Release of mycobacterial antigens

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

Genes required for mycobacterial growth defined by high density mutagenesis

Sassetti, C. M., Boyd, D. H., & Rubin, E. J. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03425.x · Cited by 2,544

A new evolutionary scenario for the Mycobacterium tuberculosis complex

Brosch, R., Gordon, S. V., Marmiesse, M., Brodin, P. M., Buchrieser, C., Eiglmeier, K., Garnier, T., Gutierrez, C., Hewinson, R. G., Kremer, K., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052548299 · Cited by 1,645

Biological Functions and Biogenesis of Secreted Bacterial Outer Membrane Vesicles

Kulp, A., & Kuehn, M. J. (2010) · Annual Review of Microbiology · doi:10.1146/annurev.micro.091208.073413 · Cited by 1,540

Comparative Genomics of BCG Vaccines by Whole-Genome DNA Microarray

Behr, M. A., Wilson, M. A., Gill, W., Salamon, H., Schoolnik, G. K., Rane, S., & Small, P. M. (1999) · Science · doi:10.1126/science.284.5419.1520 · Cited by 1,527

Genetic requirements for mycobacterial survival during infection

Sassetti, C. M., & Rubin, E. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2134250100 · Cited by 1,327

Pathogenicity Islands and the Evolution of Microbes

Hacker, J. H., & Kaper, J. B. (2000) · Annual Review of Microbiology · doi:10.1146/annurev.micro.54.1.641 · Cited by 1,298

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

High-Resolution Phenotypic Profiling Defines Genes Essential for Mycobacterial Growth and Cholesterol Catabolism

Griffin, J. E., Gawronski, J. D., DeJesus, M. A., Ioerger, T. R., Akerley, B. J., & Sassetti, C. M. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002251 · Cited by 1,048

RESPONSE OF CULTURED MACROPHAGES TO MYCOBACTERIUM TUBERCULOSIS , WITH OBSERVATIONS ON FUSION OF LYSOSOMES WITH PHAGOSOMES

Armstrong, J. A., & Hart, P. D. (1971) · The Journal of Experimental Medicine · doi:10.1084/jem.134.3.713 · Cited by 991

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

Membrane Vesicle Release in Bacteria, Eukaryotes, and Archaea: a Conserved yet Underappreciated Aspect of Microbial Life

Deatherage, B. L., & Cookson, B. T. (2012) · Infection and Immunity · doi:10.1128/iai.06014-11 · Cited by 765

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

Host-directed therapy of tuberculosis based on interleukin-1 and type I interferon crosstalk

Mayer-Barber, K. D., Andrade, B. B., Oland, S. D., Amaral, E. P., Barber, D. L., Gonzales, J., Derrick, S. C., Shi, R., Kumar, N. P., Wei, W., et al. (2014) · Nature · doi:10.1038/nature13489 · Cited by 757

Extracellular M. tuberculosis DNA Targets Bacteria for Autophagy by Activating the Host DNA-Sensing Pathway

Watson, R. O., Manzanillo, P. S., & Cox, J. S. (2012) · Cell · doi:10.1016/j.cell.2012.06.040 · Cited by 755

The primary mechanism of attenuation of bacillus Calmette–Guérin is a loss of secreted lytic function required for invasion of lung interstitial tissue

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

Loss of RD1 contributed to the attenuation of the live tuberculosis vaccines Mycobacterium bovis BCG and Mycobacterium microti

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

Human T cell epitopes of Mycobacterium tuberculosis are evolutionarily hyperconserved

Comas, I., Chakravartti, J., Small, P. M., Galagan, J. E., Niemann, S., Kremer, K., Ernst, J., & Gagneux, S. (2010) · Nature Genetics · doi:10.1038/ng.590 · Cited by 715

Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis

Strong, M., Sawaya, M. R., Wang, S., Phillips, M. L., Cascio, D., & Eisenberg, D. S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602606103 · Cited by 704

Gram‐positive bacteria produce membrane vesicles: Proteomics‐based characterization of Staphylococcus aureus ‐derived membrane vesicles

Lee, E., Choi, D., Kim, D., Kim, J., Park, J. O., Kim, S., Kim, S., Desiderio, D. M., Kim, Y., Kim, K. P., et al. (2009) · PROTEOMICS · doi:10.1002/pmic.200900338 · Cited by 672

Recombinant BCG exporting ESAT-6 confers enhanced protection against tuberculosis

Pym, A. S., Brodin, P., Majlessi, L., Brosch, R., Demangel, C., Williams, A., Griffiths, K. E., Marchal, G., Leclerc, C., & Cole, S. T. (2003) · Nature Medicine · doi:10.1038/nm859 · Cited by 644

Identification of a virulence gene cluster of Mycobacterium tuberculosis by signature‐tagged transposon mutagenesis

Camacho, L. R., Ensergueix, D., Pérez‐Herrán, E., Gicquel, B., & Guilhot, C. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01593.x · Cited by 616

Disclosure of the mycobacterial outer membrane: Cryo-electron tomography and vitreous sections reveal the lipid bilayer structure

Hoffmann, C., Leis, A., Niederweis, M., Plitzko, J. M., & Engelhardt, H. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709530105 · Cited by 596

Deletion of RD1 from Mycobacterium tuberculosis 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

Purification and characterization of a low-molecular-mass T-cell antigen secreted by Mycobacterium tuberculosis

Sørensen, A. L., Nagai, S., Houen, G., Andersen, P., & Andersen, A. B. (1995) · Infection and Immunity · doi:10.1128/iai.63.5.1710-1717.1995 · Cited by 586

The Tat protein export pathway

Berks, B. C., Sargent, F., & Palmer, T. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.01719.x · Cited by 578

Insights from the complete genome sequence of Mycobacterium marinum on the evolution of Mycobacterium tuberculosis

Stinear, T. P., Seemann, T., Harrison, P. F., Jenkin, G. A., Davies, J. K., Johnson, P. D. R., Abdellah, Z., Arrowsmith, C., Chillingworth, T., Churcher, C., et al. (2008) · Genome Research · doi:10.1101/gr.075069.107 · Cited by 570

Acute infection and macrophage subversion by Mycobacterium tuberculosis require a specialized secretion system

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

Pre-Columbian mycobacterial genomes reveal seals as a source of New World human tuberculosis

Bos, K. I., Harkins, K. M., Herbig, A., Coscolla, M., Weber, N., Comas, I., Forrest, S. A., Bryant, J. M., Harris, S. R., Schuenemann, V. J., et al. (2014) · Nature · doi:10.1038/nature13591 · Cited by 566

Phagosomal Rupture by Mycobacterium tuberculosis Results in Toxicity and Host Cell Death

Simeone, R., Bobard, A., Lippmann, J., Bitter, W., Majlessi, L., Brosch, R., & Enninga, J. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002507 · Cited by 561

Identification of variable regions in the genomes of tubercle bacilli using bacterial artificial chromosome arrays

Gordon, S. V., Brosch, R., Billault, A., Garnier, T., Eiglmeier, K., & Cole, S. T. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01383.x · Cited by 537

Individual RD1‐region genes are required for export of ESAT‐6/CFP‐10 and for virulence of Mycobacterium tuberculosis

Guinn, 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

ideR , an Essential Gene in Mycobacterium tuberculosis : Role of IdeR in Iron-Dependent Gene Expression, Iron Metabolism, and Oxidative Stress Response

Rodríguez, G. M., Voskuil, M. I., Gold, B., Schoolnik, G. K., & Smith, I. (2002) · Infection and Immunity · doi:10.1128/iai.70.7.3371-3381.2002 · Cited by 493

A Mycobacterium tuberculosis operon encoding ESAT=6 and a novel low-molecular-mass culture filtrate protein (CFP-10)

Berthet, F., Rasmussen, P. B., Rosenkrands, I., Andersen, P. L., & Gicquel, B. (1998) · Microbiology · doi:10.1099/00221287-144-11-3195 · Cited by 486

Mycobacterium Tuberculosis Activates the DNA-Dependent Cytosolic Surveillance Pathway within Macrophages

Manzanillo, P. S., Shiloh, M. U., Portnoy, D. A., & Cox, J. S. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.03.007 · Cited by 467

Evidence for occurrence of the ESAT-6 protein in Mycobacterium tuberculosis and virulent Mycobacterium bovis and for its absence in Mycobacterium bovis BCG

Harboe, M., Oettinger, T., Wiker, H. G., Rosenkrands, I., & Andersen, P. L. (1996) · Infection and Immunity · doi:10.1128/iai.64.1.16-22.1996 · Cited by 465

Direct Visualization of the Outer Membrane of Mycobacteria and Corynebacteria in Their Native State

Zuber, B., Chami, M., Houssin, C., Dubochet, J., Griffiths, G., & Daffé, M. (2008) · Journal of Bacteriology · doi:10.1128/jb.01919-07 · Cited by 458

The Type I IFN Response to Infection with Mycobacterium tuberculosis Requires ESX-1-Mediated Secretion and Contributes to Pathogenesis

Stanley, S. A., Johndrow, J. E., Manzanillo, P. S., & Cox, J. S. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.5.3143 · Cited by 439

The Mycobacterium tuberculosis regulatory network and hypoxia

Galagan, J. E., Minch, K., Peterson, M., Lyubetskaya, A., Azizi, E., Sweet, L., Gomes, A., Rustad, T., Dolganov, G., Glotova, I., et al. (2013) · Nature · doi:10.1038/nature12337 · Cited by 431

Evasion of innate immunity by Mycobacterium tuberculosis: is death an exit strategy?

Behar, S. M., Divangahi, M., & Remold, H. G. (2010) · Nature Reviews Microbiology · doi:10.1038/nrmicro2387 · Cited by 427

ESX‐1‐mediated translocation to the cytosol controls virulence of mycobacteria

Houben, D., Demangel, C., van Ingen, J., Pérez, J., Baldeón, L., Abdallah, A. M., Caleechurn, L., Bottai, D., van Zon, M., de Punder, K., et al. (2012) · Cellular Microbiology · doi:10.1111/j.1462-5822.2012.01799.x · Cited by 427

Evolution and expansion of the Mycobacterium tuberculosis PE and PPE multigene families and their association with the duplication of the ESAT-6 (esx) gene cluster regions.

van Pittius, N. C. G., Sampson, S. L., Lee, H., Kim, Y., van Helden, P. D., & Warren, R. M. (2006) · BMC Evolutionary Biology · doi:10.1186/1471-2148-6-95 · Cited by 423

Granuloma-Specific Expression of Mycobacterium Virulence Proteins from the Glycine-Rich PE-PGRS Family

Ramakrishnan, L., Federspiel, N. A., & Falkow, S. (2000) · Science · doi:10.1126/science.288.5470.1436 · Cited by 420

Properties and clinical performance of vaccines containing outer membrane vesicles from Neisseria meningitidis

Holst, J., Martin, D., Arnold, R., Huergo, C. C., Oster, P., O’Hallahan, J., & Rosenqvist, E. (2009) · Vaccine · doi:10.1016/j.vaccine.2009.04.071 · Cited by 404

Mutually 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

A mycobacterial virulence gene cluster extending RD1 is required for cytolysis, bacterial spreading and ESAT‐6 secretion

Gao, L., Guo, S., McLaughlin, B., Morisaki, H., Engel, J. N., & Brown, E. J. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04261.x · Cited by 395

Apoptotic Vesicles Crossprime CD8 T Cells and Protect against Tuberculosis

Winau, F., Weber, S., Sad, S., de Diego, J., Hoops, S. L., Breiden, B., Sandhoff, K., Brinkmann, V., Kaufmann, S. H. E., & Schaible, U. E. (2006) · Immunity · doi:10.1016/j.immuni.2005.12.001 · Cited by 395

Bacillus anthracis produces membrane-derived vesicles containing biologically active toxins

Rivera, J., Cordero, R. J. B., Nakouzi, A. S., Frasés, S., Nicola, A. M., & Casadevall, A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008843107 · Cited by 393

The Mycobacterium tuberculosis PhoPR two‐component system regulates genes essential for virulence and complex lipid biosynthesis

Walters, S. B., Dubnau, E., Kolesnikova, I., Laval, F., Daffé, M., & Smith, I. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05102.x · Cited by 385

Pathogenesis of tuberculosis: interaction of Mycobacterium tuberculosis with macrophages

McDonough, K. A., Kress, Y., & Bloom, B. R. (1993) · Infection and Immunity · doi:10.1128/iai.61.7.2763-2773.1993 · Cited by 377

Mycobacteria release active membrane vesicles that modulate immune responses in a TLR2-dependent manner in mice

Prados‐Rosales, R., Baena, A., Martinez, L. R., Luque-Garcia, J. L., Kalscheuer, R., Usha, V., Cámara, C., Nosanchuk, J. D., Besra, G. S., Chen, B., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44261 · Cited by 376

The ESAT-6 gene cluster of Mycobacterium tuberculosis and other high G+C Gram-positive bacteria

Gey van Pittius, N. C., Gamieldien, J., Hide, W., Brown, G. D., Siezen, R. J., & Beyers, A. D. (2001) · Genome Biology · doi:10.1186/gb-2001-2-10-research0044 · Cited by 375

Mycobacterium tuberculosis and the environment within the phagosome

Rohde, K. H., Yates, R. M., Purdy, G. E., & Russell, D. G. (2007) · Immunological Reviews · doi:10.1111/j.1600-065x.2007.00547.x · Cited by 374

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

Mycobacterium tuberculosis protein ESAT-6 is a potent activator of the NLRP3/ASC inflammasome

Mishra, B. B., Moura‐Alves, P., Sonawane, A., Hacohen, N., Griffiths, G. W., Moita, L. F., & Anes, E. (2010) · Cellular Microbiology · doi:10.1111/j.1462-5822.2010.01450.x · Cited by 353

Mycobacterial Esx-3 is required for mycobactin-mediated iron acquisition

Siegrist, M. S., Unnikrishnan, M., McConnell, M. J., Borowsky, M. L., Cheng, T., Siddiqi, N., Fortune, S. M., Moody, D. B., & Rubin, E. J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900589106 · Cited by 347

EsxA and EsxB are secreted by an ESAT-6-like system that is required for the pathogenesis of Staphylococcus aureus infections

Burts, M. L., Williams, W. A., DeBord, K. L., & Missiakas, D. M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405620102 · Cited by 345

Conclusive Evidence That the Major T-cell Antigens of theMycobacterium tuberculosis Complex ESAT-6 and CFP-10 Form a Tight, 1:1 Complex and Characterization of the Structural Properties of ESAT-6, CFP-10, and the ESAT-6·CFP-10 Complex

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

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

Comparative proteome analysis of Mycobacterium tuberculosis and Mycobacterium bovis BCG strains: towards functional genomics of microbial pathogens

Jungblut, P. R., Schaible, U. E., Mollenkopf, H., Zimny‐Arndt, U., Raupach, B., Mattow, J., Halada, P., Lamer, S., Hagens, K., & Kaufmann, S. H. E. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01549.x · Cited by 327

Membrane Vesicles Are Immunogenic Facsimiles of Salmonella typhimurium That Potently Activate Dendritic Cells, Prime B and T Cell Responses, and Stimulate Protective Immunity In Vivo

Alaniz, R. C., Deatherage, B. L., Lara, J. C., & Cookson, B. T. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.11.7692 · Cited by 321

ESAT-6 from Mycobacterium tuberculosis Dissociates from Its Putative Chaperone CFP-10 under Acidic Conditions and Exhibits Membrane-Lysing Activity

de Jonge, M. I., Pehau‐Arnaudet, G., Fretz, M. M., Félix, R., Bottai, D., Brodin, P. M., Honoré, N., Marchal, G., Jiskoot, W., England, P., et al. (2007) · Journal of Bacteriology · doi:10.1128/jb.00469-07 · Cited by 316

Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv

Målen, H., Berven, F. S., Fladmark, K. E., & Wiker, H. G. (2007) · PROTEOMICS · doi:10.1002/pmic.200600853 · Cited by 314

ESAT-6 proteins: protective antigens and virulence factors?

Brodin, P., Rosenkrands, I., Andersen, P., Cole, S. T., & Brosch, R. (2004) · Trends in Microbiology · doi:10.1016/j.tim.2004.09.007 · Cited by 312

Dissection of ESAT-6 System 1 of Mycobacterium tuberculosis and Impact on Immunogenicity and Virulence

Brodin, P. M., Majlessi, L., Marsollier, L., de Jonge, M. I., Bottai, D., Demangel, C., Hinds, J., Neyrolles, O., Butcher, P. D., Leclerc, C., et al. (2005) · Infection and Immunity · doi:10.1128/iai.74.1.88-98.2006 · Cited by 312

Analysis of the proteome of Mycobacterium tuberculosis in silico

Tekaia, F., Gordon, S. V., Garnier, T., Brosch, R., Barrell, B. G., & Cole, S. T. (1999) · Tubercle and Lung Disease · doi:10.1054/tuld.1999.0220 · Cited by 311

Systematic Genetic Nomenclature for Type VII Secretion Systems

Bitter, W., Houben, E. N. G., Bottai, D., Brodin, P., Brown, E. J., Cox, J. S., Derbyshire, K., Fortune, S. M., Gao, L.-Y., Liu, J., et al. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000507 · Cited by 307

Mycobacterium tuberculosis CDC1551 Induces a More Vigorous Host Response In Vivo and In Vitro, But Is Not More Virulent Than Other Clinical Isolates

Manca, C., Tsenova, L., Barry, C. E., Bergtold, A., Freeman, S. L., Haslett, P. A. J., Musser, J. M., Freedman, V. H., & Kaplan, G. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.11.6740 · Cited by 306

The Rieske protein from Paracoccus denitrificans is inserted into the cytoplasmic membrane by the twin‐arginine translocase

Bachmann, J., Bauer, B., Zwicker, K., Ludwig, B., & Anderka, O. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05480.x · Cited by 306

Direct Visualization by Cryo-EM of the Mycobacterial Capsular Layer: A Labile Structure Containing ESX-1-Secreted Proteins

Sani, M., Houben, E. N. G., Geurtsen, J., Pierson, J., de Punder, K., van Zon, M., Wever, B., Piersma, S. R., Jiménez, C. R., Daffé, M., et al. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000794 · Cited by 306

Genomic analysis of smooth tubercle bacilli provides insights into ancestry and pathoadaptation of Mycobacterium tuberculosis

Supply, P., Marceau, M., Mangenot, S., Roche, D., Rouanet, C., Khanna, V., Majlessi, L., Criscuolo, A., Tap, J., Pawlik, A., et al. (2013) · Nature Genetics · doi:10.1038/ng.2517 · Cited by 305

Human T Cell Responses to the ESAT‐6 Antigen fromMycobacterium tuberculosis

Ravn, P., Demissie, A., Eguale, T., Wondwosson, H., Lein, D., Amoudy, H. A., Mustafa, A. S., Jensen, A. K., Holm, A., Rosenkrands, I., et al. (1999) · The Journal of Infectious Diseases · doi:10.1086/314640 · Cited by 301

Mycobacterium marinum Escapes from Phagosomes and Is Propelled by Actin-based Motility

Stamm, L. M., Morisaki, J. H., Gao, L., Jeng, R. L., McDonald, K. L., Roth, R. A., Takeshita, S., Heuser, J., Welch, M. D., & Brown, E. J. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20031072 · Cited by 299

Control of M. tuberculosis ESAT-6 Secretion and Specific T Cell Recognition by PhoP

Frigui, W., Bottai, D., Majlessi, L., Monot, M., Josselin, E., Brodin, P. M., Garnier, T., Gicquel, B., Martı́n, C., Leclerc, C., et al. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.0040033 · Cited by 294

Protein secretion systems and adhesins: The molecular armory of Gram-negative pathogens

Gerlach, R. G., & Hensel, M. (2007) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2007.03.017 · Cited by 294

Progression to Active Tuberculosis, but Not Transmission, Varies byMycobacterium tuberculosisLineage in The Gambia

de Jong, B. C., Hill, P. C., Aiken, A. M., Awine, T., Antonio, M., Adetifa, I., Jackson-Sillah, D., Fox, A., DeRiemer, K., Gagneux, S., et al. (2008) · The Journal of Infectious Diseases · doi:10.1086/591504 · Cited by 290

Cholesterol Catabolism by Mycobacterium tuberculosis Requires Transcriptional and Metabolic Adaptations

Griffin, J. E., Pandey, A. K., Gilmore, S. A., Mizrahi, V., McKinney, J. D., Bertozzi, C. R., & Sassetti, C. M. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.12.016 · Cited by 289

ESX-1 dependent impairment of autophagic flux by Mycobacterium tuberculosis in human dendritic cells

Romagnoli, A., Etna, M. P., Giacomini, E., Pardini, M., Remoli, M. E., Corazzari, M., Falasca, L., Goletti, D., Gafa, V., Siméone, R., et al. (2012) · Autophagy · doi:10.4161/auto.20881 · Cited by 276

PPE and PE_PGRS proteins of Mycobacterium marinum are transported via the type VII secretion system ESX‐5

Abdallah, A. M., Verboom, T., Weerdenburg, E. M., van Pittius, N. C. G., Mahasha, P. W., Jiménez, C. R., Parra, M., Cadieux, N., Brennan, M. J., Appelmelk, B. J., et al. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06783.x · Cited by 276

Are the PE‐PGRS proteins of Mycobacterium tuberculosis variable surface antigens?

Banu, S., Honoré, N., Saint‐Joanis, B., Philpott, D. J., Prévost, M., & Cole, S. T. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02813.x · Cited by 275

SecA2 functions in the secretion of superoxide dismutase A and in the virulence of Mycobacterium tuberculosis

Braunstein, M., Espinosa, B. J., Chan, J., Belisle, J. T., & R. Jacobs, W. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03438.x · Cited by 272

Evidence that Mycobacterial PE_PGRS Proteins Are Cell Surface Constituents That Influence Interactions with Other Cells

Brennan, M. J., Delogu, G., Chen, Y., Bardarov, S., Kriakov, J., Alavi, M., & Jacobs, W. R. (2001) · Infection and Immunity · doi:10.1128/iai.69.12.7326-7333.2001 · Cited by 272

Bacterial Contact-Dependent Delivery Systems

Hayes, C. S., Aoki, S. K., & Low, D. A. (2010) · Annual Review of Genetics · doi:10.1146/annurev.genet.42.110807.091449 · Cited by 272

Memory T Cells in Latent Mycobacterium tuberculosis Infection Are Directed against Three Antigenic Islands and Largely Contained in a CXCR3+CCR6+ Th1 Subset

Arlehamn, C. S. L., Gerasimova, A. V., Mele, F., Henderson, R., Swann, J., Greenbaum, J., Kim, Y., Sidney, J., James, E. A., Taplitz, R., et al. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003130 · Cited by 269

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 259

Mycobacterial PE/PPE Proteins at the Host-Pathogen Interface

Sampson, S. L. (2011) · Clinical and Developmental Immunology · doi:10.1155/2011/497203 · Cited by 258

Global Analysis of theMycobacterium tuberculosisZur (FurB) Regulon

Maciag, A. E., Dainese, E., Rodríguez, G. M., Milano, A., Provvedi, R., Pasca, M. R., Smith, I., Palù, G., Riccardi, G., & Manganelli, R. (2006) · Journal of Bacteriology · doi:10.1128/jb.01190-06 · Cited by 257

Construction, characterization and preclinical evaluation of MTBVAC, the first live-attenuated M. tuberculosis-based vaccine to enter clinical trials

Arbués, A., Aguilo, J. I., Gonzalo‐Asensio, J., Marinova, D., Uranga, S., Puentes, E., Fernandez, C., Parra, A., Cardona, P.-J., Vilaplana, C., et al. (2013) · Vaccine · doi:10.1016/j.vaccine.2013.07.051 · Cited by 256

Induction of nonspecific acquired resistance and delayed-type hypersensitivity, but not specific acquired resistance in mice inoculated with killed mycobacterial vaccines

Orme, I. M. (1988) · Infection and Immunity · doi:10.1128/iai.56.12.3310-3312.1988 · Cited by 253

Exchanging ESAT6 with TB10.4 in an Ag85B Fusion Molecule-Based Tuberculosis Subunit Vaccine: Efficient Protection and ESAT6-Based Sensitive Monitoring of Vaccine Efficacy

Dietrich, J., Aagaard, C., Leah, R., Olsen, A. W., Stryhn, A., Doherty, T. M., & Andersen, P. L. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.10.6332 · Cited by 252

Characterization of protective extracellular membrane-derived vesicles produced by Streptococcus pneumoniae

Olaya‐Abril, A., Prados‐Rosales, R., McConnell, M. J., et al. (2014) · Journal of Proteomics · doi:10.1016/j.jprot.2014.04.023 · Cited by 246

Mycobacterial outer membranes: in search of proteins

Niederweis, M., Danilchanka, O., Huff, J., Hoffmann, C., & Engelhardt, H. (2010) · Trends in Microbiology · doi:10.1016/j.tim.2009.12.005 · Cited by 244

Global Assessment of Genomic Regions Required for Growth in Mycobacterium tuberculosis

Zhang, Y. J., Ioerger, T. R., Huttenhower, C., Long, J. E., Sassetti, C. M., Sacchettini, J. C., & Rubin, E. J. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002946 · Cited by 242

Impact of Mycobacterium ulcerans Biofilm on Transmissibility to Ecological Niches and Buruli Ulcer Pathogenesis

Marsollier, L., Brodin, P. M., Jackson, M., Korduláková, J., Tafelmeyer, P., Carbonnelle, É., Aubry, J., Milon, G., Legras, P., Saint‐André, J., et al. (2007) · PLoS Pathogens · doi:10.1371/journal.ppat.0030062 · Cited by 236

A specific secretion system mediates PPE41 transport in pathogenic mycobacteria

Abdallah, A. M., Verboom, T., Hannes, F., Safi, M., Strong, M., Eisenberg, D. S., Musters, R. J. P., Vandenbroucke‐Grauls, C. M. J. E., Appelmelk, B. J., Luirink, J., et al. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05409.x · Cited by 234

Infection by Tubercular Mycobacteria Is Spread by Nonlytic Ejection from Their Amoeba Hosts

Hagedorn, M., Rohde, K. H., Russell, D. G., & Soldati, T. (2009) · Science · doi:10.1126/science.1169381 · Cited by 233

PhoP: A Missing Piece in the Intricate Puzzle of Mycobacterium tuberculosis Virulence

Gonzalo‐Asensio, J., Mostowy, S., Harders-Westerveen, J., Huygen, K., Hernández‐Pando, R., Thole, J. E. R., Behr, M. A., Gicquel, B., & Martı́n, C. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003496 · Cited by 228

Chapter 2 Biogenesis of the Cell Wall and Other Glycoconjugates of Mycobacterium tuberculosis

Kaur, D., Guerin, M. E., Škovierová, H., Brennan, P. J., & Jackson, M. (2009) · Advances in applied microbiology · doi:10.1016/s0065-2164(09)69002-x · Cited by 223

Take five — Type VII secretion systems of Mycobacteria

Houben, E. N. G., Korotkov, K. V., & Bitter, W. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.11.003 · Cited by 223 · cited 3×

C-Terminal Signal Sequence Promotes Virulence Factor Secretion in Mycobacterium tuberculosis

Champion, P. A. D., Stanley, S. A., Champion, M. M., Brown, E. J., & Cox, J. S. (2006) · Science · doi:10.1126/science.1131167 · Cited by 219

Disruption of the ESX‐5 system of Mycobacterium tuberculosis causes loss of PPE protein secretion, reduction of cell wall integrity and strong attenuation

Bottai, D., Di Luca, M., Majlessi, L., Frigui, W., Simeone, R., Sayes, F., Bitter, W., Brennan, M. J., Leclerc, C., Batoni, G., et al. (2012) · Molecular Microbiology · doi:10.1111/j.1365-2958.2012.08001.x · Cited by 210

Critical role for NLRP3 in necrotic death triggered by Mycobacterium tuberculosis

Wong, K., & Jacobs Jr, W. R. (2011) · Cellular Microbiology · doi:10.1111/j.1462-5822.2011.01625.x · Cited by 209

Role for Mycobacterium tuberculosis Membrane Vesicles in Iron Acquisition

Prados‐Rosales, R., Weinrick, B. C., Piqué, D. G., Jacobs, W. R., Casadevall, A., & Rodríguez, G. M. (2014) · Journal of Bacteriology · doi:10.1128/jb.01090-13 · Cited by 209

A recombinant Mycobacterium smegmatis induces potent bactericidal immunity against Mycobacterium tuberculosis

Sweeney, K. A., Dao, D. N., Goldberg, M. F., Hsu, T., Venkataswamy, M. M., Henao-Tamayo, M. I., Ordway, D. J., Sellers, R. S., Jain, P., Chen, B., et al. (2011) · Nature Medicine · doi:10.1038/nm.2420 · Cited by 208

Phospholipases C are involved in the virulence of Mycobacterium tuberculosis

Raynaud, C., Guilhot, C., Rauzier, J., Bordat, Y., Pelicic, V., Manganelli, R., Smith, I., Gicquel, B., & Jackson, M. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03009.x · Cited by 205

Secreted transcription factor controls Mycobacterium tuberculosis virulence

Raghavan, S., Manzanillo, P., Chan, K., Dovey, C., & Cox, J. S. (2008) · Nature · doi:10.1038/nature07219 · Cited by 202

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 199

Characterization of a Mycobacterium tuberculosis ESX-3 Conditional Mutant: Essentiality and Rescue by Iron and Zinc

Serafini, A., Boldrin, F., Palù, G., & Manganelli, R. (2009) · Journal of Bacteriology · doi:10.1128/jb.00756-09 · Cited by 198

Mycobacterial Mutants with Defective Control of Phagosomal Acidification

Stewart, G. R., Patel, J., Robertson, B. D., Rae, A. J., & Young, D. B. (2005) · PLoS Pathogens · doi:10.1371/journal.ppat.0010033 · Cited by 198

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

High Content Phenotypic Cell-Based Visual Screen Identifies Mycobacterium tuberculosis Acyltrehalose-Containing Glycolipids Involved in Phagosome Remodeling

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 196

Evolutionary history of tuberculosis shaped by conserved mutations in the PhoPR virulence regulator

Gonzalo‐Asensio, J., Malaga, W., Pawlik, A., Astarie‐Dequeker, C., Passemar, C., Moreau, F., Laval, F., Daffé, M., Martı́n, C., Brosch, R., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1406693111 · Cited by 195

Mycobacterium tuberculosis Type VII Secreted Effector EsxH Targets Host ESCRT to Impair Trafficking

Mehra, A., Zahra, A., Thompson, V., Sirisaengtaksin, N., Wells, A., Porto, M., Köster, S., Penberthy, K., Kubota, Y., Dricot, A., et al. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003734 · Cited by 192

A Genetic Screen forMycobacterium tuberculosisMutants Defective for Phagosome Maturation Arrest Identifies Components of the ESX-1 Secretion System

MacGurn, J. A., & Cox, J. S. (2007) · Infection and Immunity · doi:10.1128/iai.01872-06 · Cited by 190

Comparative Immune Response to PE and PE_PGRS Antigens of Mycobacterium tuberculosis

Delogu, G., & Brennan, M. J. (2001) · Infection and Immunity · doi:10.1128/iai.69.9.5606-5611.2001 · Cited by 187

A non‐RD1 gene cluster is required for Snm secretion in Mycobacterium tuberculosis

MacGurn, J. A., Raghavan, S., Stanley, S. A., & Cox, J. S. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04800.x · Cited by 186

Influence of maternal antibodies on vaccine responses: inhibition of antibody but not T cell responses allows successful early prime-boost strategies in mice

Siegrist, C., Barrios, C. S., Martínez, X., Brandt, C., Berney, M., Córdova, M., Kovařík, J., & Lambert, P. (1998) · European Journal of Immunology · doi:10.1002/(sici)1521-4141(199812)28:12 · Cited by 184

Immunization with Vibrio cholerae Outer Membrane Vesicles Induces Protective Immunity in Mice

Schild, S., Nelson, E. J., & Camilli, A. (2008) · Infection and Immunity · doi:10.1128/iai.00532-08 · Cited by 181

Mutation in the Transcriptional Regulator PhoP Contributes to Avirulence of Mycobacterium tuberculosis H37Ra Strain

Lee, J. S., Krause, R., Schreiber, J., Mollenkopf, H., Kowall, J., Stein, R., Jeon, B., Kwak, J.-Y., Song, M.-K., Patron, J. P., et al. (2008) · Cell Host & Microbe · doi:10.1016/j.chom.2008.01.002 · Cited by 180

Crystal structure of the secreted form of antigen 85C reveals potential targets for mycobacterial drugs and vaccines.

Sacchettini, J. C., Ronning, D. R., Klabunde, T., Besra, G. S., Vissa, V., & Belisle, J. T. (2000) · Nature Structural Biology · doi:10.1038/72413 · Cited by 177

Extracellular vesicles produced by the G ram‐positive bacterium B acillus subtilis are disrupted by the lipopeptide surfactin

Brown, L. C., Kessler, A., Cabezas-Sánchez, P., Luque-Garcia, J. L., & Casadevall, A. (2014) · Molecular Microbiology · doi:10.1111/mmi.12650 · Cited by 173

Activation of the NLRP3 inflammasome by Mycobacterium tuberculosis is uncoupled from susceptibility to active tuberculosis

Dorhoi, A., Nouailles, G., Jörg, S., Hagens, K., Heinemann, E., Pradl, L., Oberbeck‐Müller, D., Correa, M. A. D., Reece, S. T., Ruland, J., et al. (2011) · European Journal of Immunology · doi:10.1002/eji.201141548 · Cited by 172

Epitope Mapping of the Immunodominant Antigen TB10.4 and the Two Homologous Proteins TB10.3 and TB12.9, Which Constitute a Subfamily of the esat-6 Gene Family

Skjøt, R. L. V., Brock, I., Arend, S. M., Munk, M. E., Theisen, M., Ottenhoff, T. H. M., & Andersen, P. L. (2002) · Infection and Immunity · doi:10.1128/iai.70.10.5446-5453.2002 · Cited by 169

Composition of the type VII secretion system membrane complex

Houben, E. N. G., Bestebroer, J., Ummels, R., Wilson, L., Piersma, S. R., Jiménez, C. R., Ottenhoff, T. H. M., Luirink, J., & Bitter, W. (2012) · Molecular Microbiology · doi:10.1111/j.1365-2958.2012.08206.x · Cited by 168

Functional Analysis of Early Secreted Antigenic Target-6, the Dominant T-cell Antigen of Mycobacterium tuberculosis, Reveals Key Residues Involved in Secretion, Complex Formation, Virulence, and Immunogenicity

Brodin, P. M., de Jonge, M. I., Majlessi, L., Leclerc, C., Nilges, M., Cole, S. T., & Brosch, R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503515200 · Cited by 165

Mycobacterium tuberculosis MycP1 Protease Plays a Dual Role in Regulation of ESX-1 Secretion and Virulence

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 158

Mycobacterial Secretion Systems ESX-1 and ESX-5 Play Distinct Roles in Host Cell Death and Inflammasome Activation

Abdallah, A. M., Bestebroer, J., Savage, N. D. L., de Punder, K., van Zon, M., Wilson, L., Korbee, C. J., van der Sar, A. M., Ottenhoff, T. H. M., van der Wel, N. N., et al. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1101457 · Cited by 158

ESX‐1 secreted virulence factors are recognized by multiple cytosolic AAA ATPases in pathogenic mycobacteria

Champion, P. A. D., Champion, M. M., Manzanillo, P. S., & Cox, J. S. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06821.x · Cited by 157

Predominant recognition of the ESAT-6 protein in the first phase of interferon with Mycobacterium bovis in cattle

Pollock, J. M., & Andersen, P. L. (1997) · Infection and Immunity · doi:10.1128/iai.65.7.2587-2592.1997 · Cited by 153

The Streptomyces coelicolor whiB gene encodes a small transcription factor-like protein dispensable for growth but essential for sporulation

Davis, N. K., & Chater, K. F. (1992) · Molecular and General Genetics MGG · doi:10.1007/bf00266237 · Cited by 152

Conserved Pro-Glu (PE) and Pro-Pro-Glu (PPE) Protein Domains Target LipY Lipases of Pathogenic Mycobacteria to the Cell Surface via the ESX-5 Pathway

Daleke, M. H., Cascioferro, A., de Punder, K., Ummels, R., Abdallah, A. M., van der Wel, N. N., Peters, P. J., Luirink, J., Manganelli, R., & Bitter, W. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.204966 · Cited by 150

Evasion and subversion of antigen presentation by Mycobacterium tuberculosis

Baena, A., & Porcelli, S. A. (2009) · Tissue Antigens · doi:10.1111/j.1399-0039.2009.01301.x · Cited by 148

A CD74-dependent MHC class I endolysosomal cross-presentation pathway

Basha, G., Omilusik, K. D., Chávez-Steenbock, A., Reinicke, A. T., Lack, N. A., Choi, K. B., & Jefferies, W. A. (2012) · Nature Immunology · doi:10.1038/ni.2225 · Cited by 147

The 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

Virulence Regulator EspR of Mycobacterium tuberculosis Is a Nucleoid-Associated Protein

Blasco, B., Chen, J. M., Hartkoorn, R. C., Sala, C., Uplekar, S., Rougemont, J., Pojer, F., & Cole, S. T. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002621 · Cited by 146

Capsular glucan and intracellular glycogen of Mycobacterium tuberculosis: biosynthesis and impact on the persistence in mice

Sambou, T., Dinadayala, P., Stadthagen, G., Barilone, N., Bordat, Y., Constant, P., Levillain, F., Neyrolles, O., Gicquel, B., Lemassu, A., et al. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06445.x · Cited by 145

The ESX-5 Secretion System of Mycobacterium marinum Modulates the Macrophage Response

Abdallah, A. M., Savage, N. D. L., van Zon, M., Wilson, L., Vandenbroucke‐Grauls, C. M. J. E., van der Wel, N. N., Ottenhoff, T. H. M., & Bitter, W. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.10.7166 · Cited by 143

Protein secretion systems in Mycobacteria

Champion, P. A. D., & Cox, J. S. (2007) · Cellular Microbiology · doi:10.1111/j.1462-5822.2007.00943.x · Cited by 142

Rv3615c is a highly immunodominant RD1 (Region of Difference 1)-dependent secreted antigen specific for Mycobacterium tuberculosis infection

Millington, K. A., Fortune, S. M., Low, J., Garces, A., Hingley‐Wilson, S., Wickremasinghe, M., Kon, O. M., & Lalvani, A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1015153108 · Cited by 141

The Twin-Arginine Translocation Pathway of Mycobacterium smegmatis Is Functional and Required for the Export of Mycobacterial β-Lactamases

McDonough, J. A., Hacker, K., Flores, A. R., Pavelka, M. S., & Braunstein, M. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.22.7667-7679.2005 · Cited by 140

Regulation of the Mycobacterium tuberculosis PE/PPE genes

Voskuil, M. I., Schnappinger, D., Rutherford, R. S., Liu, Y., & Schoolnik, G. K. (2004) · Tuberculosis · doi:10.1016/j.tube.2003.12.014 · Cited by 139

An outer membrane channel protein of Mycobacterium tuberculosis with exotoxin activity

Danilchanka, O., Sun, J., Pavlenok, M., Maueröder, C., Speer, A., Siroy, A., Marrero, J., Trujillo, C., Mayhew, D. L., Doornbos, K. S., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1400136111 · Cited by 135

Influence of ESAT-6 Secretion System 1 (RD1) of Mycobacterium tuberculosis on the Interaction between Mycobacteria and the Host Immune System

Majlessi, L., Brodin, P. M., Brosch, R., Rojas, M.-J., Khun, H., Huerre, M., Cole, S. T., & Leclerc, C. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.6.3570 · Cited by 128

Strong Immunogenicity and Cross-Reactivity of Mycobacterium tuberculosis ESX-5 Type VII Secretion -Encoded PE-PPE Proteins Predicts Vaccine Potential

Sayes, F., Sun, L., Luca, M. D., Siméone, R., Degaiffier, N., Fiette, L., Esin, S., Brosch, R., Bottai, D., Leclerc, C., et al. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.03.003 · Cited by 125

An esat6 knockout mutant of Mycobacterium bovis produced by homologous recombination will contribute to the development of a live tuberculosis vaccine

Wards, B. J., de Lisle, G. W., & Collins, D. M. (2000) · Tubercle and Lung Disease · doi:10.1054/tuld.2000.0244 · Cited by 122

PE is a functional domain responsible for protein translocation and localization on mycobacterial cell wall

Cascioferro, A., Delogu, G., Colone, M., Sali, M., Stringaro, A., Arancia, G., Fadda, G., Palù, G., & Manganelli, R. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.06023.x · Cited by 120

A Mycobacterium avium PPE gene is associated with the ability of the bacterium to grow in macrophages and virulence in mice

Li, Y., Miltner, E. C., Wu, M., Petrofsky, M., & Bermudez, L. E. (2004) · Cellular Microbiology · doi:10.1111/j.1462-5822.2004.00484.x · Cited by 119

Tuberculosis vaccines – rethinking the current paradigm

Andersen, P. L., & Woodworth, J. S. (2014) · Trends in Immunology · doi:10.1016/j.it.2014.04.006 · Cited by 117

Polar Localization of Virulence-Related Esx-1 Secretion in Mycobacteria

Carlsson, F., Joshi, S. A., Rangell, L. K., & Brown, E. J. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000285 · Cited by 116

Disruption of phagosomal membranes of normal alveolar macrophages by the H37Rv strain of Mycobacterium tuberculosis. A correlate of virulence.

Myrvik, Q. N., Leake, E. S., & Wright, M. J. (1984) · PubMed · Cited by 114

Screening of Highly Expressed Mycobacterial Genes Identifies Rv3615c as a Useful Differential Diagnostic Antigen for theMycobacterium tuberculosisComplex

Sidders, B. S., Pirson, C., Hogarth, P. J., Hewinson, R. G., Stoker, N. G., Vordermeier, H. M., & Ewer, K. (2008) · Infection and Immunity · doi:10.1128/iai.00150-08 · Cited by 112

Genetic regulation of vesiculogenesis and immunomodulation in Mycobacterium tuberculosis

Rath, P., Huang, C., Wang, T., Wang, T., Li, H., Prados‐Rosales, R., Elemento, O., Casadevall, A., & Nathan, C. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1320118110 · Cited by 111

PE_PGRS30 is required for the full virulence of Mycobacterium tuberculosis

Iantomasi, R., Sali, M., Cascioferro, A., Palucci, I., Zumbo, A., Soldini, S., Rocca, S., Greco, E., Maulucci, G., Spirito, M. D., et al. (2011) · Cellular Microbiology · doi:10.1111/j.1462-5822.2011.01721.x · Cited by 108

EspA Acts as a Critical Mediator of ESX1-Dependent Virulence in Mycobacterium tuberculosis by Affecting Bacterial Cell Wall Integrity

Garces, A., Atmakuri, K., Chase, M. R., Woodworth, J. S., Krastins, B., Rothchild, A. C., Ramsdell, T. L., Lopez, M. F., Behar, S. M., Sarracino, D. A., et al. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000957 · Cited by 108

A Specific Polymorphism in Mycobacterium tuberculosis H37Rv Causes Differential ESAT-6 Expression and Identifies WhiB6 as a Novel ESX-1 Component

Solans, 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 107

A Point Mutation in the Two-Component Regulator PhoP-PhoR Accounts for the Absence of Polyketide-Derived Acyltrehaloses but Not That of Phthiocerol Dimycocerosates in Mycobacterium tuberculosis H37Ra

Chesne-Seck, M.-L., Barilone, N., Boudou, F., et al. (2007) · Journal of Bacteriology · doi:10.1128/jb.01465-07 · Cited by 105

Distributive Conjugal Transfer in Mycobacteria Generates Progeny with Meiotic-Like Genome-Wide Mosaicism, Allowing Mapping of a Mating Identity Locus

Gray, T. A., Krywy, J. A., Harold, J., Palumbo, M. J., & Derbyshire, K. M. (2013) · PLoS Biology · doi:10.1371/journal.pbio.1001602 · Cited by 100

Induction of CD8 T Cells against a Novel Epitope in TB10.4: Correlation with Mycobacterial Virulence and the Presence of a Functional Region of Difference-1

Billeskov, R., Lundberg, C. V., Andersen, P. L., & Dietrich, J. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.6.3973 · Cited by 100

Bacillus Calmette Guerin Vaccination of Human Newborns Induces a Specific, Functional CD8+ T Cell Response

Murray, R. A., Mansoor, N., Harbacheuski, R., Soler, J., Davids, V., Soares, A. P., Hawkridge, A., Hussey, G. D., Maecker, H. T., Kaplan, G., et al. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.8.5647 · Cited by 100

Inactivation of Rv2525c, a Substrate of the Twin Arginine Translocation (Tat) System of Mycobacterium tuberculosis , Increases β-Lactam Susceptibility and Virulence

Saint‐Joanis, B., Demangel, C., Jackson, M., Brodin, P. M., Marsollier, L., Boshoff, H. I., & Cole, S. T. (2006) · Journal of Bacteriology · doi:10.1128/jb.00631-06 · Cited by 97

High Frequency of CD4+T Cells Specific for the TB10.4 Protein Correlates with Protection againstMycobacterium tuberculosisInfection

Hervás‐Stubbs, S., Majlessi, L., Simsova, M., Morová, J., Rojas, M.-J., Nouzé, C., Brodin, P. M., Šebo, P., & Leclerc, C. (2006) · Infection and Immunity · doi:10.1128/iai.02086-05 · Cited by 96

Cell Envelope Protein PPE68 Contributes to Mycobacterium tuberculosis RD1 Immunogenicity Independently of a 10-Kilodalton Culture Filtrate Protein and ESAT-6

Demangel, C., Brodin, P. M., Cockle, P. J., Brosch, R., Majlessi, L., Leclerc, C., & Cole, S. T. (2004) · Infection and Immunity · doi:10.1128/iai.72.4.2170-2176.2004 · Cited by 95

Mycobacterium tuberculosis and the host cell inflammasome: a complex relationship

Briken, V., Ahlbrand, S. E., & Shah, S. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00062 · Cited by 92

Solution Structure of the Mycobacterium tuberculosis EsxG·EsxH Complex

Ilghari, D., Lightbody, K. L., Veverka, V., Waters, L. C., Muskett, F. W., Renshaw, P. S., & Carr, M. D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.248732 · Cited by 92

A glimpse into the past and predictions for the future: the molecular evolution of the tuberculosis agent

Boritsch, E. C., Supply, P., Honoré, N., Seeman, T., Stinear, T. P., & Brosch, R. (2014) · Molecular Microbiology · doi:10.1111/mmi.12720 · Cited by 92

Sequence Diversity in the pe_pgrs Genes of Mycobacterium tuberculosis Is Independent of Human T Cell Recognition

Copin, R., Coscollá, M., Seiffert, S. N., Bothamley, G. H., Sutherland, J. S., Mbayo, G., Gagneux, S., & Ernst, J. (2014) · mBio · doi:10.1128/mbio.00960-13 · Cited by 91

Identification of Functional Tat Signal Sequences in Mycobacterium tuberculosis Proteins

McDonough, J. A., McCann, J. R., McElvania, E., Silverman, J. S., Rigel, N. W., & Braunstein, M. (2008) · Journal of Bacteriology · doi:10.1128/jb.00749-08 · Cited by 91

Tubercle bacilli rely on a type VII army for pathogenicity

Stoop, E. J. M., Bitter, W., & van der Sar, A. M. (2012) · Trends in Microbiology · doi:10.1016/j.tim.2012.07.001 · Cited by 90

Mycobacterial PE, PPE and ESX clusters: novel insights into the secretion of these most unusual protein families

Bottai, D., & Brosch, R. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06784.x · Cited by 90

The ins and outs of Mycobacterium tuberculosis protein export

Ligon, L. S., Hayden, J., & Braunstein, M. (2011) · Tuberculosis · doi:10.1016/j.tube.2011.11.005 · Cited by 88

Mycobacterial Esx-3 Requires Multiple Components for Iron Acquisition

Siegrist, M. S., Steigedal, M., Ahmad, R., Mehra, A., Dragset, M. S., Schuster, B. M., Philips, J. A., Carr, S. A., & Rubin, E. J. (2014) · mBio · doi:10.1128/mbio.01073-14 · Cited by 87

Specific Chaperones for the Type VII Protein Secretion Pathway

Daleke, M. H., van der Woude, A. D., Parret, A. H. A., Ummels, R., de Groot, A. M., Watson, D., Piersma, S. R., Jiménez, C. R., Luirink, J., Bitter, W., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.397596 · Cited by 85

PPE38 Modulates the Innate Immune Response and Is Required for Mycobacterium marinum Virulence

Dong, D., Wang, D., Li, M., Wang, H., Yu, J., Wang, C., Liu, J., & Gao, Q. (2011) · Infection and Immunity · doi:10.1128/iai.05249-11 · Cited by 85

The T Cell Response to Secreted Antigens of Mycobacterium tuberculosis

Andersen, P. L. (1994) · Immunobiology · doi:10.1016/s0171-2985(11)80460-2 · Cited by 80

Inside or outside the phagosome? The controversy of the intracellular localization of Mycobacterium tuberculosis

Welin, A., & Lerm, M. (2011) · Tuberculosis · doi:10.1016/j.tube.2011.09.009 · Cited by 80

ESAT-6 Secretion-Independent Impact of ESX-1 Genes espF and espG1 on Virulence of Mycobacterium tuberculosis

Bottai, 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 78

M 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 77

Structure of the Response Regulator PhoP from Mycobacterium tuberculosis Reveals a Dimer through the Receiver Domain

Menon, S., & Wang, S. (2011) · Biochemistry · doi:10.1021/bi2005575 · Cited by 71

ESX-5-deficient Mycobacterium marinum is hypervirulent in adult zebrafish

Weerdenburg, E. M., Abdallah, A. M., Mitra, S., de Punder, K., van der Wel, N. N., Bird, S., Appelmelk, B. J., Bitter, W., & van der Sar, A. M. (2012) · Cellular Microbiology · doi:10.1111/j.1462-5822.2012.01755.x · Cited by 70

Analysis of SecA2-dependent substrates in M ycobacterium marinum identifies protein kinase G (PknG) as a virulence effector: Mycobacterial SecA2 substrates

van der Woude, A. D., Stoop, E. J. M., Stiess, M., Wang, S., Ummels, R., van Stempvoort, G., Piersma, S. R., Cascioferro, A., Jiménez, C. R., Houben, E. N. G., et al. (2014) · Cellular Microbiology · doi:10.1111/cmi.12221 · Cited by 64

The ESX-5 Associated eccB5-eccC5 Locus Is Essential for Mycobacterium tuberculosis Viability

Luca, M. D., Bottai, D., Batoni, G., Orgeur, M., Aulicino, A., Counoupas, C., Campa, M., Brosch, R., & Esin, S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0052059 · Cited by 63

Conserved Immune Recognition Hierarchy of Mycobacterial PE/PPE Proteins during Infection in Natural Hosts

Vordermeier, H. M., Hewinson, R. G., Wilkinson, R. J., Wilkinson, K. A., Gideon, H. P., Young, D., & Sampson, S. L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040890 · Cited by 63

Cuban Meningococcal BC Vaccine: Experiences & Contributions from 20 Years of Application

Sotolongo, F., Campa, C., Casanueva, V., et al. (2007) · MEDICC Review · doi:10.37757/mr2007v9.n1.6 · Cited by 62

Antigen Load Governs the Differential Priming of CD8 T Cells in Response to the Bacille Calmette Guérin Vaccine or Mycobacterium tuberculosis Infection

Ryan, A. A., Nambiar, J. K., Wozniak, T. M., Roediger, B., Shklovskaya, E., Britton, W. J., Groth, B. F. D. S., & Triccas, J. A. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0801694 · Cited by 61

CD8+-T-CellResponses of Mycobacterium-Infected Mice to a Newly Identified MajorHistocompatibility Complex Class I-Restricted Epitope Shared byProteins of the ESAT-6Family

Majlessi, L., Rojas, M.-J., Brodin, P. M., & Leclerc, C. (2003) · Infection and Immunity · doi:10.1128/iai.71.12.7173-7177.2003 · Cited by 60

DNA Substrate-Induced Activation of the Agrobacterium VirB/VirD4 Type IV Secretion System

Cascalès, E., Atmakuri, K., Sarkar, M. K., & Christie, P. J. (2013) · Journal of Bacteriology · doi:10.1128/jb.00114-13 · Cited by 58

Mycobacterial Pathogenomics and Evolution

Bottai, D., Stinear, T. P., Supply, P., & Brosch, R. (2014) · Microbiology Spectrum · doi:10.1128/microbiolspec.mgm2-0025-2013 · Cited by 55

Differential Effect of TLR2 and TLR4 on the Immune Response after Immunization with a Vaccine against Neisseria meningitidis or Bordetella pertussis

Fransen, F., Stenger, R. M., Poelen, M. C. M., van Dijken, H. H., Kuipers, B., Boog, C. J. P., van Putten, J. P. M., van Els, C. A. C. M., & van der Ley, P. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015692 · Cited by 53

Phenotypic Profiling of Mycobacterium tuberculosis EspA Point Mutants Reveals that Blockage of ESAT-6 and CFP-10 Secretion In Vitro Does Not Always Correlate with Attenuation of Virulence

Chen, J. M., Zhang, M., Rybniker, J., Basterra, L., Dhar, N., Tischler, A. D., Pojer, F., & Cole, S. T. (2013) · Journal of Bacteriology · doi:10.1128/jb.00967-13 · Cited by 53

Unexpected Link between Lipooligosaccharide Biosynthesis and Surface Protein Release in Mycobacterium marinum

van der Woude, A. D., Sarkar, D., Bhatt, A., Sparrius, M., Raadsen, S. A., Boon, L., Geurtsen, J., van der Sar, A. M., Luirink, J., Houben, E. N. G., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.336461 · Cited by 51

Surface Expression of MPT64 as a Fusion with the PE Domain of PE_PGRS33 Enhances Mycobacterium bovis BCG Protective Activity against Mycobacterium tuberculosis in Mice

Sali, M., Sante, G. D., Cascioferro, A., et al. (2010) · Infection and Immunity · doi:10.1128/iai.00267-10 · Cited by 50

Escape from the Phagosome: The Explanation for MHC-I Processing of Mycobacterial Antigens?

Harriff, M. J., Purdy, G. E., & Lewinsohn, D. M. (2012) · Frontiers in Immunology · doi:10.3389/fimmu.2012.00040 · Cited by 48

Isolation of a proline-rich mycobacterial protein eliciting delayed-type hypersensitivity reactions only in guinea pigs immunized with living mycobacteria.

Romain, F., Augier, J., Pescher, P., et al. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.11.5322 · Cited by 42

Bacterial Protein Secretion Is Required for Priming of CD8+T Cells Specific for theMycobacterium tuberculosisAntigen CFP10

Woodworth, J. S., Fortune, S. M., & Behar, S. M. (2008) · Infection and Immunity · doi:10.1128/iai.00307-08 · Cited by 41

The Transcriptional Regulator Rv0485 Modulates the Expression of a pe and ppe Gene Pair and Is Required for Mycobacterium tuberculosis Virulence

Goldstone, R. M., Goonesekera, S. D., Bloom, B. R., & Sampson, S. L. (2009) · Infection and Immunity · doi:10.1128/iai.01495-08 · Cited by 38

Inhibition of Phagosome Maturation by Mycobacteria Does Not Interfere with Presentation of Mycobacterial Antigens by MHC Molecules

Majlessi, L., Combaluzier, B., Albrecht, I., Garcia, J. E., Nouzé, C., Pieters, J., & Leclerc, C. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.3.1825 · Cited by 36

Proteoliposomes from Mycobacterium smegmatis induce immune cross-reactivity against Mycobacterium tuberculosis antigens in mice

Rodriguez, L., Tirado, Y., Reyes, F., Puig, A., Kadir, R., Borrero, R., Fernandez, S., Reyes, G., Álvarez, N., Garcia, M. A., et al. (2011) · Vaccine · doi:10.1016/j.vaccine.2011.06.077 · Cited by 33

EspI regulates the ESX ‐1 secretion system in response to ATP levels in M ycobacterium tuberculosis

Zhang, M., Chen, J. M., Sala, C., Rybniker, J., Dhar, N., & Cole, S. T. (2014) · Molecular Microbiology · doi:10.1111/mmi.12718 · Cited by 32

Type VII secretion in mycobacteria: classification in line with cell envelope structure

Bitter, W., Houben, E. N. G., Luirink, J., & Appelmelk, B. J. (2009) · Trends in Microbiology · doi:10.1016/j.tim.2009.05.007 · Cited by 32

Building a better tuberculosis vaccine

Young, D. (2003) · Nature Medicine · doi:10.1038/nm868 · Cited by 29

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

Cytosolic Access of Mycobacterium tuberculosis: Critical Impact of Phagosomal Acidification Control and Demonstration of Occurrence In Vivo

Simeone, R., Sayes, F., Song, O., Gröschel, M. I., Brodin, P., Brosch, R., & Majlessi, L. (2015) · PLOS Pathogens · doi:10.1371/journal.ppat.1004650 · Cited by 198

Recombinant BCG Expressing ESX-1 of Mycobacterium marinum Combines Low Virulence with Cytosolic Immune Signaling and Improved TB Protection

Gröschel, M. I., Sayes, F., Shin, S. J., Frigui, W., Pawlik, A., Orgeur, M., Canetti, R., Honoré, N., Simeone, R., van der Werf, T. S., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.02.057 · Cited by 125

Mycobacterial Pan-Genome Analysis Suggests Important Role of Plasmids in the Radiation of Type VII Secretion Systems

Dumas, E., Christina Boritsch, E., Vandenbogaert, M., Rodríguez de la Vega, R. C., Thiberge, J.-M., Caro, V., Gaillard, J.-L., Heym, B., Girard-Misguich, F., Brosch, R., et al. (2016) · Genome Biology and Evolution · doi:10.1093/gbe/evw001 · Cited by 112

ESAT-6–dependent cytosolic pattern recognition drives noncognate tuberculosis control in vivo

Kupz, A., Zedler, U., Stäber, M., Perdomo, C., Dorhoi, A., Brosch, R., & Kaufmann, S. H. E. (2016) · Journal of Clinical Investigation · doi:10.1172/jci84978 · Cited by 67

Mycobacterium bovis and you: A comprehensive look at the bacteria, its similarities to Mycobacterium tuberculosis, and its relationship with human disease

Kanipe, C. R., & Palmer, M. V. (2020) · Tuberculosis · doi:10.1016/j.tube.2020.102006 · Cited by 43

In vitro infection with Mycobacterium tuberculosis induces a distinct immunological pattern in blood from healthy relatives of tuberculosis patients

Juan-García, J., García‐García, S., Guerra-Laso, J. M., Raposo‐García, S., Diez‐Tascón, C., Nebreda-Mayoral, T., López-Fidalgo, E., López-Medrano, R., Fernández-Maraña, A., & Rivero-Lezcano, O. M. (2017) · Pathogens and Disease · doi:10.1093/femspd/ftx109 · Cited by 6

Evaluation of the Mycobacterium smegmatis and BCG models for the discovery of Mycobacterium tuberculosis inhibitors

Altaf, M., Miller, C. H., Bellows, D. S., et al. (2010) · Tuberculosis · doi:10.1016/j.tube.2010.09.002 · Cited by 138

A century of bovine tuberculosis 1888–1988: Conquest and controversy

Pritchard, D. G. (1988) · Journal of Comparative Pathology · doi:10.1016/0021-9975(88)90058-8 · Cited by 152

The Antigens of Mycobacterium tuberculosis, H37Rv, Studied by Crossed Immunoelectrophoresis. Comparison with a Reference System for Mycobacterium bovis, BCG

Wiker, H. G., Harboe, M., Bennedsen, J., et al. (1988) · Scandinavian Journal of Immunology · doi:10.1111/j.1365-3083.1988.tb02342.x · Cited by 58