcus aureus: overcoming nutritional immunity (2012) · cites this paper as [144]
In the citing paper
“In S. aureus, mutation of mntA, mntH, or mntR in the laboratory strain 8325-4 does not lead to a significant reduction in bacterial recovery in a murine skin abscess model.”
From Metal ion acquisition in Staphylococcus aureus: overcoming nutritional immunity (2012) · cites this paper as [144]
In the citing paper
“Additionally, S. aureus employs superoxide dismutase-independent mechanisms to detoxify superoxide, a process that is also dependent on manganese [144].”
From Metal ion acquisition in Staphylococcus aureus: overcoming nutritional immunity (2012) · cites this paper as [144]
In the citing paper
“Disruption of mntA, mntH, mntR, or both mntA and mntH also significantly reduces intracellular survival in human endothelial cells [144].”
From Metal ion acquisition in Staphylococcus aureus: overcoming nutritional immunity (2012) · cites this paper as [144]
In the citing paper
“In contrast, concurrent inactivation of mntA and mntH significantly decreases bacterial recovery in this model.”
From Metal ion acquisition in Staphylococcus aureus: overcoming nutritional immunity (2012) · cites this paper as [144]
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Citations
Cites
Molecular cloning: A laboratory manual
Deininger, P. L. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,684
Staphylococcus aureus Infections
Lowy, F. D. (1998) · New England Journal of Medicine · doi:10.1056/nejm199808203390806 · Cited by 6,018
Iron and metal regulation in bacteria
Hantke, K. (2001) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(00)00184-3 · Cited by 755
Transition Metals in Control of Gene Expression
O’Halloran, T. V. (1993) · Science · doi:10.1126/science.8342038 · Cited by 626
Antibiotic-resistance cassettes for Bacillus subtilis
Guérout, A.-M., Shazand, K., Frandsen, N., & Stragier, P. (1995) · Gene · doi:10.1016/0378-1119(95)00652-4 · Cited by 595
[27] Genetic systems in Staphylococci
Novick, R. P. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)04029-n · Cited by 562
Lack of a role for iron in the Lyme disease pathogen
Posey, J. E., & Gherardini, F. C. (2000) · Science · doi:10.1126/science.288.5471.1651 · Cited by 538
Improved method for electroporation of Staphylococcus aureus
Schenk, S., & Laddaga, R. A. (1992) · FEMS Microbiology Letters · doi:10.1016/0378-1097(92)90596-g · Cited by 431
The scavenging of superoxide radical by manganous complexes: In vitro
Archibald, F. S., & Fridovich, I. (1982) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(82)90049-2 · Cited by 427
Iron uptake mechanisms of pathogenic bacteria
Wooldridge, K. G., & WILLIAMS, P. H. (1993) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.1993.tb00026.x · Cited by 426
Cited by
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Items 101–200 of 229
Schmitt, M. P. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.24.6882-6892.2002 · Cited by 50
Role and Regulation of the Shigella flexneri Sit and MntH Systems
Runyen-Janecky, L. J., Dazenski, E., Hawkins, S., & Warner, L. (2006) · Infection and Immunity · doi:10.1128/iai.00562-06 · Cited by 49
Role of the hprT–ftsH locus in Staphylococcus aureus
Lithgow, J. K., Ingham, E., & Foster, S. J. (2004) · Microbiology · doi:10.1099/mic.0.26674-0 · Cited by 48
Self-citationCovering all the Bases: Preclinical Development of an Effective Staphylococcus aureus Vaccine
Scully, I. L., Liberator, P., Jansen, K. U., & Anderson, A. S. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00109 · Cited by 47
Functional Studies of the Mycobacterium tuberculosis Iron-dependent Regulator
Chou, C. J., Wisedchaisri, G., Monfeli, R., Oram, D. M., Holmes, R. K., Hol, W. G. J., & Beeson, C. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407385200 · Cited by 47
Imlay, J. A. (2009) · EcoSal Plus · doi:10.1128/ecosalplus.5.4.4 · Cited by 46
Searching for small σB-regulated genes in Staphylococcus aureus
Nielsen, J. S., Christiansen, M. H. G., Bonde, M. J., Gottschalk, S., Frees, D., Thomsen, L. E., & Kallipolitis, B. H. (2010) · Archives of Microbiology · doi:10.1007/s00203-010-0641-1 · Cited by 46
Multiple Bactericidal Mechanisms of the Zinc Ionophore PBT2
Harbison-Price, N., Ferguson, S. A., Heikal, A., Taiaroa, G., Hards, K., Nakatani, Y., Rennison, D., Brimble, M. A., El-Deeb, I. M., Bohlmann, L., et al. (2020) · mSphere · doi:10.1128/msphere.00157-20 · Cited by 44
bifA Regulates Biofilm Development of Pseudomonas putida MnB1 as a Primary Response to H2O2 and Mn2+
Zheng, Y.-J., Li, Y., Long, H., Zhao, X., Jia, K., Li, J., Wang, L., Wang, R., Lu, X., & Zhang, D. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.01490 · Cited by 44
The iron-regulated staphylococcal lipoproteins
Sheldon, J. R., & Heinrichs, D. E. (2012) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2012.00041 · Cited by 46
Radin, J. N., Zhu, J., Brazel, E. B., McDevitt, C. A., & Kehl‐Fie, T. E. (2018) · Infection and Immunity · doi:10.1128/iai.00642-18 · Cited by 42
The impact of metal sequestration on Staphylococcus aureus metabolism
Hammer, N. D., & Skaar, E. P. (2011) · Current Opinion in Microbiology · doi:10.1016/j.mib.2011.11.004 · Cited by 44
Handke, L. D., Gribenko, A. V., Timofeyeva, Y., Scully, I. L., & Anderson, A. S. (2018) · mSphere · doi:10.1128/msphere.00336-18 · Cited by 42
Chen, H., Wu, R., Xu, G., Fang, X., Qiu, X., Guo, H., Tian, B., & Hua, Y. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.04.106 · Cited by 40
Ando, M., Manabe, Y. C., Converse, P. J., Miyazaki, E., Harrison, R., Murphy, J. R., & Bishai, W. R. (2003) · Infection and Immunity · doi:10.1128/iai.71.5.2584-2590.2003 · Cited by 40
Diep, B. A., Phung, Q. T., Date, S. V., Arnott, D. P., Bakalarski, C. E., Xu, M. J., Nakamura, G. R., Swem, D. L., Alexander, M. K., Le, H. N., et al. (2013) · The Journal of Infectious Diseases · doi:10.1093/infdis/jit662 · Cited by 38
Parveen, S., Bishai, W. R., & Murphy, J. R. (2019) · Microbiology Spectrum · doi:10.1128/microbiolspec.gpp3-0063-2019 · Cited by 38
Al‐Tameemi, H., Beavers, W. N., Norambuena, J., Skaar, E. P., & Boyd, J. M. (2020) · Molecular Microbiology · doi:10.1111/mmi.14623 · Cited by 39
Mur-LH, the Broad-Spectrum Endolysin of Lactobacillus helveticus Temperate Bacteriophage φ-0303
Deutsch, S., Guézenec, S., Piot, M., Foster, S. J., & Lortal, S. (2004) · Applied and Environmental Microbiology · doi:10.1128/aem.70.1.96-103.2004 · Cited by 38
Self-citationYu, W., Yao, D., Yu, S., Wang, X., Li, X., Wang, M., Liu, S., Feng, Z., Chen, X., Li, W., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-22044-y · Cited by 37
Toukoki, C., Gold, K. M., McIver, K. S., & Eichenbaum, Z. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07157.x · Cited by 37
Exploring Staphylococcus aureus pathways to disease for vaccine development
DeDent, A. C., Kim, H. K., Missiakas, D. M., & Schneewind, O. (2011) · Seminars in Immunopathology · doi:10.1007/s00281-011-0299-z · Cited by 36
Structural Analysis of Bacterial ABC Transporter Inhibition by an Antibody Fragment
Ahuja, S., Rougé, L., Swem, D. L., Sudhamsu, J., Wu, P., Russell, S. J., Alexander, M. K., Tam, C., Nishiyama, M., Starovasnik, M. A., et al. (2015) · Structure · doi:10.1016/j.str.2015.01.020 · Cited by 38
Popa, A. C., Fernandes, H. R., Necşulescu, M., Luculescu, C. R., Cioangher, M., Dumitru, V., Stuart, B. W., Grant, D. M., Ferreira, J. M. F., & Stan, G. E. (2018) · Ceramics International · doi:10.1016/j.ceramint.2018.11.112 · Cited by 38
Regulation of Staphylococcus aureus MntC Expression and Its Role in Response to Oxidative Stress
Handke, L. D., Hawkins, J. C., Miller, A. A., Jansen, K. U., & Anderson, A. S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077874 · Cited by 36
YsxC, an essential protein in Staphylococcus aureus crucial for ribosome assembly/stability
Cooper, E. L., Garcı́a-Lara, J., & Foster, S. J. (2009) · BMC Microbiology · doi:10.1186/1471-2180-9-266 · Cited by 36
Self-citationShabayek, S., Bauer, R., Mauerer, S., Mizaikoff, B., & Spellerberg, B. (2016) · Molecular Microbiology · doi:10.1111/mmi.13335 · Cited by 40
Radin, J. N., Kelliher, J. L., Solórzano, P. K. P., Grim, K. P., Ramezanifard, R., Slauch, J. M., & Kehl‐Fie, T. E. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1007971 · Cited by 36
Kragh, M. L., & Hansen, L. T. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.03132 · Cited by 35
Courville, P., Chaloupka, R., Veyrier, F. J., & Cellier, M. F. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309913200 · Cited by 36
Competition for Manganese at the Host–Pathogen Interface
Kelliher, J. L., & Kehl-Fie, T. E. (2016) · Progress in Molecular Biology and Translational Science · doi:10.1016/bs.pmbts.2016.05.002 · Cited by 34
Mermod, M., Mourlane, F., Waltersperger, S., Oberholzer, A. E., Baumann, U., & Solioz, M. (2010) · Journal of Bacteriology · doi:10.1128/jb.00372-10 · Cited by 34
Monoclonal Antibodies Targeting Surface-Exposed and Secreted Proteins from Staphylococci
Speziale, P., & Pietrocola, G. (2021) · Vaccines · doi:10.3390/vaccines9050459 · Cited by 37
Ménard, G., Silard, C., Suriray, M., Rouillon, A., & Augagneur, Y. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137346 · Cited by 39
Metalloregulators: Arbiters of Metal Sufficiency
Helmann, J. D., Soonsanga, S., & Gabriel, S. E. (2007) · Springer eBooks · doi:10.1007/7171_2006_073 · Cited by 33
Abrantes, M. C., Kok, J., & Lopes, M. D. F. (2013) · Infection and Immunity · doi:10.1128/iai.06377-11 · Cited by 35
Zhang, J., Yang, F., Zhang, X., Jing, H., Ren, C., Cai, C., Dong, Y., Zhang, Y., Zou, Q., & Zeng, H. (2015) · Scientific Reports · doi:10.1038/srep15553 · Cited by 31
Solórzano, P. K. P., Yao, J., Rock, C. O., & Kehl‐Fie, T. E. (2019) · mBio · doi:10.1128/mbio.01321-19 · Cited by 34
Bray, B. A., Sutcliffe, I. C., & Harrington, D. J. (2008) · Antonie van Leeuwenhoek · doi:10.1007/s10482-008-9291-6 · Cited by 30
Responses of Lactic Acid Bacteria to Heavy Metal Stress
Solioz, M., Mermod, M., Abicht, H. K., & Mancini, S. (2011) · Springer eBooks · doi:10.1007/978-0-387-92771-8_9 · Cited by 29
Sun, H., Li, M., Xu, G., Chen, H., Jiao, J., Tian, B., Wang, L., & Hua, Y. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035057 · Cited by 29
Coady, A. M., Xu, M. J., Phung, Q. T., Cheung, T. K., Bakalarski, C. E., Alexander, M. K., Lehar, S. M., Kim, J., Park, S., Tan, M., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0138350 · Cited by 30
Wang, H., Kraus, F., Popella, P., Baykal, A., Guttroff, C., François, P., Saß, P., Plietker, B. J., & Götz, F. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.00014 · Cited by 29
Genome-Wide Characterization of the SloR Metalloregulome in Streptococcus mutans
O’Rourke, K. P., Shaw, J. D., Pesesky, M. W., Cook, B. T., Roberts, S. M., Bond, J. P., & Spatafora, G. A. (2009) · Journal of Bacteriology · doi:10.1128/jb.01161-09 · Cited by 28
Massonet, C., Pintens, V., Merckx, R., Anné, J., Lammertyn, E., & Eldere, J. V. (2006) · BMC Microbiology · doi:10.1186/1471-2180-6-103 · Cited by 27
Gribenko, A. V., Parris, K. D., Mosyak, L., Li, S., Handke, L. D., Hawkins, J. C., Elena, S., Matsuka, Y. V., & Anderson, A. S. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005908 · Cited by 26
Sujith, P. P., Mourya, B. S., Krishnamurthi, S., Meena, R. M., & Bharathi, P. A. L. (2013) · Chemosphere · doi:10.1016/j.chemosphere.2013.09.103 · Cited by 26
Thomsen, I. P., & Liu, G. Y. (2018) · JCI Insight · doi:10.1172/jci.insight.98216 · Cited by 27
Love, J. F., vanderSpek, J. C., & Murphy, J. R. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.7.2251-2258.2003 · Cited by 25
Yoo, D., Bagon, B. B., Valeriano, V. D., Oh, J. K., Kim, H., Cho, S., & Kang, D. (2017) · FEMS Microbiology Letters · doi:10.1093/femsle/fnx185 · Cited by 24
Intracellular accumulation of staphylopine impairs the fitness of Staphylococcus aureus cntE mutant
Chen, C., & Hooper, D. C. (2019) · FEBS Letters · doi:10.1002/1873-3468.13396 · Cited by 22
Grim, K. P., Radin, J. N., Solórzano, P. K. P., Morey, J. R., Frye, K. A., Ganio, K., Neville, S. L., McDevitt, C. A., & Kehl‐Fie, T. E. (2020) · Journal of Bacteriology · doi:10.1128/jb.00014-20 · Cited by 22
Two Vaccines for Staphylococcus aureus Induce a B-Cell-Mediated Immune Response
Dupont, C. D., Scully, I. L., Zimnisky, R. M., Monian, B., Rossitto, C. P., O'Connell, E. B., Jansen, K. U., Anderson, A. S., & Love, J. C. (2018) · mSphere · doi:10.1128/msphere.00217-18 · Cited by 21
Staphylococcus and the Healing Power of Pus
Russell, D. G. (2008) · Cell Host & Microbe · doi:10.1016/j.chom.2008.02.008 · Cited by 21
Solórzano, P. K. P., Bastille, T. S., Radin, J. N., & Kehl‐Fie, T. E. (2023) · mBio · doi:10.1128/mbio.03223-22 · Cited by 21
Coordinated adaptation of Staphylococcus aureus to calprotectin-dependent metal sequestration
Ruiz, V. M. R., Freiberg, J. A., Weiss, A., Green, E. R., Jobson, M.-E., Felton, E. A., Shaw, L. N., Chazin, W., & Skaar, E. P. (2024) · mBio · doi:10.1128/mbio.01389-24 · Cited by 19
Manganese in health and disease
Wang, Y., Li, J., Jing, Z., Wu, Y., Liu, J., & Han, S. (2025) · Nutrition Research Reviews · doi:10.1017/s0954422425100139 · Cited by 19
The roles of GpsB and DivIVA in Staphylococcus aureus growth and division
Sutton, J. A. F., Cooke, M., Tinajero-Trejo, M., Wacnik, K., Salamaga, B., Portman-Ross, C., Lund, V. A., Hobbs, J., & Foster, S. (2023) · bioRxiv · doi:10.3389/fmicb.2023.1241249 · Cited by 14
Self-citationLam, L. N., Wong, J. J., Chong, K. K. L., & Kline, K. A. (2020) · Infection and Immunity · doi:10.1128/iai.00058-20 · Cited by 18
Staphylococcus aureus metal acquisition in the mastitic mammary gland
Carlson, S. K., Erickson, D. L., & Wilson, E. (2020) · Microbial Pathogenesis · doi:10.1016/j.micpath.2020.104179 · Cited by 18
A Small-Molecule Modulator of Metal Homeostasis in Gram-Positive Pathogens
Juttukonda, L. J., Beavers, W. N., Unsihuay, D., Kim, K., Pishchany, G., Horning, K. J., Weiss, A., Al‐Tameemi, H., Boyd, J. M., Sulikowski, G. A., et al. (2020) · mBio · doi:10.1128/mbio.02555-20 · Cited by 17
The Bradyrhizobium japonicum Fur protein is an iron-responsive regulator in vivo
Yang, J., Sangwan, I., & O’Brian, M. R. (2006) · Molecular Genetics and Genomics · doi:10.1007/s00438-006-0162-4 · Cited by 17
Murine Calprotectin Coordinates Mn(II) at a Hexahistidine Site with Ca(II)-Dependent Affinity
Hadley, R. C., Gagnon, D. M., Ozarowski, A., Britt, R. D., & Nolan, E. M. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.9b00763 · Cited by 16
Host-imposed manganese starvation of invading pathogens: two routes to the same destination
Morey, J. R., McDevitt, C. A., & Kehl‐Fie, T. E. (2015) · BioMetals · doi:10.1007/s10534-015-9850-z · Cited by 16
Characterization of Staphylococcus aureus Responses to Spermine Stress
Yao, X., & Lu, C. (2014) · Current Microbiology · doi:10.1007/s00284-014-0603-y · Cited by 18
Specific of accumulation of manganese in organs and tissues of Hereford cattle
Нарожных, К. Н., Петухов, В. Л., Сысо, А. И., Коновалова, Т. В., Сергеевна, К. О., & Игоревна, С. О. (2024) · Brazilian Journal of Biology · doi:10.1590/1519-6984.282174 · Cited by 14
Gagnon, D. M., Hadley, R. C., Ozarowski, A., Nolan, E. M., & Britt, R. D. (2019) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.9b03633 · Cited by 14
Structure and Metal Binding Properties of Chlamydia trachomatis YtgA
Luo, Z., Neville, S. L., Campbell, R., Morey, J. R., Menon, S., Thomas, M., Eijkelkamp, B. A., Ween, M. P., Huston, W. M., Kobe, B., et al. (2019) · Journal of Bacteriology · doi:10.1128/jb.00580-19 · Cited by 14
Ferritin, an iron source in meat for Staphylococcus xylosus?
Vermassen, A., Talòn, R., & Léroy, S. (2016) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2016.03.005 · Cited by 15
Nanfara, M. T., Babu, V. M. P., Ghazy, M. A., & Sutton, M. D. (2016) · PLoS ONE · doi:10.1371/journal.pone.0163643 · Cited by 13
Singh, R. R., Ranaivoarisoa, T. O., Gupta, D. K., Bai, W., & Bose, A. (2020) · Applied and Environmental Microbiology · doi:10.1128/aem.01057-20 · Cited by 13
Manganese Transport, Trafficking and Function in Invertebrates
Jensen, A. N., & Jensen, L. T. (2014) · Royal Society of Chemistry eBooks · doi:10.1039/9781782622383-00001 · Cited by 14
Fang, Y., Wang, H., Liu, X., Rao, Y., Dedong, X., & Zhu, B. (2019) · PLoS ONE · doi:10.1371/journal.pone.0218844 · Cited by 11
Salazar, M. J., Machado, H., Dillon, N. A., Tsunemoto, H., Szubin, R., Dahesh, S., Pogliano, J., Sakoulas, G., Palsson, B. Ø., Nizet, V., et al. (2020) · mSystems · doi:10.1128/msystems.00828-19 · Cited by 13
Iron and Zinc Regulate Expression of a Putative ABC Metal Transporter in Corynebacterium diphtheriae
Peng, E. D., Oram, D. M., Battistel, M. D., Lyman, L. R., Freedberg, D. I., & Schmitt, M. P. (2018) · Journal of Bacteriology · doi:10.1128/jb.00051-18 · Cited by 11
Monteith, A. J., Miller, J. M., Beavers, W. N., Juttukonda, L. J., & Skaar, E. P. (2022) · Infection and Immunity · doi:10.1128/iai.00685-21 · Cited by 11
Mis-regulation of Zn and Mn homeostasis is a key phenotype of Cu stress in Streptococcus pyogenes
Hong, Y., Mackenzie, E. S., Firth, S. J., Bolton, J., Stewart, L. J., Waldron, K. J., & Djoko, K. Y. (2023) · Metallomics · doi:10.1093/mtomcs/mfad064 · Cited by 10
Novick, R. P. (2008) · Science · doi:10.1126/science.1154769 · Cited by 10
Chakraborty, D., Kumar, S. A., Sen, M., Apte, S. K., Das, S., Acharya, R., Das, T., Reddy, Α. V. R., Roychaudhury, S., Rajaram, H., et al. (2011) · Plant and Soil · doi:10.1007/s11104-010-0696-4 · Cited by 9
Analysis of the Manganese and MntR Regulon in Corynebacterium diphtheriae
Peng, E. D., Lyman, L. R., & Schmitt, M. P. (2021) · Journal of Bacteriology · doi:10.1128/jb.00274-21 · Cited by 9
Cellier, M. F. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.988866 · Cited by 9
Kuznetsova, A., Masrati, G., Vigonsky, E., Livnat‐Levanon, N., Rose, J., Grupper, M., Baloum, A., Yang, J. G., Rees, D. C., Ben‐Tal, N., et al. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101087 · Cited by 8
Aspartate tightens the anchoring of staphylococcal lipoproteins to the cytoplasmic membrane
Kumari, N., Götz, F., & Nguyen, M. (2017) · MicrobiologyOpen · doi:10.1002/mbo3.525 · Cited by 8
Metal Sequestration: An Important Contribution of Antimicrobial Peptides to Nutritional Immunity
Damo, S. M., & Kehl‐Fie, T. E. (2015) · Springer eBooks · doi:10.1007/978-3-319-24199-9_6 · Cited by 8
Manganese and Nutritional Immunity
Juttukonda, L. J., & Skaar, E. P. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802168-2.00031-2 · Cited by 9
Love, J. F., & Murphy, J. R. (2014) · ASM Press eBooks · doi:10.1128/9781555816513.ch59 · Cited by 8
Pathogenesis of Staphylococcus aureus in Humans
Lu, T., & DeLeo, F. R. (2015) · Wiley eBooks · doi:10.1002/9781118644843.ch39 · Cited by 8
Chen, Y., Moran, J. C., Campbell-Lee, S., & Horsburgh, M. J. (2021) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00569-21 · Cited by 7
Self-citationLiu, Y., Li, W., Wei, Y., Jiang, Y., & Tan, X. (2013) · Metallomics · doi:10.1039/c3mt00163f · Cited by 7
Lee, Y., Choi, K.-M., Mun, S. H., Yoo, J.-W., & Jung, J.-H. (2024) · PLoS ONE · doi:10.1371/journal.pone.0308246 · Cited by 6
An Aromatic Hydroxyamide Attenuates Multiresistant Staphylococcus aureus Toxin Expression
Vomacka, J., Korotkov, V. S., Bauer, B., Weinandy, F., Kunzmann, M. H., Krysiak, J. M., Baron, O., Böttcher, T., Lorenz‐Baath, K., & Sieber, S. A. (2016) · Chemistry - A European Journal · doi:10.1002/chem.201503981 · Cited by 7
Function analysis of two Mn(II) ion transporter genes (DR1709 and DR2523) in Deinococcus radiodurans
Shu, H., & Baoming, T. (2010) · AFRICAN JOURNAL OF BIOTECHNOLOGY · doi:10.5897/ajb2010.000-3098 · Cited by 6
Manganese: Uptake, Biological Function, and Role in Virulence
Papp‐Wallace, K. M., Moomaw, A. S., & Maguire, M. E. (2007) · Springer eBooks · doi:10.1007/7171_2006_080 · Cited by 6
Yu, W., Wang, L., Wang, M., Liu, S., Li, W., Wang, X., Li, X., Yu, S., Yao, D., Ma, J., et al. (2017) · Microbial Pathogenesis · doi:10.1016/j.micpath.2017.09.045 · Cited by 5
SSR42 is a novel regulator of cytolytic activity in Staphylococcus aureus
Jobson, M.-E., Tomlinson, B. R., Mustor, E. M., Felton, E. A., Weiss, A., Caswell, C. C., & Shaw, L. N. (2025) · mBio · doi:10.1128/mbio.00772-25 · Cited by 5
Staphylococcus aureus virulence factors synthesis is controlled by central metabolism
Zhu, Y. (2010) · Lincoln (University of Nebraska) · Cited by 4
Manzoor, S., Abbas, S., Zulfiqar, S., Wu, D., Wang, H., Li, W.-J., Arshad, M., & Ahmed, I. (2025) · Antonie van Leeuwenhoek · doi:10.1007/s10482-025-02132-6 · Cited by 3
Metal ion activation and DNA recognition by the Deinococcus radiodurans manganese sensor DR2539
Mota, C., Webster, M., Saïdi, M., Kapp, U., Zubieta, C., Giachin, G., Manso, J. A., & de Sanctis, D. (2024) · FEBS Journal · doi:10.1111/febs.17140 · Cited by 3
McFarlane, R. A., Radin, J. N., Mazgaj, R., Waldron, K. J., Lalaouna, D., & Kehl‐Fie, T. E. (2025) · mBio · doi:10.1128/mbio.01439-25 · Cited by 4
Čapek, J., Procházková, I., Matoušek, T., Hot, D., & Večerek, B. (2021) · mBio · doi:10.1128/mbio.01902-21 · Cited by 3
Metadata
- Authors
- Horsburgh, M. J., Wharton, S. J., Cox, A. G., Ingham, E., Peacock, S., & Foster, S. J.
- Affiliations
- University of Sheffield (GB)
- University of Leeds (GB)
- John Radcliffe Hospital (GB)
- Corresponding author
- Foster, Simon J.
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2002-05-23
- Volume
- 44
- Issue
- 5
- Pages
- 1269-1286
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- OpenAlex
- W2154476329
- Cited by
- 228
- References
- 65
- Citations by year
- 2026: 7 · 2025: 7 · 2024: 7 · 2023: 4 · 2022: 4 · 2021: 8 · 2020: 15 · 2019: 15 · 2018: 11 · 2017: 9 · 2016: 12 · 2015: 13 · 2014: 9 · 2013: 14 · 2012: 8
- FWCI
- 4.49
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Health Sciences › Medicine › Infectious Diseases › Antimicrobial Resistance in Staphylococcus
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Keywords
- MntR, PerR, Staphylococcus aureus, manganese uptake, MntH, oxidative stress resistance, fur, kata, ferritin, metal homeostasis, gene expression regulation, virulence
- MeSH terms
- Animals, Bacterial Proteins, Base Sequence, Endothelium, Vascular, Genes, Bacterial, Herbicides, Homeostasis, Humans, Manganese, Mice, Inbred BALB C, Molecular Sequence Data, Paraquat, Promoter Regions, Genetic, Recombinant Fusion Proteins, Repressor Proteins, Staphylococcus aureus, Superoxides, Transcription Factors, Gene Expression Regulation, Bacterial, Genes, Reporter, Regulon, Mice
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