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Mycobacterial P1-Type ATPases Mediate Resistance to Zinc Poisoning in Human Macrophages
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Mycobacterium tuberculosis thrives within macrophages by residing in phagosomes and preventing them from maturing and fusing with lysosomes. A parallel transcriptional survey of intracellular mycobacteria and their host macrophages revealed signatures of heavy metal poisoning. In particular, mycobacterial genes encoding heavy metal efflux P-type ATPases CtpC, CtpG, and CtpV, and host cell metallothioneins and zinc exporter ZnT1, were induced during infection. Consistent with this pattern of gene modulation, we observed a burst of free zinc inside macrophages, and intraphagosomal zinc accumulation within a few hours postinfection. Zinc exposure led to rapid CtpC induction, and ctpC deficiency caused zinc retention within the mycobacterial cytoplasm, leading to impaired intracellular growth of the bacilli. Thus, the use of P(1)-type ATPases represents a M. tuberculosis strategy to neutralize the toxic effects of zinc in macrophages. We propose that heavy metal toxicity and its counteraction might represent yet another chapter in the host-microbe arms race.
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“Loss of Zn detoxification machinery in several bacterial pathogens, including Group A and B streptococci 166 , M. tuberculosis and S. pneumoniae , results in decreased intracellular survival 167-170 or in vivo survival in mouse models of infection 169 .”
From Nutritional immunity: the battle for nutrient metals at the host–pathogen interface (2022) · cites this paper as [167]
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“As with copper, M. tuberculosis express p-type ATPase to promote zinc efflux and to resist metal intoxication (239, 242).”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [242]
In the citing paper
“Transcriptional profiling of M. tuberculosis in human macrophages identified signs of metal intoxication in bacteria and in the host, revealing a burst of free zinc in macrophages and intraphagosomal zinc accumulation (18).”
From Transition Metals and Virulence in Bacteria (2016) · cites this paper as [18]
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Cites
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
Cole, S. T., Brosch, R., Parkhill, J., Garnier, T., Churcher, C., Harris, D., Gordon, S. V., Eiglmeier, K., Gas, S., Barry, C. E., et al. (1998) · Nature · doi:10.1038/31159 · Cited by 7,847
Exaptation—a missing term in the science of form
Gould, S. J., & Vrba, E. S. (1982) · Paleobiology · doi:10.1017/s0094837300004310 · Cited by 5,136
The Essential Toxin: Impact of Zinc on Human Health
Plum, L. M., Rink, L., & Haase, H. (2010) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph7041342 · Cited by 1,577
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
Synthetic fluorescent sensors for studying the cell biology of metals
Domaille, D. W., Que, E. L., & Chang, C. J. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.69 · Cited by 1,085
Armstrong, J. A., & Hart, P. D. (1971) · The Journal of Experimental Medicine · doi:10.1084/jem.134.3.713 · Cited by 991
Regulation of metallothionein gene expression by oxidative stress and metal ions
Andrews, G. K. (2000) · Biochemical Pharmacology · doi:10.1016/s0006-2952(99)00301-9 · Cited by 834
Mammalian Zinc Transporters: Nutritional and Physiologic Regulation
Lichten, L. A., & Cousins, R. J. (2009) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-033009-083312 · Cited by 749
Nutritional immunity beyond iron: a role for manganese and zinc
Kehl-Fie, T. E., & Skaar, E. P. (2010) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2009.11.008 · Cited by 634
Zinc is a novel intracellular second messenger
Yamasaki, S., Sakata-Sogawa, K., Hasegawa, A., Suzuki, T., Kabu, K., Sato, E., Kurosaki, T., Yamashita, S., Tokunaga, M., Nishida, K., et al. (2007) · Journal of Cell Biology · doi:10.1083/jcb.200702081 · Cited by 592
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Weiss, G., & Schaible, U. E. (2015) · Immunological Reviews · doi:10.1111/imr.12266 · Cited by 989
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Read, S. A., Obeid, S., Ahlenstiel, C., & Ahlenstiel, G. (2019) · Advances in Nutrition · doi:10.1093/advances/nmz013 · Cited by 801
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Forrellad, M. A., Klepp, L. I., Gioffré, A., y García, J. S., Morbidoni, H. R., Santangelo, M. D. L. P., Cataldi, A. A., & Bigi, F. (2013) · Virulence · doi:10.4161/viru.22329 · Cited by 676
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Lin, P.-H., Sermersheim, M., Li, H., Lee, P. H. U., Steinberg, S. M., & Ma, J. (2017) · Nutrients · doi:10.3390/nu10010016 · Cited by 643
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Russell, D. G., Huang, L., & VanderVen, B. C. (2019) · Nature reviews. Immunology · doi:10.1038/s41577-019-0124-9 · Cited by 470
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Palmer, L. D., & Skaar, E. P. (2016) · Annual Review of Genetics · doi:10.1146/annurev-genet-120215-035146 · Cited by 449
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Chen, B., Yu, P., Chan, W. N., Xie, F., Zhang, Y., Liang, L., Leung, K. T., Lo, K. W., Yu, J., Tse, G. M. K., et al. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01679-y · Cited by 420
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Sweet, M. J., Ramnath, D., Singhal, A., & Kapétanovic, R. (2024) · Nature reviews. Immunology · doi:10.1038/s41577-024-01080-y · Cited by 164
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Focarelli, F., Giachino, A., & Waldron, K. J. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010617 · Cited by 97
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Healy, C. M., Muñoz‐Wolf, N., Strydom, J., Faherty, L., Williams, N. C., Kenny, S., Donnelly, S. C., & Cloonan, S. M. (2021) · Respiratory Research · doi:10.1186/s12931-021-01722-y · Cited by 90
Gaddy, J. A., Radin, J. N., Loh, J. T., Piazuelo, M. B., Kehl-Fie, T. E., Delgado, A. G., Ilca, F. T., Peek, R. M., Cover, T. L., Chazin, W. J., et al. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004450 · Cited by 87
Harris, N. C., Sato, M., Herman, N. A., Twigg, F. F., Cai, W., Liu, J., Zhu, X., Downey, J., Khalaf, R., Martin, J., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1705016114 · Cited by 87
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Leblanc, C., Prudhomme, T., Tabouret, G., Ray, A. A., Burbaud, S., Cabantous, S., Mourey, L., Guilhot, C., & Chalut, C. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1003097 · Cited by 86
Salina, E. G., Waddell, S. J., Hoffmann, N. A., Rosenkrands, I., Butcher, P. D., & Kaprelyants, A. S. (2014) · Open Biology · doi:10.1098/rsob.140106 · Cited by 85
Self-citationBettencourt, P., Marion, S., Pires, D., Santos, L. F., Lastrucci, C., Carmo, N., Blake, J., Benes, V., Griffiths, G., Neyrolles, O., et al. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00019 · Cited by 84
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Rosenzweig, A. C., & ARGÜELLO, J. M. (2012) · Current topics in membranes · doi:10.1016/b978-0-12-394390-3.00005-7 · Cited by 71
Vignesh, K. S., & Deepe, G. S. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.02.020 · Cited by 74
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Honsa, E. S., Johnson, M. D. L., & Rosch, J. W. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00092 · Cited by 71
Haeili, M., Moore, C. V., Davis, C. J. C., Cochran, J. B., Shah, S., Shrestha, T. B., Zhang, Y., Bossmann, S. H., Benjamin, W. H., Kutsch, O., et al. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02316-13 · Cited by 70
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Crawford, A., Lehtovirta‐Morley, L. E., Alamir, O., Niemiec, M. J., Alawfi, B. S., Alsarraf, M., Skrahina, V., Costa, A. C. B. P., Anderson, A., Yellagunda, S., et al. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007013 · Cited by 69
Ellis, T., Chiappi, M., García‐Trenco, A., Al‐Ejji, M., Sarkar, S., Georgiou, T. K., Shaffer, M. S. P., Tetley, T. D., Schwander, S., Ryan, M. P., et al. (2018) · ACS Nano · doi:10.1021/acsnano.7b08264 · Cited by 68
Stocks, C. J., Phan, M., Achard, M. E. S., Nhu, N. T. K., Condon, N. D., Gawthorne, J. A., Lo, A. W. H., Peters, K. M., McEwan, A. G., Kapétanovic, R., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1820870116 · Cited by 66
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Sanson, M. A., Makthal, N., Flores, A. R., Olsen, R. J., Musser, J. M., & Kumaraswami, M. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku1304 · Cited by 60
Chandrangsu, P., & Helmann, J. D. (2016) · PLoS Genetics · doi:10.1371/journal.pgen.1006515 · Cited by 62
Raimunda, D., Long, J. E., Padilla‐Benavides, T., Sassetti, C. M., & ARGÜELLO, J. M. (2013) · Molecular Microbiology · doi:10.1111/mmi.12454 · Cited by 59
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Metadata
- Authors
- Botella, H., Peyron, P., Levillain, F., Poincloux, R., Poquet, Y., Brandli, I., Wang, C., Tailleux, L., Tilleul, S., Charrière, G. M., Waddell, S. J., Foti, M., Lugo-Villarino, G., Gao, Q., Maridonneau-Parini, I., Butcher, P. D., Castagnoli, P. R., Gicquel, B., de Chastellier, C., & Neyrolles, O.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Institut Pasteur (FR)
- Brighton and Sussex Medical School (GB)
- University of Milano-Bicocca (IT)
- Shanghai Medical College of Fudan University (CN)
- St George's, University of London (GB)
- Singapore Immunology Network (SG)
- Corresponding author
- Neyrolles, Olivier
- ORCID
- Venue
- Cell Host & Microbe
- Publisher
- Elsevier BV
- Published
- 2011-09
- Volume
- 10
- Issue
- 3
- Pages
- 248-259
- ISSN
- 1931-3128 (ISSN-L)
- PMC
- PMC3221041
- OpenAlex
- W2128702173
- Cited by
- 381
- References
- 48
- Citations by year
- 2026: 23 · 2025: 20 · 2024: 32 · 2023: 21 · 2022: 27 · 2021: 41 · 2020: 30 · 2019: 32 · 2018: 23 · 2017: 27 · 2016: 19 · 2015: 23 · 2014: 23 · 2013: 21 · 2012: 17
- FWCI
- 13.38
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Cell Host & Microbe (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Sussex Research Online (University of Sussex) (submittedVersion, cc-by)
- HAL (submittedVersion)
- HAL AMU (submittedVersion)
- BOA (University of Milano-Bicocca) (submittedVersion)
- Figshare (submittedVersion, cc-by)
- Funders
- Wellcome Trust (086547)
- Topics
- Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Health Sciences › Medicine › Epidemiology › Mycobacterium research and diagnosis
- Keywords
- Mycobacterium tuberculosis, zinc efflux, zinc toxicity, metallothionein, ZnT1, phagosome maturation, intracellular bacterial growth, macrophages
- MeSH terms
- Animals, Cells, Cultured, Female, Humans, Macrophages, Mice, Inbred BALB C, Mycobacterium tuberculosis, Tuberculosis, Zinc, Bacterial Proton-Translocating ATPases, Mice
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