Correction of the Iron Overload Defect in β-2-Microglobulin Knockout Mice by Lactoferrin Abolishes Their Increased Susceptibility to Tuberculosis

Schaible, Ulrich E.; Collins, Helen L.; Priem, Friedrich; Kaufmann, Stefan H.E.

doi:10.1084/jem.20020897

Cited by 198Tuberculosis Research and EpidemiologyIron Metabolism and DisordersImmune responses and vaccinations

Correction of the Iron Overload Defect in β-2-Microglobulin Knockout Mice by Lactoferrin Abolishes Their Increased Susceptibility to Tuberculosis

Open access

Schaible, Ulrich E., Collins, Helen L., Priem, Friedrich, Kaufmann, Stefan H.E.·2002·The Journal of Experimental Medicine

DOI 10.1084/jem.20020897PMC PMC2194267

Open this paper in CoChat — free account Open PDF

Abstract

As a resident of early endosomal phagosomes, Mycobacterium tuberculosis is connected to the iron uptake system of the host macrophage. β-2-microglobulin (β2m) knockout (KO) mice are more susceptible to tuberculosis than wild-type mice, which is generally taken as a proof for the role of major histocompatibility complex class I (MHC-I)–restricted CD8 T cells in protection against M. tuberculosis. However, β2m associates with a number of MHC-I–like proteins, including HFE. This protein regulates transferrin receptor mediated iron uptake and mutations in its gene cause hereditary iron overload (hemochromatosis). Accordingly, β2m-deficient mice suffer from tissue iron overload. Here, we show that modulating the extracellular iron pool in β2m–KO mice by lactoferrin treatment significantly reduces the burden of M. tuberculosis to numbers comparable to those observed in MHC class I–KO mice. In parallel, the generation of nitric oxide impaired in β2m–KO mice was rescued. Conversely, iron overload in the immunocompetent host exacerbated disease. Consistent with this, iron deprivation in infected resting macrophages was detrimental for intracellular mycobacteria. Our data establish: (a) defective iron metabolism explains the increased susceptibility of β2m-KO mice over MHC-I–KO mice, and (b) iron overload represents an exacerbating cofactor for tuberculosis.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1084/jem.20020897

Cites

30 of 30 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

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?

β2m-deficient mice develop greater M tuberculosis burden than WT mice, which can be reversed by treatment with lactoferrin.
“It was previously reported that β2m-deficient mice, which have liver iron overload and aberrant major histocompatibility complex type I expression, develop greater M tuberculosis burden that WT mice, which can be reversed by treatment with lactoferrin.19”
From Endogenous hepcidin and its agonist mediate resistance to selected infections by clearing non-transferrin-bound iron (2017) · cites this paper as [19]
Even with M. tuberculosis iron-acquisition factors, macrophage iron withholding effectively limits bacterial growth.
“Even with the expression of M. tuberculosis iron-acquisition factors, macrophage iron withholding effectively aids in limiting bacterial growth (Schaible et al., 2002).”
From The Impact of Dietary Transition Metals on Host-Bacterial Interactions (2018) · cites this paper as Schaible et al., 2002
Increased availability of iron promotes the growth of M. tuberculosis and exacerbates TB.
“It is well-established that increased availability of iron promotes the growth of M. tuberculosis and exacerbates TB (163–166).”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [163]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Major histocompatibility complex class I-restricted T cells are required for resistance to Mycobacterium tuberculosis infection.
Flynn, J. L., Goldstein, M. M., Triebold, K. J., Koller, B. H., & Bloom, B. R. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.24.12013 · Cited by 793 · see citing works
Lactoferrin: a general review.
Levay, P., & Viljoen, M. (1995) · PubMed · Cited by 645 · see citing works
The salicylate-derived mycobactin siderophores of Mycobacterium tuberculosis are essential for growth in macrophages
De Voss, J. J., Rutter, K., Schroeder, B. G., Su, H., Zhu, Y., & Barry, C. E. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.3.1252 · Cited by 532 · see citing works
Cytokine Activation Leads to Acidification and Increases Maturation of Mycobacterium avium -Containing Phagosomes in Murine Macrophages
Schaible, U. E., Sturgill-Koszycki, S., Schlesinger, P. H., & Russell, D. G. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.160.3.1290 · Cited by 402 · see citing works
Self-citation
Susceptibility of Mice Deficient in CD1D or TAP1 to Infection with Mycobacterium tuberculosis
Behar, S. M., Dascher, C. C., Grusby, M. J., Wang, C.-R., & Brenner, M. B. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.189.12.1973 · Cited by 374 · see citing works
Identification of committed NK cell progenitors in adult murine bone marrow
Rosmaraki, E. E., Douagi, I., Roth, C., Colucci, F., Cumano, A., & Santo, J. P. D. (2001) · European Journal of Immunology · doi:10.1002/1521-4141(200106)31:6 · Cited by 361 · see citing works
Relative contributions of distinct MHC class I-dependent cell populations in protection to tuberculosis infection in mice
Sousa, A. O., Mazzaccaro, R. J., Russell, R. G., Lee, F. K., Turner, O. C., Hong, S., Kaer, L. V., & Bloom, B. R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.8.4204 · Cited by 275 · see citing works
Iron Acquisition and Metabolism by Mycobacteria
Voss, J. J. D., Rutter, K., Schroeder, B. G., & Barry, C. E. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.15.4443-4451.1999 · Cited by 268 · see citing works
The Mycobacterium tuberculosis IdeR is a dual functional regulator that controls transcription of genes involved in iron acquisition, iron storage and survival in macrophages
Gold, B., Rodríguez, G. M., Marras, S. A. E., Pentecost, M., & Smith, I. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02684.x · Cited by 261 · see citing works
Lactoferrin: a multifunctional glycoprotein.
Vorland, L. H. (1999) · APMIS · doi:10.1111/j.1699-0463.1999.tb01499.x · Cited by 252 · see citing works
Gallium Disrupts Iron Metabolism of Mycobacteria Residing within Human Macrophages
Olakanmi, O., Britigan, B. E., & Schlesinger, L. S. (2000) · Infection and Immunity · doi:10.1128/iai.68.10.5619-5627.2000 · Cited by 220 · cited 1× · see citing works
“Furthermore, treatment of infected macrophages with Tf saturated with gallium, which substitutes for Fe without undergoing redox recycling, inhibits the intracellular growth of M. tuberculosis in vitro ( 25 ).”
Background
Exochelins of Mycobacterium tuberculosis remove iron from human iron-binding proteins and donate iron to mycobactins in the M. tuberculosis cell wall.
Gobin, J., & Horwitz, M. A. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.183.4.1527 · Cited by 208 · see citing works
Defective iron homeostasis in beta 2-microglobulin knockout mice recapitulates hereditary hemochromatosis in man.
Santos, M. M., Schilham, M. W., Rademakers, L. H. P. M., Marx, J. J. M., de Sousa, M. A. B., & Clevers, H. C. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.184.5.1975 · Cited by 195 · see citing works
beta2 knockout mice develop parenchymal iron overload: A putative role for class I genes of the major histocompatibility complex in iron metabolism.
Rothenberg, B. E., & Voland, J. R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.4.1529 · Cited by 194 · see citing works
Association of Pulmonary Tuberculosis with Increased Dietary Iron
Gangaidzo, I. T., Moyo, V. M., Mvundura, E., Aggrey, G., Murphree, N. L., Khumalo, H., Saungweme, T., Kasvosve, I., Gomo, Z. A. R., Rouault, T., et al. (2001) · The Journal of Infectious Diseases · doi:10.1086/323203 · Cited by 191 · see citing works
Iron overload in β2-microglobulin-deficient mice
DESOUSA, M., REIMAO, R., Lacerda, R., Hugo, P., Kaufmann, S. H. E., & Porto, G. (1994) · Immunology Letters · doi:10.1016/0165-2478(94)90094-9 · Cited by 172 · see citing works
Self-citation
Regulation of transferrin receptor expression and ferritin content in human mononuclear phagocytes. Coordinate upregulation by iron transferrin and downregulation by interferon gamma.
Byrd, T. F., & Horwitz, M. A. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116318 · Cited by 149 · see citing works
Iron and Mycobacterium tuberculosis infection
Lounis, N., Truffot-Pernot, C., Grosset, J., Gordeuk, V. R., & Boelaert, J. R. (2001) · Journal of Clinical Virology · doi:10.1016/s1386-6532(00)00136-0 · Cited by 142 · see citing works
Correlation analysis between frequencies of circulating antigen-specific IgG-bearing memory B cells and serum titers of antigen-specific IgG
Leyendeckers, H., Odendahl, M., Löhndorf, A., Irsch, J., Spangfort, M. D., Miltenyi, S., Hunzelmann, N., Assenmacher, M., Radbruch, A., & Schmitz, J. (1999) · European Journal of Immunology · doi:10.1002/(sici)1521-4141(199904)29:04 · Cited by 135 · see citing works
Attenuation of virulence in Mycobacterium tuberculosis expressing a constitutively active iron repressor
Manabe, Y. C., Saviola, B., Sun, L., Murphy, J. R., & Bishai, W. R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.22.12844 · Cited by 92 · see citing works
A pathway of costimulation that prevents anergy in CD28- T cells: B7-independent costimulation of CD1-restricted T cells.
Behar, S. M., Porcelli, S. A., Beckman, E. M., & Brenner, M. B. (1995) · The Journal of Experimental Medicine · doi:10.1084/jem.182.6.2007 · Cited by 85 · see citing works
Molecular aspects of iron absorption and HFE expression
Parkkila, S., Niemelä, O. J., Britton, R. S., Fleming, R. E., Waheed, A., Bacon, B. R., & Sly, W. S. (2001) · Gastroenterology · doi:10.1053/gast.2001.29617 · Cited by 78 · see citing works
A Novel Nonclassic β 2-Microglobulin–Restricted Mechanism Influencing Early Lymphocyte Accumulation and Subsequent Resistance to Tuberculosis in the Lung
D'Souza, C. D., Cooper, A. M., Frank, A. A., Ehlers, S., Turner, J., Bendelac, A. S., & Orme, I. M. (2000) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.23.2.4063 · Cited by 72 · see citing works
Iron Chelation Via Deferoxamine Exacerbates Experimental Salmonellosis Via Inhibition of the Nicotinamide Adenine Dinucleotide Phosphate Oxidase-Dependent Respiratory Burst
Collins, H. L., Kaufmann, S. H. E., & Schaible, U. E. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.168.7.3458 · Cited by 69 · see citing works
Self-citation
Iron-Overload Cardiomyopathy: Evidence for a Free Radical– Mediated Mechanism of Injury and Dysfunction in a Murine Model
Bartfay, W. J., & Bartfay, E. (2000) · Biological Research For Nursing · doi:10.1177/109980040000200106 · Cited by 66 · see citing works
Lactoferrin Peptide Increases the Survival of Candida albicans - Inoculated Mice by Upregulating Neutrophil and Macrophage Functions, Especially in Combination with Amphotericin B and Granulocyte-Macrophage Colony-Stimulating Factor
Tanida, T., Rao, F., Hamada, T., Ueta, E., & Osaki, T. (2001) · Infection and Immunity · doi:10.1128/iai.69.6.3883-3890.2001 · Cited by 50 · see citing works
Why intracellular parasitism need not be a degrading experience for Mycobacterium
Russell, D. G., Sturgill-Koszycki, S., Vanheyningen, T. K., Collins, H., & Schaible, U. E. (1997) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.1997.0114 · Cited by 46 · see citing works
Self-citation
Pumping iron: the strange partnership of the hemochromatosis protein, a class I MHC homolog, with the transferrin receptor
Enns, C. A. (2001) · Traffic · doi:10.1034/j.1600-0854.2001.020303.x · Cited by 45 · see citing works
HFE—A Novel Nonclassical Class I Molecule that Is Involved in Iron Metabolism
Ehrlich, R. L., & Lemonnier, F. A. (2000) · Immunity · doi:10.1016/s1074-7613(00)00058-3 · Cited by 33 · see citing works
Chapter 7: Modulation of Murine Macrophage Behavior in Vivo and in Vitro
Bancroft, G. J., Collins, H., Sigola, L. B., & Cross, C. E. (1995) · Methods in cell biology · doi:10.1016/s0091-679x(08)61849-x · Cited by 16 · see citing works
Self-citation

Flagged first, then by citations

Sorted by citations

IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin
Nemeth, E., Rivera, S., Gabayan, V., Keller, C., Taudorf, S., Pedersen, B. K., & Ganz, T. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200420945 · Cited by 2,650 · see citing works
Nutritional immunity: transition metals at the pathogen–host interface
Hood, M. I., & Skaar, E. P. (2012) · Nature Reviews Microbiology · doi:10.1038/nrmicro2836 · Cited by 1,535 · see citing works
Systemic Iron Homeostasis
Ganz, T. (2013) · Physiological Reviews · doi:10.1152/physrev.00008.2013 · Cited by 1,122 · see citing works
Macrophage defense mechanisms against intracellular bacteria
Weiss, G., & Schaible, U. E. (2015) · Immunological Reviews · doi:10.1111/imr.12266 · Cited by 989 · see citing works
Self-citation
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
Self-citation
Lactoferrin: structure, function and applications
González‐Chávez, S. A., Arévalo‐Gallegos, S., & Rascón-Cruz, Q. (2008) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2008.07.020 · Cited by 759 · see citing works
Hepcidin and the iron-infection axis
Drakesmith, H., & Prentice, A. M. (2012) · Science · doi:10.1126/science.1224577 · Cited by 686 · see citing works
I mmunity to T uberculosis
North, R. J., & Jung, Y. (2004) · Annual Review of Immunology · doi:10.1146/annurev.immunol.22.012703.104635 · Cited by 677 · see citing works
A major role for ferroptosis in Mycobacterium tuberculosis –induced cell death and tissue necrosis
Amaral, E. P., Costa, D. L., Namasivayam, S., Riteau, N., Kamenyeva, O., Mittereder, L., Mayer-Barber, K. D., Andrade, B. B., & Sher, A. (2019) · Journal of Experimental Medicine · doi:10.1084/jem.20181776 · Cited by 464 · see citing works
Lactoferrin a multiple bioactive protein: an overview
García-Montoya, I. A., Cendón, T. S., Arévalo-Gallegos, S., & Rascón-Cruz, Q. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.06.018 · Cited by 473 · see citing works
Vaccines against Tuberculosis: Where Are We and Where Do We Need to Go?
Ottenhoff, T. H. M., & Kaufmann, S. H. E. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002607 · Cited by 455 · see citing works
Self-citation
CELL BIOLOGY OF MYCOBACTERIUM TUBERCULOSIS PHAGOSOME
Vergne, I., Chua, J., Singh, S., & Deretic, V. P. (2004) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.20.010403.114015 · Cited by 440 · see citing works
Elemental Analysis of Mycobacterium avium -, Mycobacterium tuberculosis -, and Mycobacterium smegmatis -Containing Phagosomes Indicates Pathogen-Induced Microenvironments within the Host Cell’s Endosomal System
Wagner, D., Maser, J. M., Lai, B. C. H., Cai, Z., Barry, C. E., zu Bentrup, K. H., Russell, D. G., & Bermudez, L. E. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.3.1491 · Cited by 430 · see citing works
Lactoferrin
Legrand, D., Elass, E., Carpentier, M., & Mazurier, J. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5370-2 · Cited by 421 · see citing works
Sexual Inequality in Tuberculosis
Neyrolles, O., & Quintana‐Murci, L. (2009) · PLoS Medicine · doi:10.1371/journal.pmed.1000199 · Cited by 420 · see citing works
Impact of vitamin D on immune function: lessons learned from genome-wide analysis
Chun, R. F., Liu, P. T., Modlin, R. L., Adams, J. S., & Hewison, M. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00151 · Cited by 403 · 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 Sequestration and Anemia of Inflammation
Ganz, T., & Nemeth, E. (2009) · Seminars in Hematology · doi:10.1053/j.seminhematol.2009.06.001 · Cited by 361 · see citing works
Suppression of iron-regulatory hepcidin by vitamin D
Bacchetta, J., Zaritsky, J. J., Sea, J. L., Chun, R. F., Lisse, T. S., Zavala, K., Nayak, A., Wesseling-Perry, K., Westerman, M., Hollis, B. W., et al. (2014) · Journal of the American Society of Nephrology · doi:10.1681/asn.2013040355 · Cited by 350 · see citing works
Life and death in the granuloma: immunopathology of tuberculosis
Saunders, B. M., & Britton, W. J. (2007) · Immunology and Cell Biology · doi:10.1038/sj.icb.7100027 · Cited by 336 · see citing works
Rediscovering Beta-2 Microglobulin As a Biomarker across the Spectrum of Kidney Diseases
Argyropoulos, C., Chen, S. S., Ng, Y., Roumelioti, M., Shaffi, S. K., Singh, P., & Tzamaloukas, A. H. (2017) · Frontiers in Medicine · doi:10.3389/fmed.2017.00073 · Cited by 313 · see citing works
Mycobacterium tuberculosis inhibition of phagolysosome biogenesis and autophagy as a host defence mechanism
Deretic, V. P., Singh, S., Master, S. S., Harris, J., Roberts, E. A., Kyei, G. B., Davis, A., Haro, S. A. D., Naylor, J., Lee, H.-H., et al. (2006) · Cellular Microbiology · doi:10.1111/j.1462-5822.2006.00705.x · Cited by 306 · see citing works
Iron in innate immunity: starve the invaders
Ganz, T. (2009) · Current Opinion in Immunology · doi:10.1016/j.coi.2009.01.011 · Cited by 284 · see citing works
Cytotoxic and Proinflammatory CD8 + T Lymphocytes Promote Development of Vulnerable Atherosclerotic Plaques in ApoE-Deficient Mice
Kyaw, T. S., Winship, A., Tay, C., Kanellakis, P., Hosseini, H., Cao, A. H., Li, P., Tipping, P. G., Bobik, A., & Toh, B. (2013) · Circulation · doi:10.1161/circulationaha.112.001347 · Cited by 288 · see citing works
Differential expression of iron-, carbon-, and oxygen-responsive mycobacterial genes in the lungs of chronically infected mice and tuberculosis patients
Timm, J., Post, F. A., Bekker, L., Walther, G. B., Wainwright, H., Manganelli, R., Chan, W.-T., Tsenova, L., Gold, B., Smith, I., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2436197100 · Cited by 278 · see citing works
A Critical Role for CD8 T Cells in a Nonhuman Primate Model of Tuberculosis
Chen, C. Y., Huang, D., Wang, R. C., Shen, L., Zeng, G., Yao, S., Shen, Y., Halliday, L. C., Fortman, J., McAllister, M. Μ., et al. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000392 · Cited by 279 · see citing works
Lessons from experimental Mycobacterium tuberculosis infections
Flynn, J. L. (2006) · Microbes and Infection · doi:10.1016/j.micinf.2005.10.033 · Cited by 270 · see citing works
Mycobacterium tuberculosisPhagosome Maturation Arrest: Mycobacterial Phosphatidylinositol Analog Phosphatidylinositol Mannoside Stimulates Early Endosomal Fusion
Vergne, I., Fratti, R. A., Hill, P. J., Chua, J., Belisle, J. T., & Deretic, V. P. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-05-0307 · Cited by 260 · see citing works
Iron metabolism and the innate immune response to infection
Johnson, E. E., & Wessling-Resnick, M. (2012) · Microbes and Infection · doi:10.1016/j.micinf.2011.10.001 · Cited by 253 · see citing works
“tuberculosis infection that could be reversed with iron chelation using lactoferrin [16].”
Background
A precious metal: Iron, an essential nutrient for all cells
Cairo, G., Bernuzzi, F., & Recalcati, S. (2006) · Genes & Nutrition · doi:10.1007/bf02829934 · Cited by 252 · see citing works
CD8 T cells and Mycobacterium tuberculosis infection
Lin, P. L., & Flynn, J. L. (2015) · Seminars in Immunopathology · doi:10.1007/s00281-015-0490-8 · Cited by 244 · see citing works
Candidate biomarkers for discrimination between infection and disease caused by Mycobacterium tuberculosis
Jacobsen, M., Repsilber, D., Gutschmidt, A., Neher, A., Feldmann, K., Mollenkopf, H., Ziegler, A., & Kaufmann, S. H. E. (2007) · Journal of Molecular Medicine · doi:10.1007/s00109-007-0157-6 · Cited by 239 · see citing works
Self-citation
Mycobacteria, metals, and the macrophage
Neyrolles, O., Wolschendorf, F., Mitra, A., & Niederweis, M. (2015) · Immunological Reviews · doi:10.1111/imr.12265 · Cited by 217 · see citing works
The Effect of the Host’s Iron Status on Tuberculosis
Boelaert, J. R., Vandecasteele, S. J., Appelberg, R., & Gordeuk, V. R. (2007) · The Journal of Infectious Diseases · doi:10.1086/518040 · Cited by 217 · see citing works
Ferroptosis as an emerging target in inflammatory diseases
Mao, H., Zhao, Y., Li, H., & Lei, L. (2020) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2020.04.001 · Cited by 200 · see citing works
Expression analysis of the acute phase response in channel catfish (Ictalurus punctatus) after infection with a Gram-negative bacterium
Peatman, E., Baoprasertkul, P., Terhune, J. S., Xu, P., Nandi, S., Kucuktas, H., Li, P., Wang, S., Somridhivej, B., Dunham, R. A., et al. (2007) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2007.03.003 · Cited by 199 · see citing works
The Impact of Dietary Transition Metals on Host-Bacterial Interactions
Lopez, C. A., & Skaar, E. P. (2018) · Cell Host & Microbe · doi:10.1016/j.chom.2018.05.008 · Cited by 190 · see citing works
“High levels of Akkermansia muciniphila, a member of the Verrucomicrobia, are associated with low inflammation and normal lipid and carbohydrate metabolism (Dao et al., 2016; Schneeberger et al., 2015), while high abundance of the Enterobacteriaceae is associated with intestinal dysbiosis.”
Lactoferrin, a key molecule in immune and inflammatory processes 1 This article is part of Special Issue entitled Lactoferrin and has undergone the Journal’s usual peer review process.
Legrand, D. (2012) · Biochemistry and Cell Biology · doi:10.1139/o11-056 · Cited by 193 · see citing works
Wolbachia Interferes with Ferritin Expression and Iron Metabolism in Insects
Kremer, N., Voronin, D., Charif, D., Mavingui, P., Mollereau, B., & Vavre, F. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000630 · Cited by 191 · see citing works
Alternative activation deprives macrophages of a coordinated defense program to Mycobacterium tuberculosis
Kahnert, A., Seiler, P. J., Stein, M., Bandermann, S., Hahnke, K., Mollenkopf, H., & Kaufmann, S. H. E. (2006) · European Journal of Immunology · doi:10.1002/eji.200535496 · Cited by 187 · see citing works
Self-citation
The Implication and Significance of Beta 2 Microglobulin
Li, L., Dong, M., & Wang, X.-G. (2016) · Chinese Medical Journal · doi:10.4103/0366-6999.176084 · Cited by 187 · see citing works
Mycobacterium tuberculosis-Specific CD8+ T Cells and Their Role in Immunity
Woodworth, J. S., & Behar, S. M. (2006) · Critical Reviews in Immunology · doi:10.1615/critrevimmunol.v26.i4.30 · Cited by 175 · see citing works
Ferritin: An Inflammatory Player Keeping Iron at the Core of Pathogen-Host Interactions
Moreira, A. C., Mesquita, G., & Gomes, M. S. (2020) · Microorganisms · doi:10.3390/microorganisms8040589 · Cited by 166 · see citing works
Iron Deficiency and Anemia Predict Mortality in Patients with Tuberculosis3
Isanaka, S., Mugusi, F. M., Urassa, W. K., Willett, W. C., Bosch, R. J., Villamor, E., Spiegelman, D. L., Duggan, C., & Fawzi, W. W. (2011) · Journal of Nutrition · doi:10.3945/jn.111.144287 · Cited by 164 · see citing works
The ESAT-6 Protein of Mycobacterium tuberculosis Interacts with Beta-2-Microglobulin (β2M) Affecting Antigen Presentation Function of Macrophage
Sreejit, G., Ahmed, A., Parveen, N., Jha, V., Valluri, V. L., Ghosh, S., & Mukhopadhyay, S. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004446 · Cited by 165 · see citing works
Autocrine IL-10 Induces Hallmarks of Alternative Activation in Macrophages and Suppresses Antituberculosis Effector Mechanisms without Compromising T Cell Immunity
Schreiber, T., Ehlers, S., Heitmann, L., Rausch, A., Mages, J., Murray, P. J., Lang, R., & Hölscher, C. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0803567 · Cited by 161 · see citing works
Immune cell interactions in tuberculosis
Flynn, J. L., & Chan, J. (2022) · Cell · doi:10.1016/j.cell.2022.10.025 · Cited by 157 · see citing works
Lactoferrin: Role in iron homeostasis and host defense against microbial infection
Ward, P. P., & Conneely, O. M. (2004) · BioMetals · doi:10.1023/b:biom.0000027693.60932.26 · Cited by 149 · see citing works
Endogenous hepcidin and its agonist mediate resistance to selected infections by clearing non-transferrin-bound iron
Stefanova, D., Raychev, A., Arezes, J., Ruchala, P., Gabayan, V., Skurnik, M., Dillon, B. J., Horwitz, M. A., Ganz, T., Bulut, Y., et al. (2017) · Blood · doi:10.1182/blood-2017-03-772715 · Cited by 145 · see citing works
Control of iron metabolism in Mycobacterium tuberculosis
Rodríguez, G. M. (2006) · Trends in Microbiology · doi:10.1016/j.tim.2006.05.006 · Cited by 148 · see citing works
Hepcidin—A Peptide Hormone at the Interface of Innate Immunity and Iron Metabolism
Ganz, T. (2006) · Springer eBooks · doi:10.1007/3-540-29916-5_7 · Cited by 146 · see citing works
Iron Homeostasis in Mycobacterium tuberculosis: Mechanistic Insights into Siderophore-Mediated Iron Uptake
Sritharan, M. (2016) · Journal of Bacteriology · doi:10.1128/jb.00359-16 · Cited by 133 · see citing works
CD8+ T Cells in Tuberculosis
Lazarevic, V., & Flynn, J. L. (2002) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.2204027 · Cited by 129 · see citing works
Mycobacterium's arrest of phagosome maturation in macrophages requires Rab5 activity and accessibility to iron.
Kelley, V. A., & Schorey, J. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-12-0780 · Cited by 145 · see citing works
Heme Uptake and Utilization by Gram-Negative Bacterial Pathogens
Richard, K. L., Kelley, B. R., & Johnson, J. G. (2019) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2019.00081 · Cited by 120 · see citing works
Interactions of lactoferrin with cells involved in immune functionThis paper is one of a selection of papers published in this Special Issue, entitled 7th International Conference on Lactoferrin: Structure, Function, and Applications, and has undergone the Journal's usual peer review process.
Legrand, D., Elass, E., Carpentier, M., & Mazurier, J. (2006) · Biochemistry and Cell Biology · doi:10.1139/o06-045 · Cited by 121 · see citing works
Early T‐cell responses in tuberculosis immunity
Winslow, G. M., Cooper, A. M., Reiley, W. W., Chatterjee, M., & Woodland, D. L. (2008) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00693.x · Cited by 121 · see citing works
Human Lung Epithelial Cells Contain Mycobacterium tuberculosis in a Late Endosomal Vacuole and Are Efficiently Recognized by CD8+ T Cells
Harriff, M. J., Cansler, M. E., Toren, K. G., Canfield, E. T., Kwak, S., Gold, M. C., & Lewinsohn, D. M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0097515 · Cited by 116 · see citing works
Iron Metabolism and Infection
Ratledge, C. (2007) · Food and Nutrition Bulletin · doi:10.1177/15648265070284s405 · Cited by 118 · see citing works
Role of CD8+ T lymphocytes in control of Mycobacterium tuberculosis infection
Grotzke, J. E., & Lewinsohn, D. M. (2005) · Microbes and Infection · doi:10.1016/j.micinf.2005.03.001 · Cited by 110 · see citing works
Majority of B2M -Mutant and -Deficient Colorectal Carcinomas Achieve Clinical Benefit From Immune Checkpoint Inhibitor Therapy and Are Microsatellite Instability-High
Middha, S., Yaeger, R. D., Shia, J., Stadler, Z. K., King, S., Guercio, S., Paroder, V., Bates, ‬. D. B., Rana, S., Diaz, L. A., et al. (2019) · JCO Precision Oncology · doi:10.1200/po.18.00321 · Cited by 111 · see citing works
Role of iron in the pathogenesis of respiratory disease
Ali, M. K., Kim, R., Karim, R., Mayall, J., Martin, K. L., Shahandeh, A., Abbasian, F., Starkey, M. R., Loustaud-Ratti, V., Johnstone, D. M., et al. (2017) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.05.003 · Cited by 112 · see citing works
A tale of two lipids: Mycobacterium tuberculosis phagosome maturation arrest
Chua, J. (2004) · Current Opinion in Microbiology · doi:10.1016/j.mib.2003.12.011 · Cited by 110 · see citing works
A nutritive view on the host–pathogen interplay
Schaible, U. E., & Kaufmann, S. H. E. (2005) · Trends in Microbiology · doi:10.1016/j.tim.2005.06.009 · Cited by 106 · see citing works
Self-citation
Iron and infection: effects of host iron status and the iron-regulatory genes haptoglobin and NRAMP1 (SLC11A1) on host–pathogen interactions in tuberculosis and HIV
McDermid, J. M., & Prentice, A. M. (2006) · Clinical Science · doi:10.1042/cs20050273 · Cited by 102 · see citing works
Tuberculosis in Africa: Learning from Pathogenesis for Biomarker Identification
Kaufmann, S. H. E., & Parida, S. K. (2008) · Cell Host & Microbe · doi:10.1016/j.chom.2008.08.002 · Cited by 98 · see citing works
Self-citation
Zinc excess increases cellular demand for iron and decreases tolerance to copper in Escherichia coli
Xu, Z., Wang, P., Wang, H., Yu, Z. H., Au-Yeung, H. Y., Hirayama, T., Sun, H., & Yan, A. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010023 · Cited by 91 · see citing works
Hereditary hemochromatosis results in decreased iron acquisition and growth byMycobacterium tuberculosiswithin human macrophages
Olakanmi, O., Schlesinger, L. S., & Britigan, B. E. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0606405 · Cited by 88 · see citing works
Heme Catabolism by Heme Oxygenase-1 Confers Host Resistance to Mycobacterium Infection
Silva-Gomes, S., Appelberg, R., Larsen, R., Soares, M. P., & Gomes, M. S. (2013) · Infection and Immunity · doi:10.1128/iai.00251-13 · Cited by 85 · see citing works
Mycobacteria–host interactions in human bronchiolar airway organoids
Iakobachvili, N., Leon‐Icaza, S. A., Knoops, K., Sachs, N., Mazères, S., Siméone, R., Peixoto, A., Bernard, C., Murris‐Espin, M., Mazières, J., et al. (2021) · Molecular Microbiology · doi:10.1111/mmi.14824 · Cited by 76 · see citing works
GeneFriends: An online co-expression analysis tool to identify novel gene targets for aging and complex diseases
van Dam, S., Cordeiro, R., Craig, T., van Dam, J., Wood, S. H., & de Magalhães, J. P. (2012) · BMC Genomics · doi:10.1186/1471-2164-13-535 · Cited by 72 · see citing works
The human innate immune protein calprotectin induces iron starvation responses in Pseudomonas aeruginosa
Zygiel, E. M., Nelson, C. E., Brewer, L. K., Oglesby-Sherrouse, A. G., & Nolan, E. M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006819 · Cited by 76 · see citing works
Host iron redistribution as a risk factor for incident tuberculosis in HIV infection: an 11-year retrospective cohort study
McDermid, J. M., Hennig, B. J., van der Sande, M., Hill, A. V., Whittle, H. C., Jaye, A., & Prentice, A. M. (2013) · BMC Infectious Diseases · doi:10.1186/1471-2334-13-48 · Cited by 75 · see citing works
Cytotoxic lymphocytes and atherosclerosis: significance, mechanisms and therapeutic challenges
Kyaw, T. S., Peter, K., Li, Y., Tipping, P. G., Toh, B., & Bobik, A. (2017) · British Journal of Pharmacology · doi:10.1111/bph.13845 · Cited by 73 · see citing works
Iron and iron chelating agents modulateMycobacterium tuberculosisgrowth and monocyte-macrophage viability and effector functions
Cronjé, L., Edmondson, N., Eisenach, K. D., & Bornman, L. (2005) · FEMS Immunology & Medical Microbiology · doi:10.1016/j.femsim.2005.02.007 · Cited by 72 · see citing works
New challenges in studying nutrition-disease interactions in the developing world
Prentice, A. M., Gershwin, M. E., Schaible, U. E., Keusch, G. T., Victora, C. G., & Gordon, J. I. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34034 · Cited by 73 · see citing works
Self-citation
Biomarkers for tuberculosis disease status and diagnosis
Doherty, M. T., Wallis, R. S., & Zumla, A. I. (2009) · Current Opinion in Pulmonary Medicine · doi:10.1097/mcp.0b013e328326f42c · Cited by 72 · see citing works
Iron Status Predicts Treatment Failure and Mortality in Tuberculosis Patients: A Prospective Cohort Study from Dar es Salaam, Tanzania
Isanaka, S., Aboud, S., Mugusi, F., Bosch, R. J., Willett, W. C., Spiegelman, D., Duggan, C., & Fawzi, W. W. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037350 · Cited by 67 · see citing works
CD4+ T Cell-Dependent IFN-γ Production by CD8+ Effector T Cells in Mycobacterium tuberculosis Infection
Bold, T. D., & Ernst, J. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1200994 · Cited by 67 · see citing works
The X-lectins: A new family with homology to the Xenopus laevis oocyte lectin XL-35
Lee, J. K., Baum, L. G., Moremen, K., & Pierce, M. (2004) · Glycoconjugate Journal · doi:10.1007/s10719-004-5534-6 · Cited by 56 · see citing works
Iron and Ferritin Modulate MHC Class I Expression and NK Cell Recognition
Sottile, R., Federico, G., Garofalo, C., Tallerico, R., Faniello, M. C., Quaresima, B., Cristiani, C. M., Sanzo, M. D., Cuda, G., Ventura, V., et al. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00224 · Cited by 62 · see citing works
Mycobacterium tuberculosis hijacks host TRIM21- and NCOA4-dependent ferritinophagy to enhance intracellular growth
Dai, Y., Zhu, C., Xiao, W., Huang, K., Wang, X., Shi, C., Lin, D., Zhang, H., Liu, X., Peng, B., et al. (2023) · Journal of Clinical Investigation · doi:10.1172/jci159941 · Cited by 63 · see citing works
Self-citation
Influence of oral lactoferrin on Mycobacterium tuberculosis induced immunopathology
Welsh, K. J., Hwang, S., Boyd, S., Kruzel, M. L., Hunter, R. L., & Actor, J. K. (2011) · Tuberculosis · doi:10.1016/j.tube.2011.10.019 · Cited by 58 · see citing works
Iron in intracellular infection: to provide or to deprive?
Silva-Gomes, S., Vale-Costa, S., Appelberg, R., & Gomes, M. S. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00096 · Cited by 51 · see citing works
Hepcidin, iron, and bacterial infection
Barton, J. C., & Acton, R. T. (2019) · Vitamins and hormones · doi:10.1016/bs.vh.2019.01.011 · Cited by 53 · see citing works
CD8+ T Cells Accumulate in the Lungs of Mycobacterium tuberculosis -Infected Kb−/−Db−/− Mice, But Provide Minimal Protection
Urdahl, K. B., Liggitt, D., & Bevan, M. J. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.4.1987 · Cited by 52 · see citing works
CD8+ T Cells Restrict Yersinia pseudotuberculosis Infection: Bypass of Anti-Phagocytosis by Targeting Antigen-Presenting Cells
Bergman, M. A., Loomis, W. P., Mecsas, J. C., Starnbach, M. N., & Isberg, R. R. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000573 · Cited by 51 · see citing works
The Nature of Extracellular Iron Influences Iron Acquisition by Mycobacterium tuberculosis Residing within Human Macrophages
Olakanmi, O., Schlesinger, L., Ahmed, A., & Britigan, B. (2004) · Infection and Immunity · doi:10.1128/iai.72.4.2022-2028.2004 · Cited by 48 · see citing works
The Role of Iron Metabolism in Lung Inflammation and Injury
Kim, J. (2012) · Journal of Allergy & Therapy · doi:10.4172/2155-6121.s4-004 · Cited by 46 · see citing works
Transgenic fish resistant to infectious diseases, their risk and prevention of escape into the environment and future candidate genes for disease transgene manipulation
Dunham, R. A. (2008) · Comparative Immunology Microbiology and Infectious Diseases · doi:10.1016/j.cimid.2007.11.006 · Cited by 46 · see citing works
Transferrin-mediated iron sequestration as a novel therapy for bacterial and fungal infections
Bruhn, K. W., & Spellberg, B. (2015) · Current Opinion in Microbiology · doi:10.1016/j.mib.2015.07.005 · Cited by 48 · see citing works
Nippostrongylus brasiliensis: Identification of intelectin-1 and -2 as Stat6-dependent genes expressed in lung and intestine during infection
Voehringer, D., Stanley, S. A., Cox, J. S., Completo, G. C. J., Lowary, T. L., & Locksley, R. M. (2007) · Experimental Parasitology · doi:10.1016/j.exppara.2007.02.015 · Cited by 45 · see citing works
Lactoferrin modulation of BCG-infected dendritic cell functions
Hwang, S., & Actor, J. K. (2009) · International Immunology · doi:10.1093/intimm/dxp084 · Cited by 44 · see citing works
Increased expression of host iron-binding proteins precedes iron accumulation and calcification of primary lung lesions in experimental tuberculosis in the guinea pig
Basaraba, R. J., Bielefeldt‐Ohmann, H., Eschelbach, E. K., Reisenhauer, C., Tolnay, A.-E., Taraba, L. C., Shanley, C. A., Smith, E. A., Bedwell, C. L., Chlipala, E. A., et al. (2007) · Tuberculosis · doi:10.1016/j.tube.2007.09.002 · Cited by 44 · see citing works
Iron homeostasis during anemia of inflammation: a prospective study of patients with tuberculosis
Cercamondi, C. I., Stoffel, N. U., Moretti, D., Zöller, T., Swinkels, D. W., Zeder, C., Mhimibra, F., Hella, J., Fenner, L., & Zimmermann, M. B. (2021) · Blood · doi:10.1182/blood.2020010562 · Cited by 43 · see citing works
Desferrioxamine Supports Metabolic Function in Primary Human Macrophages Infected With Mycobacterium tuberculosis
Phelan, J. J., McQuaid, K., Kenny, C., Gogan, K. M., Cox, D. J., Basdeo, S. A., O’Leary, S. M., Tazoll, S. C., Maoldomhnaigh, C. Ó., O’Sullivan, M. P., et al. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00836 · Cited by 41 · see citing works
Increased Serum Iron Levels and Infectious Complications after Liver Transplantation
Chow, J. K. L., Werner, B. G., Ruthazer, R., & Snydman, D. R. (2010) · Clinical Infectious Diseases · doi:10.1086/654802 · Cited by 43 · see citing works
Iron Supplementation Therapy, A Friend and Foe of Mycobacterial Infections?
Agoro, R., & Mura, C. (2019) · Pharmaceuticals · doi:10.3390/ph12020075 · Cited by 41 · see citing works
Increased Susceptibility to Mycobacterium avium in Hemochromatosis Protein HFE-Deficient Mice
Gomes-Pereira, S., Rodrigues, P. N., Appelberg, R., & Gomes, M. S. (2008) · Infection and Immunity · doi:10.1128/iai.00612-08 · Cited by 38 · see citing works
Trace metal elements: a bridge between host and intestinal microorganisms
Ma, Y., Fei, Y., Ding, S., Jiang, H., Fang, J. Q., & Liu, G. (2023) · Science China Life Sciences · doi:10.1007/s11427-022-2359-4 · Cited by 37 · see citing works

Brief Definitive Report Correction of the Iron Overload Defect in �-2-Microglobulin Knockout Mice by Lactoferrin Abolishes Their Increased Susceptibility
Tuberculosis, T., Schaible, U. E., Collins, H. L., Priem, F., & Kaufmann, S. H. E. (2013)
Self-citation
Defective iron homeostasis in beta 2-microglobulin knockout mice recapitulates hereditary hemochromatosis in man.
Santos, M. M., Schilham, M. W., Rademakers, L. H. P. M., Marx, J. J. M., de Sousa, M. A. B., & Clevers, H. C. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.184.5.1975 · Cited by 195 · see citing works
Defective iron homeostasis in β2-microglobulin knockout mice recapitulates hereditary hemochromatosis in man
Santos, M. M., Schilham, M. W., Rademakers, L. H. P. M., Marx, J. J. M., de Sousa, M. A. B., & Clevers, H. C. (1997) · Immunology Letters · doi:10.1016/s0165-2478(97)85951-2 · Cited by 20 · see citing works
Adaptive Response of Iron Absorption to Anemia, Increased Erythropoiesis, Iron Deficiency, and Iron Loading in β2-Microglobulin Knockout Mice
Santos, M. M., Clevers, H. C., de Sousa, M. A. B., & Marx, J. J. M. (1998) · Blood · doi:10.1182/blood.v91.8.3059.3059_3059_3065 · Cited by 42 · see citing works
Iron overload in β2-microglobulin-deficient mice
DESOUSA, M., REIMAO, R., Lacerda, R., Hugo, P., Kaufmann, S. H. E., & Porto, G. (1994) · Immunology Letters · doi:10.1016/0165-2478(94)90094-9 · Cited by 172 · see citing works
Self-citation

Authors: Schaible, U. E., Collins, H. L., Priem, F., & Kaufmann, S. H. E.
Affiliations: Max Planck Society (DE)
Humboldt-Universität zu Berlin (DE)
Corresponding author: Priem, Friedrich
ORCID: Schaible, Ulrich E.
Collins, Helen L.
Kaufmann, Stefan H.E.
Venue: The Journal of Experimental Medicine
Publisher: Rockefeller University Press
Published: 2002-11-25
Volume: 196
Issue: 11
Pages: 1507-1513
ISSN: 0022-1007 (ISSN-L)
1540-9538
DOI: 10.1084/jem.20020897
PMC: PMC2194267
OpenAlex: W1990564189
Cited by: 198
References: 30
Citations by year: 2026: 3 · 2025: 5 · 2024: 1 · 2023: 8 · 2022: 6 · 2021: 9 · 2020: 6 · 2019: 13 · 2018: 4 · 2017: 10 · 2016: 6 · 2015: 9 · 2014: 8 · 2013: 10 · 2012: 10
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: The Journal of Experimental Medicine (publishedVersion)
PubMed Central (publishedVersion, cc-by-nc-sa)
PubMed (publishedVersion)
LSHTM Research Online (London School of Hygiene and Tropical Medicine) (acceptedVersion)
Research Portal (King's College London) (submittedVersion)
Topics: Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Life Sciences › Immunology and Microbiology › Immunology › Immune responses and vaccinations
Keywords: beta2-microglobulin, lactoferrin, tuberculosis susceptibility, Mycobacterium tuberculosis, iron overload, hemochromatosis, HFE gene, MHC class I, CD8+ T cells, macrophages, nitric oxide, iron metabolism, phagosome, iron starvation
MeSH terms: Hemochromatosis Protein, Animals, beta 2-Microglobulin, Disease Susceptibility, Interferon-gamma, Lactoferrin, Macrophages, Membrane Proteins, Mycobacterium tuberculosis, Nitric Oxide, Receptors, Transferrin, Tuberculosis, Histocompatibility Antigens Class I, Mice, Knockout, Iron Overload, 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

Correction of the Iron Overload Defect in β-2-Microglobulin Knockout Mice by Lactoferrin Abolishes Their Increased Susceptibility to Tuberculosis

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks