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Secreted transcription factor controls Mycobacterium tuberculosis virulence
Open accessAbstract
Bacterial pathogens trigger specialized virulence factor secretion systems on encountering host cells. The ESX-1 protein secretion system of Mycobacterium tuberculosis-the causative agent of the human disease tuberculosis-delivers bacterial proteins into host cells during infection and is critical for virulence, but how it is regulated is unknown. Here we show that EspR (also known as Rv3849) is a key regulator of ESX-1 that is required for secretion and virulence in mice. EspR activates transcription of an operon that includes three ESX-1 components, Rv3616c-Rv3614c, whose expression in turn promotes secretion of ESX-1 substrates. EspR directly binds to and activates the Rv3616c-Rv3614c promoter and, unexpectedly, is itself secreted from the bacterial cell by the ESX-1 system that it regulates. Efflux of the DNA-binding regulator results in reduced Rv3616c-Rv3614c transcription, and thus reduced ESX-1 secretion. Our results reveal a direct negative feedback loop that regulates the activity of a secretion system essential for virulence. As the virulence factors secreted by the ESX-1 system are highly antigenic, fine control of secretion may be critical to successful infection.
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“Thus far, four ESX-1 substrates have been identified in addition to ESAT-6 and CFP-10. These substrates are called EspA [39], EspB [46], EspR [41], and the M. marinum homologue of Rv3864 [22].”
From Systematic Genetic Nomenclature for Type VII Secretion Systems (2009) · cites this paper as [41]
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Cites
In silico prediction of protein-protein interactions in human macrophages
Souiai, O., Guerfali, F. Z., Miled, S. B., Brun, C., & Benkahla, A. (2014) · BMC Research Notes · doi:10.1186/1756-0500-7-157 · Cited by 10,785
Significance analysis of microarrays applied to the ionizing radiation response
Tusher, V. G., Tibshirani, R., & Chu, G. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.091062498 · Cited by 10,568
Enhanced genome annotation using structural profiles in the program 3D-PSSM 1 1Edited by J. Thornton
Kelley, L. A., MacCallum, R. M., & Sternberg, M. J. E. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3741 · Cited by 1,464
Transcriptional Adaptation of Mycobacterium tuberculosis within Macrophages
Schnappinger, D., Ehrt, S., Voskuil, M. I., Liu, Y., Mangan, J. A., Monahan, I. M., Dolganov, G., Efron, B., Butcher, P. D., Nathan, C., et al. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20030846 · Cited by 1,420
Molecular analysis of genetic differences between Mycobacterium bovis BCG and virulent M. bovis
Mahairas, G. G., Sabo, P. J., Hickey, M. J., Singh, D. C., & Stover, C. K. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.5.1274-1282.1996 · Cited by 1,103
Ensoli, B., Buonaguro, L., Barillari, G., Valeria Fiorelli, A., Gendelman, R., Morgan, R. A., Wingfield, P. T., & Gallo, R. C. (1993) · Journal of Virology · doi:10.1128/jvi.67.1.277-287.1993 · Cited by 795
Type VII secretion — mycobacteria show the way
Abdallah, A. M., Gey van Pittius, N. C., DiGiuseppe Champion, P. A., Cox, J., Luirink, J., Vandenbroucke-Grauls, C. M. J. E., Appelmelk, B. J., & Bitter, W. (2007) · Nature Reviews Microbiology · doi:10.1038/nrmicro1773 · Cited by 763
Self-citationHsu, T., Hingley-Wilson, S. M., Chen, B., Chen, M., Dai, A. Z., Morin, P. M., Marks, C. B., Padiyar, J., Goulding, C., Gingery, M., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1635213100 · Cited by 731
Stanley, S. A., Raghavan, S., Hwang, W. W., & Cox, J. S. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2235593100 · Cited by 570
Self-citationGuinn, K. M., Hickey, M. J., Mathur, S. K., Zakel, K. L., Grotzke, J. E., Lewinsohn, D. M., Smith, S., & Sherman, D. R. (2004) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03844.x · Cited by 508
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Research works printed but not linked: 4
- Stanley, S. A., Raghavan, S., Hwang, W. W. & Cox, J. S. Acute infection and macrophage subversion by Mycobacterium tuberculosis require a specialized secretion system. Proc. Natl Acad. Sci. USA 100, 13001–13006 (2003) · DOI · Paper page
- MacGurn, J. A., Raghavan, S., Stanley, S. A. & Cox, J. S. A non-RD1 gene cluster is required for Snm secretion in Mycobacterium tuberculosis . Mol. Microbiol. 57, 1653–1663 (2005) · DOI · Paper page
- Greenstein, A. E. et al. tuberculosis Ser/Thr protein kinase D phosphorylates an anti-anti-sigma factor homolog. PLoS Pathog. 3, e49 (2007) · DOI
- Schnappinger, D. et al. Transcriptional adaptation of Mycobacterium tuberculosis within macrophages: Insights into the phagosomal environment. J. Exp. Med. 198, 693–704 (2003) · DOI · Paper page
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Molecular mechanisms underlying the function diversity of transcriptional factor IclR family
zhou, Y., Huang, H., Zhou, P., & Xie, J. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.02.008 · Cited by 21
Yandrapally, S., Agarwal, A., Chatterjee, A., Sarkar, S., Mohareer, K., & Banerjee, S. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1276817 · Cited by 20
Behra, P. R. K., Das, S., Pettersson, B. M. F., Shirreff, L., DuCote, T. J., Jacobsson, K.-G., Ennis, D. G., & Kirsebom, L. A. (2019) · Scientific Reports · doi:10.1038/s41598-019-40922-x · Cited by 20
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van der Woude, A. D., Luirink, J., & Bitter, W. (2012) · Current topics in microbiology and immunology · doi:10.1007/82_2012_298 · Cited by 20
Vargas-Romero, F., Gutiérrez-Nájera, N., Mendoza‐Hernández, G., Ortega‐Bernal, D., Hernández‐Pando, R., & Castañón-Arreola, M. (2016) · Pathogens and Disease · doi:10.1093/femspd/ftv127 · Cited by 19
Expression and regulatory networks of Mycobacterium tuberculosis PE/PPE family antigens
Li, W., Deng, W., & Xie, J. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27608 · Cited by 19
Jin, C., Wu, X., Dong, C., Li, F., Fan, L., Xiong, S., & Dong, Y. (2019) · Tuberculosis · doi:10.1016/j.tube.2019.03.010 · Cited by 19
Guan, Q., Ummels, R., Ben-Rached, F., Alzahid, Y. A., Amini, M. S., Adroub, S. A., van Ingen, J., Bitter, W., Abdallah, A. M., & Pain, A. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.00122 · Cited by 22
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Groot, A. S. D. (2011) · Immunome Research · doi:10.4172/1745-7580.1000043 · Cited by 19
Payros, D., Alonso, H., Malaga, W., Volle, A., Mazères, S., Dejean, S., Valière, S., Moreau, F., Balor, S., Stella, A., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1010020 · Cited by 18
Yap, M.-N. F., & Bernstein, H. D. (2013) · Journal of Bacteriology · doi:10.1128/jb.00211-13 · Cited by 18
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Dou, Y., Xie, Y., Zhang, L., Liu, S., Xu, D., Wei, Y., Li, Y., & Zhang, X. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.880315 · Cited by 17
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Eitson, J. L., Medeiros, J. J., Hoover, A. R., Srivastava, S., Roybal, K. T., nsa, J. ⁄. A. A. ⁄., Hansen, E. J., Gumbo, T., & van Oers, N. S. C. (2012) · Applied and Environmental Microbiology · doi:10.1128/aem.01674-12 · Cited by 16
Blasco, B., Japaridze, A., Stenta, M., Wicky, B. I. M., Dietler, G., Peraro, M. D., Pojer, F., & Cole, S. T. (2014) · Journal of Bacteriology · doi:10.1128/jb.00039-14 · Cited by 15
Nogueira, L. D. L., Cardoso, F. C., de Mattos, A. M. M., Bordignon, J., Figueiredo, C. P., Dahlstrom, P., Frota, C. C., dos Santos, C. N. D., Chalhoub, M., Cavada, B. S., et al. (2009) · European Journal of Immunology · doi:10.1002/eji.200939747 · Cited by 16
Calder, B., Soares, N. C., de Kock, E., & Blackburn, J. M. (2015) · Expert Review of Proteomics · doi:10.1586/14789450.2015.1007046 · Cited by 15
Dissecting Regulatory Networks in Host-Pathogen Interaction Using ChIP-on-chip Technology
Sala, C., Grainger, D. C., & Cole, S. T. (2009) · Cell Host & Microbe · doi:10.1016/j.chom.2009.04.007 · Cited by 14
Guo, Q., Bi, J., Li, M., Ge, W., Xu, Y., Fan, W., Wang, H., & Zhang, X. (2019) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2019.00158 · Cited by 15
Singh, A. R., Strankman, A., Orkusyan, R., Purwantini, E., & Rawat, M. (2016) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2016.08.006 · Cited by 13
Type VII Secretion: A Highly Versatile Secretion System
Ates, L. S., Houben, E. N. G., & Bitter, W. (2016) · ASM Press eBooks · doi:10.1128/9781555819286.ch13 · Cited by 13
Sun, D., Liu, Q., He, Y., Wang, C., Wu, F., Tian, C., & Zang, J. (2013) · Protein & Cell · doi:10.1007/s13238-013-3089-7 · Cited by 14
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Rajni, R. (2011) · American Journal of Immunology · doi:10.3844/ajisp.2011.1.8 · Cited by 13
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Phosphate responsive regulation provides insights for ESX-5 function in Mycobacterium tuberculosis
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Chiliza, T. E., Pillay, M., Naidoo, K., & Pillay, B. (2019) · Tuberculosis · doi:10.1016/j.tube.2019.03.005 · Cited by 11
Michelsen, S. W., Søborg, B., Díaz, L. J., Hoff, S. T., Agger, E. M., Koch, A., Rosenkrands, I., Wohlfahrt, J., & Melbye, M. (2017) · PLoS ONE · doi:10.1371/journal.pone.0177906 · Cited by 10
Odermatt, N. T., Sala, C., Benjak, A., Kolly, G. S., Vocat, A., Lupien, A., & Cole, S. T. (2017) · Journal of Bacteriology · doi:10.1128/jb.00129-17 · Cited by 10
Nicholson, K. R., Cronin, R. M., Prest, R. J., Menon, A. R., Yang, Y., Jennisch, M. K., Champion, M. M., Tobin, D. M., & Champion, P. A. D. (2024) · mBio · doi:10.1128/mbio.03357-23 · Cited by 12
A comparative structure-function analysis of active-site inhibitors ofVibrio choleraecholix toxin
Lugo, M. R., & Merrill, A. R. (2015) · Journal of Molecular Recognition · doi:10.1002/jmr.2469 · Cited by 9
Lata, S., Mahatha, A. C., Mal, S., Gupta, U. D., Kundu, M., & Basu, J. (2022) · Molecular Microbiology · doi:10.1111/mmi.14895 · Cited by 9
Manjunath, P., Ahmad, J., Samal, J., Rani, A., Sheikh, J. A., Zarin, S., Ahuja, Y., Alam, A., Hasnain, S. E., & Ehtesham, N. Z. (2024) · Frontiers in Microbiology · doi:10.3389/fmicb.2024.1344857 · Cited by 8
Lugo, M. R., & Merrill, A. R. (2015) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2014.1000972 · Cited by 8
Sarkar, S., Dey, U., Trust Boitumelo Khohliwe, Yella, V. R., & Kumar, A. A. (2021) · FEBS Letters · doi:10.1002/1873-3468.14178 · Cited by 7
Evasion of Innate and Adaptive Immunity byMycobacterium tuberculosis
Goldberg, M. F., Saini, N. K., & Porcelli, S. A. (2015) · ASM Press eBooks · doi:10.1128/9781555818845.ch36 · Cited by 7
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Bonsall, M. B. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012440 · Cited by 7
Das, C., Ghosh, T. S., & Mande, S. S. (2016) · Journal of Biosciences · doi:10.1007/s12038-016-9599-8 · Cited by 7
Keshavam, C. C., Naz, S., Gupta, A., Sanyal, P., Kochar, M., Gangwal, A., Sangwan, N., Kumar, N., Tyagi, E., Goel, S., et al. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105364 · Cited by 6
Deng, W., Xiang, X., & Xie, J. (2013) · Current Microbiology · doi:10.1007/s00284-013-0507-2 · Cited by 7
Mahani, Faturachman, F., Michelle, M., Lembong, E., Sulaeman, A., Hardinsyah, H. H. H., Nurjanah, N., Sunarno, S., & Sariadji, K. (2021) · International Journal of Pharmacy and Pharmaceutical Sciences · doi:10.22159/ijpps.2021v13i4.39618 · Cited by 6
Magombedze, G., & Marino, S. (2018) · Current Opinion in Systems Biology · doi:10.1016/j.coisb.2018.07.002 · Cited by 6
Gupta, S. K., Angara, R. K., Yousuf, S., Reddy, C. G., & Ranjan, A. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.00003 · Cited by 6
ATG16L1 controls mammalian vacuolar proton ATPase
Duque, T. L. A., Paddar, M. A., Trosdal, E. S., Javed, R., Allers, L., Mudd, M. H., Akepati, P. R., Mishra, S. R., Salemi, M., Phinney, B. S., et al. (2025) · The Journal of Cell Biology · doi:10.1083/jcb.202503166 · Cited by 5
Porcelli, S. A. (2008) · Nature · doi:10.1038/454702a · Cited by 5
Taylor, N., Bahunde, F., Thompson, A. L., Yu, J.-S., Jacobs, W. R., Letvin, N. L., Haynes, B. F., & Lee, S. (2012) · Clinical and Vaccine Immunology · doi:10.1128/cvi.00131-12 · Cited by 5
pH-responsive substrate switching in mycobacterial type VII ESX secretion
Collars, O. A., Hernandez, R. L., Weaver, S. D., Prest, R. J., Manu, C., Viswanathan, G., Cronin, R. M., Jones, B. S., Tobin, D. M., Champion, M. M., et al. (2026) · mSphere · doi:10.1128/msphere.00056-26 · Cited by 4
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Cao, G., Howard, S. T., Zhang, P., Hou, G., & Pang, X. (2013) · Current Microbiology · doi:10.1007/s00284-013-0404-8 · Cited by 4
Tiwari, S., Casey, R., Goulding, C. W., Hingley‐Wilson, S., & Jacobs, W. R. (2020) · John Wiley & Sons, Inc. eBooks · doi:10.1128/9781683670261.ch8 · Cited by 5
Novel MprA binding motifs in the phoP regulatory region in Mycobacterium tuberculosis
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Peters, R. G., Kelly, J. M., Bibeau, S., Zhou, Y., & Shell, S. S. (2024) · Pathogens · doi:10.3390/pathogens13121041 · Cited by 3
James, K. S., Jain, N., Witzl, K., Cicchetti, N., Fortune, S. M., Ioerger, T. R., Martinot, A. J., & Carey, A. F. (2025) · npj Vaccines · doi:10.1038/s41541-025-01150-9 · Cited by 3
Protein-Mediated Virulence in Mycobacterium tuberculosis
Farnia, P., Velayati, A. A., Ghanavi, J., & Farnia, P. (2025) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-96883-9_5 · Cited by 3
Gangwar, S. P., Meena, S. R., & Saxena, A. K. (2014) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x14004166 · Cited by 3
Bonnet, I., Orgeur, M., Brossier, F., Sayes, F., Frigui, W., Madacki, J., Varet, H., Chauffour, A., Aubry, A., Véziris, N., et al. (2025) · Microbiology Spectrum · doi:10.1128/spectrum.03224-24 · Cited by 3
Salemi, O., Noormohammadi, Z., Bahrami, F., Siadat, S. D., & Ajdary, S. (2020) · PubMed Central · Cited by 3
Prozorov, A. A., Зайчикова, М. В., & Даниленко, В. Н. (2013) · Генетика · doi:10.7868/s0016675813010098 · Cited by 3
More than chromosome organizers: Unique mycobacterial nucleoid-associated proteins
Milcarz, K., Hołówka, J., Strzałka, A., & Zakrzewska‐Czerwińska, J. (2025) · Microbiological Research · doi:10.1016/j.micres.2025.128239 · Cited by 2
Dahham, Z. M., & Haddad, N. I. A. (2022) · Journal of Contemporary Medical Sciences · doi:10.22317/jcms.v8i6.1299 · Cited by 2
Response of Mycobacterial Species to an Acidic Environment
Saviola, B. (2012) · InTech eBooks · doi:10.5772/30535 · Cited by 2
Gangwar, S. P., Meena, S. R., & Saxena, A. K. (2010) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s174430911004618x · Cited by 2
Regulation of Protein Secretion by … Protein Secretion?
Atmakuri, K., & Fortune, S. M. (2008) · Cell Host & Microbe · doi:10.1016/j.chom.2008.08.009 · Cited by 2
Chen, H., Wang, H., Sun, T., Tian, S., Lin, D., & Guo, C. (2016) · Protein Expression and Purification · doi:10.1016/j.pep.2016.03.009 · Cited by 2
Genetic Aspects of Drug Resistance and Virulence in Mycobacterium tuberculosis
Shur, K. V., Bekker, O. B., Зайчикова, М. В., Maslov, D. A., Акимова, Н. И., Zakharevich, N. V., Чекалина, М. С., & Даниленко, В. Н. (2018) · Russian Journal of Genetics · doi:10.1134/s1022795418120141 · Cited by 2
Prozorov, A. A., Зайчикова, М. В., & Даниленко, В. Н. (2013) · Russian Journal of Genetics · doi:10.1134/s1022795413010092 · Cited by 2
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Schnappinger, D., & Ehrt, S. (2015) · ASM Press eBooks · doi:10.1128/9781555818845.ch11 · Cited by 2
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Campen, R. (2015) · Open Access Victoria University of Wellington | Te Herenga Waka (Figshare) · doi:10.26686/wgtn.17009687.v1 · Cited by 3
Chim, N., Cp, O., Contreras, H., & Goulding, C. W. (2012) · PubMed · Cited by 2
Zhou, P., Yuan, Y., Du, Q., Yuan, R., & Xie, J. (2013) · Journal of Immunoassay and Immunochemistry · doi:10.1080/15321819.2013.829493 · Cited by 1
EspB and HtpG interact with the type III-A CRISPR/Cas system of Mycobacterium tuberculosis
Shi, M., Zhang, H., Fleming, J., Wei, W., Chen, H., Dai, X., Liu, Y., Li, C., Ran, F., Wu, Z., et al. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1261613 · Cited by 2
Turbawaty, D. K., Sugianli, A. K., Ganiem, A. R., & Parwati, I. (2022) · Biomedical Research and Therapy · doi:10.15419/bmrat.v9i6.746 · Cited by 1
Bruiners, N. (2012) · SUNScholar (Stellenbosch University) · Cited by 1
Lin, C., Chen, T., Lu, P., Lai, C.-C., Yang, Y., Lin, W., Huang, P., & Chen, Y. (2013) · PLoS ONE · doi:10.1371/annotation/c4731438-54d3-48b4-ad22-1b8f0d2d57ef · Cited by 1
The EspN transcription factor is an infection-dependent regulator of the ESX-1 system in M. marinumPreprint
Nicholson, K. R., Cronin, R. M., Menon, A. R., Jennisch, M. K., Tobin, D. M., & Champion, P. A. D. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.02.15.528779 · Cited by 1
Smith, J. (2010) · University Libraries (University of Maryland)
Elucidation of the substrates of mycosin 3, an essential protease of Mycobacterium tuberculosis
Fang, Z. (2011) · SUNScholar (Stellenbosch University)
The Structure and Function of M. tuberculosis RD-1 Region Encoded Proteins*
Li, H., Xu, J., & Chen, W. (2009) · PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS · doi:10.3724/sp.j.1206.2009.00187 · Cited by 1
Molecular Motors of ESX-Type Secretion Systems
Ramsdell, T. L. (2012) · Digital Access to Scholarship at Harvard (DASH) (Harvard University)
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Hatzios, S. K. (2010) · eScholarship (California Digital Library)
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Al-Harbi, S. A. D. (2011) · OpenGrey (Institut de l'Information Scientifique et Technique)
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Jha, S. S. (2010) · INFLIBNET
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Alzahid, Y. A. (2014) · King Abdullah University of Science and Technology Repository (King Abdullah University of Science and Technology) · doi:10.25781/kaust-2le01
Abdallah, A., Weerdenburg, E. M., Guan, Q., Ummels, R., Borggreve, S., Adroub, S. A., Malas, T. B., Naeem, R., Zhang, H., Otto, T. D., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/297440
Davis, M. M. (2018) · ResearchWorks at the University of Washington (University of Washington)
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Ting, J. H. (2014) · ScholarlyCommons (University of Pennsylvania)
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Abdelaal, H. F. M., Salem, L. M., Steinberg, H. N., & Talaat, A. M. (2025) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2025.1643664
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Ilghari, D. (2009) · Leicester Research Archive (University of Leicester)
Mukherjee, D. B., Sharadamma, N., & Babu, R. N. (2026) · Current Microbiology · doi:10.1007/s00284-025-04716-x
Whole-genome sequencing and analysis of Nocardia veterana isolates from keratitis patients
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Rushna, S., Ansari, O., Mursaleen, A., Ahmed, F., Sheikh, J. A., & Shariq, M. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-27735-1.00007-1
Salina, E. G., Grigorov, A., Martini, B. A., Skvortsova, Y., Logunova, N. N., Kapina, M., Shumkov, M., Bychenko, O. S., Svirshchevskaya, E., Bocharova, I., et al. (2026) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2026.1918881
Metadata
- Authors
- Raghavan, S., Manzanillo, P., Chan, K., Dovey, C., & Cox, J. S.
- Affiliations
- University of California, San Francisco (US)
- Corresponding author
- Cox, Jeffery S.
- Venue
- Nature
- Published
- 2008-08-07
- Volume
- 454
- Issue
- 7205
- Pages
- 717-721
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC2862998
- OpenAlex
- W1973827044
- Cited by
- 202
- References
- 42
- Citations by year
- 2026: 7 · 2025: 6 · 2024: 4 · 2023: 7 · 2022: 5 · 2021: 5 · 2020: 9 · 2019: 11 · 2018: 6 · 2017: 9 · 2016: 13 · 2015: 14 · 2014: 16 · 2013: 15 · 2012: 19
- FWCI
- 12.06
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- W. M. Keck Foundation
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (AI63302, AI51667, R01AI051667, P01AI063302)
- Topics
- Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Immunology and Microbiology › Microbiology › Escherichia coli research studies
- Keywords
- Mycobacterium tuberculosis, ESX-1 secretion system, transcriptional regulation, virulence factors, negative feedback loop, promoter activation, tuberculosis vaccine development, host-pathogen interaction
- MeSH terms
- Animals, Bacterial Proteins, Macrophages, Mice, Inbred C57BL, Mycobacterium tuberculosis, Operon, Promoter Regions, Genetic, Transcription Factors, Transcription, Genetic, Virulence, Transcriptional Activation, Gene Expression Regulation, Bacterial, Virulence Factors, Mice
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