EspL is essential for virulence and stabilizes EspE, EspF and EspH levels in Mycobacterium tuberculosis
Open accessAbstract
The ESX-1, type VII, secretion system represents the major virulence determinant of Mycobacterium tuberculosis, one of the most successful intracellular pathogens. Here, by combining genetic and high-throughput approaches, we show that EspL, a protein of 115 amino acids, is essential for mediating ESX-1-dependent virulence and for stabilization of EspE, EspF and EspH protein levels. Indeed, an espL knock-out mutant was unable to replicate intracellularly, secrete ESX-1 substrates or stimulate innate cytokine production. Moreover, proteomic studies detected greatly reduced amounts of EspE, EspF and EspH in the espL mutant as compared to the wild type strain, suggesting a role for EspL as a chaperone. The latter conclusion was further supported by discovering that EspL interacts with EspD, which was previously demonstrated to stabilize the ESX-1 substrates and effector proteins, EspA and EspC. Loss of EspL also leads to downregulation in M. tuberculosis of WhiB6, a redox-sensitive transcriptional activator of ESX-1 genes. Overall, our data highlight the importance of a so-far overlooked, though conserved, component of the ESX-1 secretion system and begin to delineate the role played by EspE, EspF and EspH in virulence and host-pathogen interaction.
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EspL can have a role as a chaperone and is essential for ESX-1-dependent virulence.
“In addition, it was suggested that EspL can have a role as a chaperone and is essential for ESX-1dependent virulence (50).”
From ESX/Type VII Secretion Systems—An Important Way Out for Mycobacterial Proteins (2019) · cites this paper as [50]
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Cites
R: A Language and Environment for Statistical Computing
R Core Team (2000) · doi:10.32614/r.manuals · Cited by 355,706 · see citing works
Moderated estimation of fold change and dispersion for RNA-seq data with DESeq2
Love, M. I., Huber, W., & Anders, S. (2014) · Genome Biology · doi:10.1186/s13059-014-0550-8 · Cited by 95,106 · see citing works
Trimmomatic: a flexible trimmer for Illumina sequence data
Bolger, A. M., Lohse, M., & Usadel, B. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btu170 · Cited by 65,548 · see citing works
Fast gapped-read alignment with Bowtie 2
Langmead, B., & Salzberg, S. L. (2012) · Nature Methods · doi:10.1038/nmeth.1923 · Cited by 56,400 · see citing works
featureCounts: an efficient general purpose program for assigning sequence reads to genomic features
Liao, Y., Smyth, G. K., & Shi, W. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btt656 · Cited by 27,219 · see citing works
Cox, J., & Mann, M. (2008) · Nature Biotechnology · doi:10.1038/nbt.1511 · Cited by 14,855 · see citing works
Universal sample preparation method for proteome analysis
Wiśniewski, J. R., Zougman, A., Nagaraj, N., & Mann, M. (2009) · Nature Methods · doi:10.1038/nmeth.1322 · Cited by 8,352 · see citing works
The Perseus computational platform for comprehensive analysis of (prote)omics data
Tyanova, S., Temu, T., Sinitcyn, P. G., Carlson, A., Hein, M. Y., Geiger, T., Mann, M., & Cox, J. (2016) · Nature Methods · doi:10.1038/nmeth.3901 · Cited by 7,977 · see citing works
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 · see citing works
Self-citationThe Pfam protein families database: towards a more sustainable future
Finn, R. D., Coggill, P., Eberhardt, R. Y., Eddy, S. R., Mistry, J., Mitchell, A. L., Potter, S. C., Punta, M., Qureshi, M., Sangrador-Vegas, A., et al. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkv1344 · Cited by 5,975 · see citing works
Cox, J., Hein, M. Y., Luber, C. A., Paron, I., Nagaraj, N., & Mann, M. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.031591 · Cited by 5,180 · see citing works
VarScan 2: Somatic mutation and copy number alteration discovery in cancer by exome sequencingPreprint
Koboldt, D. C., Zhang, Q., Larson, D. E., Shen, D., McLellan, M. D., Lin, L., Miller, C. A., Mardis, E. R., Ding, L., & Wilson, R. K. (2012) · Genome Research · doi:10.1101/gr.129684.111 · Cited by 4,822 · see citing works
Rappsilber, J., Mann, M., & Ishihama, Y. (2007) · Nature Protocols · doi:10.1038/nprot.2007.261 · Cited by 4,641 · see citing works
Massive gene decay in the leprosy bacillus.
Cole, S. T., Eiglmeier, K., Parkhill, J., James, K. D., Thomson, N. R., Wheeler, P. R., Honoré, N., Garnier, T., Churcher, C., Harris, D., et al. (2001) · Nature · doi:10.1038/35059006 · Cited by 1,777 · see citing works
Self-citationMolecular 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 · see citing works
M. tuberculosis and M. leprae Translocate from the Phagolysosome to the Cytosol in Myeloid Cells
van der Wel, N., Hava, D., Houben, D., Fluitsma, D., van Zon, M., Pierson, J., Brenner, M., & Peters, P. J. (2007) · Cell · doi:10.1016/j.cell.2007.05.059 · Cited by 960 · see citing works
Hsu, 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 · see citing works
Pym, A. S., Brodin, P., Brosch, R., Huerre, M., & Cole, S. T. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03237.x · Cited by 729 · see citing works
Self-citationLove, M. I., Huber, W. K., & Anders, S. (2014) · Cited by 718 · see citing works
Zumla, A. I., Raviglione, M. C., Hafner, R., & von Reyn, C. F. (2013) · New England Journal of Medicine · doi:10.1056/nejmra1200894 · Cited by 699 · see citing works
Mycobacterium tuberculosis: success through dormancy
Gengenbacher, M., & Kaufmann, S. H. E. (2012) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2012.00331.x · Cited by 698 · see citing works
Watson, R. O., Bell, S. L., MacDuff, D. A., Kimmey, J. M., Diner, E. J., Olivas, J., Vance, R. E., Stallings, C. L., Virgin, H. W., & Cox, J. S. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.05.004 · Cited by 645 · see citing works
Deletion of RD1 from<i>Mycobacterium tuberculosis</i>Mimics Bacille Calmette‐Guérin Attenuation
Lewis, K. N., Liao, R., Guinn, K. M., Hickey, M. J., Smith, S., Behr, M. A., & Sherman, D. R. (2003) · The Journal of Infectious Diseases · doi:10.1086/345862 · Cited by 588 · see citing works
Quantitative proteomics combined with BAC TransgeneOmics reveals in vivo protein interactions
Hubner, N. C., Bird, A. W., Cox, J., Splettstoesser, B., Bandilla, P., Poser, I., Hyman, A., & Mann, M. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200911091 · Cited by 440 · see citing works
Efficient allelic exchange and transposon mutagenesis in Mycobacterium tuberculosis
Pelicic, V., Jackson, M., Reyrat, J., Jacobs, W. R., Gicquel, B., & Guilhot, C. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.20.10955 · Cited by 423 · see citing works
Wassermann, R., Gulen, M. F., Sala, C., Perin, S. G., Lou, Y., Rybniker, J., Schmid-Burgk, J. L., Schmidt, T., Hornung, V., Cole, S. T., et al. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.05.003 · Cited by 401 · see citing works
Self-citationMutually dependent secretion of proteins required for mycobacterial virulence.
Fortune, S. M., Jaeger, A., Sarracino, D. A., Chase, M. R., Sassetti, C. M., Sherman, D. R., Bloom, B. R., & Rubin, E. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504922102 · Cited by 396 · see citing works
Cyclic GMP-AMP Synthase Is an Innate Immune DNA Sensor for Mycobacterium tuberculosis
Collins, A. C., Cai, H., Li, T., Franco, L. H., Li, X.-D., Nair, V. R., Scharn, C. R., Stamm, C. E., Levine, B., Chen, Z. J., et al. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.05.005 · Cited by 384 · see citing works
ESX secretion systems: mycobacterial evolution to counter host immunity
Gröschel, M. I., Sayes, F., Simeone, R., Majlessi, L., & Brosch, R. (2016) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2016.131 · Cited by 382 · see citing works
Diabetes and tuberculosis: the impact of the diabetes epidemic on tuberculosis incidence
Stevenson, C. R., Forouhi, N. G., Roglić, G., Williams, B. G., Lauer, J. A., Dye, C., & Unwin, N. C. (2007) · BMC Public Health · doi:10.1186/1471-2458-7-234 · Cited by 365 · see citing works
The ESAT-6/WXG100 superfamily – and a new Gram-positive secretion system?
Pallen, M. J. (2002) · Trends in Microbiology · doi:10.1016/s0966-842x(02)02345-4 · Cited by 361 · see citing works
Renshaw, P. S., Panagiotidou, P., Whelan, A. O., Gordon, S. V., Hewinson, R. G., Williamson, R. A., & Carr, M. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201625200 · Cited by 337 · see citing works
Structure and function of the complex formed by the tuberculosis virulence factors CFP‐10 and ESAT‐6
Renshaw, P. S., Lightbody, K. L., Veverka, V., Muskett, F. W., Kelly, G. P., Frenkiel, T. A., Gordon, S. V., Hewinson, R. G., Burke, B., Norman, J. C., et al. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600732 · Cited by 329 · see citing works
Cortes, T., Schubert, O. T., Rose, G., Arnvig, K. B., Comas, I., Aebersold, R., & Young, D. B. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.10.031 · Cited by 310 · see citing works
Smith, J., Manoranjan, J., Pan, M., Bohsali, A., Xu, J., Liu, J., McDonald, K. L., Szyk, A., LaRonde-LeBlanc, N. A., & Gao, L. (2008) · Infection and Immunity · doi:10.1128/iai.00614-08 · Cited by 291 · see citing works
ESX/type VII secretion systems and their role in host–pathogen interaction
Siméone, R., Bottai, D., & Brosch, R. (2009) · Current Opinion in Microbiology · doi:10.1016/j.mib.2008.11.003 · Cited by 250 · see citing works
Rickman, L., Scott, C. S., Hunt, D. M., Hutchinson, T., Menendez, M. C., Whalan, R. H., Hinds, J., Colston, M. J., Green, J. D., & Buxton, R. S. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04609.x · Cited by 226 · see citing works
Gordon, B. R. G., Li, Y., Wang, L., Sintsova, A., van Bakel, H., Tian, S., Navarre, W. W., Xia, B., & Liu, J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913551107 · Cited by 219 · see citing works
A mycobacterium ESX-1-secreted virulence factor with unique requirements for export.
McLaughlin, B., Chon, J. S., MacGurn, J. A., Carlsson, F., Cheng, T. L., Cox, J. S., & Brown, E. J. (2007) · PLoS Pathogens · doi:10.1371/journal.ppat.0030105 · Cited by 196 · see citing works
General secretion signal for the mycobacterial type VII secretion pathway
Daleke, M. H., Ummels, R., Bawono, P., Heringa, J., Vandenbroucke‐Grauls, C. M. J. E., Luirink, J., & Bitter, W. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1119453109 · Cited by 192 · see citing works
Brodin, P. M., Poquet, Y., Levillain, F., Péguillet, I., Larrouy-Maumus, G. J., Gilleron, M., Ewann, F., Christophe, T., Fenistein, D., Jang, J., et al. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001100 · Cited by 186 · see citing works
Ohol, Y. M., Goetz, D. H., Chan, K., Shiloh, M. U., Craik, C. S., & Cox, J. S. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2010.02.006 · Cited by 149 · see citing works
Brodin, P. M., Eiglmeier, K., Marmiesse, M., Billault, A., Garnier, T., Niemann, S., Cole, S. T., & Brosch, R. (2002) · Infection and Immunity · doi:10.1128/iai.70.10.5568-5578.2002 · Cited by 148 · see citing works
Self-citationThe PhoP-Dependent ncRNA Mcr7 Modulates the TAT Secretion System in Mycobacterium tuberculosis
Solans, L., Gonzalo-Asensio, J., Sala, C., Benjak, A., Uplekar, S., Rougemont, J., Guilhot, C., Malaga, W., Martín, C., & Cole, S. T. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004183 · Cited by 147 · see citing works
Self-citationVirulence Regulator EspR of Mycobacterium tuberculosis Is a Nucleoid-Associated Protein
Blasco, B., Chen, J. M., Hartkoorn, R. C., Sala, C., Uplekar, S. M., Rougemont, J., Pojer, F., & Cole, S. T. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002621 · Cited by 138 · see citing works
Self-citationwhmD is an essential mycobacterial gene required for proper septation and cell division
Gomez, J. E., & Bishai, W. R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.140225297 · Cited by 132 · see citing works
Impact of tuberculosis on HIV-1 replication, diversity, and disease progression.
Collins, K. R., Quiñones‐Mateu, M. E., Toossi, Z., & Arts, E. J. (2002) · PubMed · Cited by 128 · see citing works
Beckham, K. S. H., Ciccarelli, L., Bunduc, C. M., Mertens, H. D. T., Ummels, R., Lugmayr, W., Mayr, J., Rettel, M., Savitski, M. M., Svergun, D. I., et al. (2017) · Nature Microbiology · doi:10.1038/nmicrobiol.2017.47 · Cited by 112 · see citing works
Stoop, E. J. M., Schipper, T., Huber, S. K. R., Nezhinsky, A. E., Verbeek, F. J., Gurcha, S. S., Besra, G. S., Vandenbroucke‐Grauls, C. M. J. E., Bitter, W., & van der Sar, A. M. (2011) · Disease Models & Mechanisms · doi:10.1242/dmm.006676 · Cited by 104 · see citing works
Anticytolytic Screen Identifies Inhibitors of Mycobacterial Virulence Protein Secretion
Rybniker, J., Chen, J. M., Sala, C., Hartkoorn, R. C., Vocat, A., Benjak, A., Boy‐Röttger, S., Zhang, M., Székely, R., Greff, Z., et al. (2014) · Cell Host & Microbe · doi:10.1016/j.chom.2014.09.008 · Cited by 98 · see citing works
Self-citationSolans, L., Aguiló, N., Samper, S., Pawlik, A., Frigui, W., Martı́n, C., Brosch, R., & Gonzalo‐Asensio, J. (2014) · Infection and Immunity · doi:10.1128/iai.01824-14 · Cited by 98 · see citing works
Chen, Z., Hu, Y., Cumming, B. M., Lu, P., Feng, L., Deng, J., Steyn, A. J. C., & Chen, S. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.07.080 · Cited by 91 · see citing works
Kolly, G. S., Boldrin, F., Sala, C., Dhar, N., Hartkoorn, R. C., Ventura, M., Serafini, A., McKinney, J. D., Manganelli, R., & Cole, S. T. (2014) · Molecular Microbiology · doi:10.1111/mmi.12546 · Cited by 90 · see citing works
Self-citationStructure of EspB from the ESX-1 Type VII Secretion System and Insights into its Export Mechanism
Solomonson, M., Setiaputra, D., Makepeace, K. A. T., Lameignère, E., Petrotchenko, E. V., Conrady, D. G., Bergeron, J. R. C., Vuckovic, M., DiMaio, F., Borchers, C. H., et al. (2015) · Structure · doi:10.1016/j.str.2015.01.002 · Cited by 89 · see citing works
Lou, Y., Rybniker, J., Sala, C., & Cole, S. T. (2016) · Molecular Microbiology · doi:10.1111/mmi.13575 · Cited by 84 · see citing works
Self-citationPang, X., Samten, B., Cao, G., Wang, X., Tvinnereim, A., Chen, X.-L., & Howard, S. T. (2012) · Journal of Bacteriology · doi:10.1128/jb.01067-12 · Cited by 80 · see citing works
EspD Is Critical for the Virulence-Mediating ESX-1 Secretion System in Mycobacterium tuberculosis
Chen, J. M., Boy‐Röttger, S., Dhar, N., Sweeney, N. P., Buxton, R. S., Pojer, F., Rosenkrands, I., & Cole, S. T. (2011) · Journal of Bacteriology · doi:10.1128/jb.06417-11 · Cited by 80 · see citing works
Self-citationBottai, D., Majlessi, L., Siméone, R., Frigui, W., Laurent‐Winter, C., Lenormand, P., Chen, J. M., Rosenkrands, I., Huerre, M., Leclerc, C., et al. (2011) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiq089 · Cited by 74 · see citing works
Self-citationM ycobacterium tuberculosis EspB binds phospholipids and mediates EsxA ‐independent virulence
Chen, J. M., Zhang, M., Rybniker, J., Boy‐Röttger, S., Dhar, N., Pojer, F., & Cole, S. T. (2013) · Molecular Microbiology · doi:10.1111/mmi.12336 · Cited by 74 · see citing works
Self-citationMycobacteria employ two different mechanisms to cross the blood-brain barrier
van Leeuwen, L. M., Boot, M., Kuijl, C. P., Picavet, D. I., van Stempvoort, G., van der Pol, S. M. A., de Vries, H. E., van der Wel, N. N., van der Kuip, M., van Furth, A. M., et al. (2018) · Cellular Microbiology · doi:10.1111/cmi.12858 · Cited by 69 · see citing works
Uplekar, S. M., Rougemont, J., Cole, S. T., & Sala, C. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1260 · Cited by 49 · see citing works
Self-citationBosserman, R. E., Nguyen, T. T. M., Sanchez, K. G., Chirakos, A. E., Ferrell, M. J., Thompson, C. R., Champion, M. M., Abramovitch, R. B., & Champion, P. A. D. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1710167114 · Cited by 44 · see citing works
Riley, S. P., Bykowski, T., Cooley, A. E., et al. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp027 · Cited by 43 · see citing works
Phan, T. H., van Leeuwen, L. M., Kuijl, C. P., Ummels, R., van Stempvoort, G., Rubio-Canalejas, A., Piersma, S. R., Jiménez, C. R., van der Sar, A. M., Houben, E. N. G., et al. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007247 · Cited by 42 · see citing works
Lim, K., Tempczyk, A., Parsons, J. F., et al. (2002) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10297 · Cited by 33 · see citing works
Cooley, A. E., Riley, S. P., Kral, K., et al. (2009) · BMC Microbiology · doi:10.1186/1471-2180-9-137 · Cited by 30 · see citing works
Odermatt, N. T., Sala, C., Benjak, A., & Cole, S. T. (2018) · Scientific Reports · doi:10.1038/s41598-018-32340-2 · Cited by 26 · see citing works
Self-citationOdermatt, 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 · see citing works
Self-citationTian, S., Chen, H., Sun, T., Wang, H., Zhang, X., Liu, Y., Xia, J., Guo, C., & Lin, D. (2016) · Protein Expression and Purification · doi:10.1016/j.pep.2016.08.001 · Cited by 7 · see citing works
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ESX/Type VII Secretion Systems—An Important Way Out for Mycobacterial Proteins
Vaziri, F., & Brosch, R. (2019) · Microbiology Spectrum · doi:10.1128/microbiolspec.psib-0029-2019 · Cited by 50 · see citing works
Lagune, M., Petit, C., Sotomayor, F. V., Johansen, M. D., Beckham, K. S. H., Ritter, C., Girard-Misguich, F., Wilmanns, M., Kremer, L., Maurer, F. P., et al. (2021) · Microbiology · doi:10.1099/mic.0.001054 · Cited by 27 · see citing works
- Authors
- Sala, C., Odermatt, N. T., Soler-Arnedo, P., Gülen, M. F., von Schultz, S., Benjak, A., & Cole, S. T.
- Affiliations
- École Polytechnique Fédérale de Lausanne (CH)
- Corresponding author
- Sala, Claudia
- Cole, Stewart T.
- ORCID
- Venue
- PLOS Pathogens
- Publisher
- Public Library of Science (PLoS)
- Published
- 2018-12-20
- Volume
- 14
- Issue
- 12
- Pages
- e1007491
- ISSN
- 1553-7366 (ISSN-L)
- 1553-7374
- PMC
- PMC6319747
- OpenAlex
- W2904946914
- Cited by
- 35
- References
- 69
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 2 · 2023: 4 · 2022: 4 · 2021: 5 · 2020: 7 · 2019: 8
- FWCI
- 3.78
- Type
- journal article
- Language
- en
- Update notices
- new_version (2019-01-04)
- Open access
- gold
- doi.org
- Licence
- Locations
- PLoS Pathogens (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (31003A_162641)
- 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
- ESX-1 secretion system, Mycobacterium tuberculosis, virulence, ESPE, EspF, EspD, molecular chaperones, protein stabilization, intracellular replication, host-pathogen interaction, type VII secretion system
- MeSH terms
- THP-1 Cells, Antigens, Bacterial, Bacterial Proteins, Humans, Mycobacterium tuberculosis, Tuberculosis, Virulence, Virulence Factors
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