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

Molecular Cloning: A Laboratory Manual

Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589

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

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

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

Tuberculosis: Pathogenesis, Protection and Control

(1996) · Nature Medicine · doi:10.1038/nm0296-244b · Cited by 977

Complex lipid determines tissue-specific replication of Mycobacterium tuberculosis in mice

Cox, J. S., Chen, B., McNeil, M., & Jacobs, W. R. (1999) · Nature · doi:10.1038/47042 · Cited by 746

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

Specialized transduction: an efficient method for generating marked and unmarked targeted gene disruptions in Mycobacterium tuberculosis, M. bovis BCG and M. smegmatis

Bardarov, S., Bardarov, S. S., Pavelka, M. S., Sambandamurthy, V. K., Larsen, M. H., Tufariello, J. M., Chan, J., Hatfull, G. F., & Jacobs, W. R. (2002) · Microbiology · doi:10.1099/00221287-148-10-3007 · Cited by 590

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

Haem-iron plays a key role in the regulation of the Ess/type VII secretion system of Staphylococcus aureus RN6390

Casabona, M. G., Kneuper, H., Headley, D. A. D. L., Harkins, C. P., Zoltner, M., Hjerde, E., Holden, M. T. G., & Palmer, T. (2017) · Microbiology · doi:10.1099/mic.0.000579 · Cited by 26

Characterization of EssB, a protein required for secretion of ESAT-6 like proteins in Staphylococcus aureus

Chen, Y.-H., Anderson, M. C., Hendrickx, A. P. A., & Missiakas, D. M. (2012) · BMC Microbiology · doi:10.1186/1471-2180-12-219 · Cited by 27

Association of ESAT-6/CFP-10-induced IFN-γ, TNF-α and IL-10 with clinical tuberculosis: evidence from cohorts of pulmonary tuberculosis patients, household contacts and community controls in an endemic setting

Abebe, F., Belay, M., Legesse, M., Mihret, A., & Franken, K. L. M. C. (2017) · Clinical & Experimental Immunology · doi:10.1111/cei.12972 · Cited by 24

Mycobacterium tuberculosis inhibits METTL14-mediated m6A methylation of Nox2 mRNA and suppresses anti-TB immunity

Ma, M., Duan, Y., Peng, C., Wu, Y., Zhang, X., Chang, B., Wang, F., Yang, H., Zheng, R., Cheng, H., et al. (2024) · Cell Discovery · doi:10.1038/s41421-024-00653-4 · Cited by 24

Analysis of Novel Mycobacteriophages Indicates the Existence of Different Strategies for Phage Inheritance in Mycobacteria

Stella, E. J., Franceschelli, J. J., Tasselli, S., & Morbidoni, H. R. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056384 · Cited by 24

The Impact of Genome Region of Difference 4 (RD4) on Mycobacterial Virulence and BCG Efficacy

Ru, H.-W., Liu, X., Lin, C., Yang, J., Chen, F.-Z., Sun, R., Zhang, L., & Liu, J. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00239 · Cited by 26

Mycobacterial virulence: impact on immunogenicity and vaccine research

Kroesen, V. M., Madacki, J., Frigui, W., Sayes, F., & Brosch, R. (2019) · F1000Research · doi:10.12688/f1000research.20572.1 · Cited by 24

Tuberculosis Vaccines

Orme, I. M. (2005) · Drugs · doi:10.2165/00003495-200565170-00002 · Cited by 24

Crosstalk between the ancestral type VII secretion system ESX-4 and other T7SS in Mycobacterium marinum

Wang, Y., Tang, Y., Lin, C., Zhang, J., Mai, J., Jiang, J. H., Gao, X., Li, Y., Zhao, G., Zhang, L., et al. (2021) · iScience · doi:10.1016/j.isci.2021.103585 · Cited by 25

Approaches for targeting the mycobactin biosynthesis pathway for novel anti-tubercular drug discovery: where we stand

Shyam, M., Shilkar, D., Rakshit, G., & Jayaprakash, V. (2022) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2022.2077328 · Cited by 23

For Better or Worse: Cytosolic DNA Sensing during Intracellular Bacterial Infection Induces Potent Innate Immune Responses

Patrick, K. L., Bell, S. L., & Watson, R. O. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.04.030 · Cited by 24

Unravelling the networks dictating host resistance versus tolerance during pulmonary infections

Meunier, I., Kaufmann, E., Downey, J., & Divangahi, M. (2017) · Cell and Tissue Research · doi:10.1007/s00441-017-2572-5 · Cited by 23

Mycobacterium tuberculosis virulence inhibitors discovered by Mycobacterium marinum high-throughput screening

Tükenmez, H., Edström, I., Ummanni, R., Fick, S. B., Sundin, C., Elofsson, M., & Larsson, C. (2019) · Scientific Reports · doi:10.1038/s41598-018-37176-4 · Cited by 23

The ESX-1 Virulence Factors Downregulate miR-147-3p in Mycobacterium marinum-Infected Macrophages

Zuo, X., Wang, L., Bao, Y., & Sun, J. (2020) · Infection and Immunity · doi:10.1128/iai.00088-20 · Cited by 23

Pathogenomic analyses of Mycobacterium microti, an ESX-1-deleted member of the Mycobacterium tuberculosis complex causing disease in various hosts

Orgeur, M., Frigui, W., Pawlik, A., Clark, S. O., Williams, A., Ates, L. S., Ma, L., Bouchier, C., Parkhill, J., Brodin, P. M., et al. (2021) · Microbial Genomics · doi:10.1099/mgen.0.000505 · Cited by 26

Mycobacterium bovis Bacillus Calmette–Guérin (BCG) stimulates IL-10 production via the PI3K/Akt and p38 MAPK pathways in human lung epithelial cells

Méndez‐Samperio, P., Trejo, A., & Pérez, A. (2008) · Cellular Immunology · doi:10.1016/j.cellimm.2008.03.002 · Cited by 24

Mycobacterium tuberculosis secreted antigen (MTSA‐10) modulates macrophage function by redox regulation of phosphatases

Basu, S. K., Kumar, D., Singh, D. K., Ganguly, N., Siddiqui, Z., Rao, K. V. S., & Sharma, P. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05543.x · Cited by 24

In silico identification and synthesis of a multi-drug loaded MOF for treating tuberculosis

Acharya, A. P., Sezginel, K. B., Gideon, H. P., Greene, A. C., Lawson, H., Inamdar, S., Tang, Y., Fraser, A. J., Patel, K. V., Liu, C., et al. (2022) · Journal of Controlled Release · doi:10.1016/j.jconrel.2022.10.024 · Cited by 22

Postprimary Tuberculosis and Macrophage Necrosis: Is There a Big ConNECtion?

Wong, K., & Jacobs, W. R. (2016) · mBio · doi:10.1128/mbio.01589-15 · Cited by 22

Discovery of a novel dehydratase of the fatty acid synthase type II critical for ketomycolic acid biosynthesis and virulence of Mycobacterium tuberculosis

Lefebvre, C., Frigui, W., Slama, N., Lauzéral-Vizcaïno, F., Constant, P., Lemassu, A., Parish, T., Eynard, N., Daffé, M., Brosch, R., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-58967-8 · Cited by 22

Safety of ESAT-6

Aggerbeck, H., & Madsen, S. M. (2005) · Tuberculosis · doi:10.1016/j.tube.2005.08.020 · Cited by 22

Human immune recognition-based multicomponent subunit vaccines against tuberculosis

Sable, S. B., Verma, I., Behera, D., & Khuller, G. K. (2005) · European Respiratory Journal · doi:10.1183/09031936.05.00105404 · Cited by 22

The dynamics of Mycobacterium tuberculosis phagosome and the fate of infection

Zhang, Q.-A., Ma, S., Li, P., & Xie, J. (2023) · Cellular Signalling · doi:10.1016/j.cellsig.2023.110715 · Cited by 21

Role of phagocyte extracellular traps during Mycobacterium tuberculosis infections and tuberculosis disease processes

García-Bengoa, M., Meurer, M., Goethe, R., Singh, M., Reljić, R., & von Köckritz‐Blickwede, M. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2023.983299 · Cited by 22

Pathogenomics of Mycobacteria

Gutierrez, M. C., Supply, P., & Brosch, R. (2009) · Genome dynamics · doi:10.1159/000235772 · Cited by 26

Mycobacteria's Export Strategy

Ize, B., & Palmer, T. (2006) · Science · doi:10.1126/science.1132537 · Cited by 21

Genetic engineering of Mycobacterium tuberculosis: A review

Lamrabet, O., & Drancourt, M. (2012) · Tuberculosis · doi:10.1016/j.tube.2012.06.002 · Cited by 21

Polymorphisms in the PE35 and PPE68 antigens in Mycobacterium tuberculosis strains may affect strain virulence and reflect ongoing immune evasion

Jiang, Y., Wei, J., Liu, H., Li, G., Guo, Q., QIU, Y., Zhao, L., Li, M., Zhao, X., Dou, X., et al. (2015) · Molecular Medicine Reports · doi:10.3892/mmr.2015.4589 · Cited by 21

Retention of EsxA in the Capsule-Like Layer of Mycobacterium tuberculosis Is Associated with Cytotoxicity and Is Counteracted by Lung Surfactant

Raffetseder, J., Iakobachvili, N., Loitto, V. M., Peters, P. J., & Lerm, M. (2019) · Infection and Immunity · doi:10.1128/iai.00803-18 · Cited by 21

Mycobacterium marinum as a model for understanding principles of mycobacterial pathogenesis

Menon, A. R., Prest, R. J., Tobin, D. M., & Champion, P. A. D. (2025) · Journal of Bacteriology · doi:10.1128/jb.00047-25 · Cited by 23

The ESX-1 Substrate PPE68 Has a Key Function in ESX-1-Mediated Secretion in Mycobacterium marinum

Damen, M. P. M., Meijers, A. S., Keizer, E., Piersma, S. R., Jiménez, C. R., Kuijl, C. P., Bitter, W., & Houben, E. N. G. (2022) · mBio · doi:10.1128/mbio.02819-22 · Cited by 21

Striking the Right Balance Determines TB or Not TB

Dasgupta, S. B., & Pieters, J. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00455 · Cited by 21

A Nonsense Mutation in Mycobacterium marinum That Is Suppressible by a Novel Mechanism

Williams, E. A., Medie, F. M., Bosserman, R. E., Johnson, B. K., Thompson, C. R., Ferrell, M. J., Champion, M. M., Abramovitch, R. B., & Champion, P. A. D. (2016) · Infection and Immunity · doi:10.1128/iai.00653-16 · Cited by 21

Esx Paralogs Are Functionally Equivalent to ESX-1 Proteins but Are Dispensable for Virulence in Mycobacterium marinum

Bosserman, R. E., Thompson, C. R., Nicholson, K. R., & Champion, P. A. D. (2018) · Journal of Bacteriology · doi:10.1128/jb.00726-17 · Cited by 20

Transposon libraries identify novel Mycobacterium bovis BCG genes involved in the dynamic interactions required for BCG to persist during in vivo passage in cattle

Mendum, T. A., Chandran, A., Williams, K. J., Vordermeier, H. M., Villarreal‐Ramos, B., Wu, H., Singh, A., Smith, A. A., Butler, R. E., Prasad, A., et al. (2019) · BMC Genomics · doi:10.1186/s12864-019-5791-1 · Cited by 20

Fatty acylCoA synthetase FadD13 regulates proinflammatory cytokine secretion dependent on the NF‐κB signalling pathway by binding to eEF1A1

Wei, S., Wang, D., Li, H., Bi, L., Deng, J., Zhu, G., Zhang, J., Li, C., Li, M., Fang, Y., et al. (2019) · Cellular Microbiology · doi:10.1111/cmi.13090 · Cited by 20

Comparative Genomic and Transcriptomic Analyses of Mycobacterium kansasii Subtypes Provide New Insights Into Their Pathogenicity and Taxonomy

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

BCG-Prime and boost with Esx-5 secretion system deletion mutant leads to better protection against clinical strains of Mycobacterium tuberculosis

Tiwari, S., Dutt, T. S., Chen, B., Chen, M., Kim, J., Dai, A. Z., Lukose, R., Shanley, C. A., Fox, A. C., Karger, B. R., et al. (2020) · Vaccine · doi:10.1016/j.vaccine.2020.08.004 · Cited by 20

Cording, Cord Factors, and Trehalose Dimycolate

Glickman, M. S. (2014) · ASM Press eBooks · doi:10.1128/9781555815783.ch5 · Cited by 20

Mycobacterial virulence and specialized secretion: same story, different ending

Behr, M. A., & Sherman, D. R. (2007) · Nature Medicine · doi:10.1038/nm0307-286 · Cited by 20

The Cell Wall-Associated Mycolactone Polyketide Synthases Are Necessary but Not Sufficient for Mycolactone Biosynthesis

Porter, J. L., Tobias, N. J., Pidot, S. J., Falgner, S., Tuck, K. L., Vettiger, A., Hong, H., Leadlay, P. F., & Stinear, T. P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0070520 · Cited by 21

RD1 region in mycobacterial genome is involved in the induction of necrosis in infected RAW264 cells via mitochondrial membrane damage and ATP depletion

Kaku, T., Kawamura, I., Uchiyama, R., Kurenuma, T., & Mitsuyama, M. (2007) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2007.00838.x · Cited by 19

Virulence-Associated Secretion in Mycobacterium abscessus

Bar-Oz, M., Meir, M., & Barkan, D. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.938895 · Cited by 21

High Bacillary Burden and the ESX-1 Type VII Secretion System Promote MHC Class I Presentation by Mycobacterium tuberculosis–Infected Macrophages to CD8 T Cells

Mott, D., Yang, J. D., Baer, C. E., Papavinasasundaram, K. G., Sassetti, C. M., & Behar, S. M. (2023) · The Journal of Immunology · doi:10.4049/jimmunol.2300001 · Cited by 20

A multi-level multi-scale approach to study essential genes in Mycobacterium tuberculosis

Ghosh, S., Baloni, P., Mukherjee, S., Anand, P., & Chandra, N. R. (2013) · BMC Systems Biology · doi:10.1186/1752-0509-7-132 · Cited by 19

Phenylalanine-Rich Peptides Potently Bind ESAT6, a Virulence Determinant of Mycobacterium tuberculosis, and Concurrently Affect the Pathogen's Growth

Kumar, K., Tharad, M., Ganapathy, S., Ram, G., Narayan, A., Khan, J. A., Pratap, R., Ghosh, A., Samuchiwal, S. K., Kumar, S., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007615 · Cited by 19

Multiple variants of the type VII secretion system in Gram-positive bacteria

Garrett, S., Higginson, A. B., & Palmer, T. (2024) · microLife · doi:10.1093/femsml/uqae013 · Cited by 19

Generation of Mycobacterium tuberculosis-specific recombinant antigens and evaluation of the clinical value of antibody detection for serological diagnosis of pulmonary tuberculosis

ZHANG, X., Su, Z., ZHANG, X., Hu, C., Yu, J., Gao, Q., & Wang, H. (2013) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2013.1254 · Cited by 18

Understanding dissemination of Mycobacterium tuberculosis from the lungs during primary infection

Ryndak, M. B., Chandra, D., & Laal, S. (2016) · Journal of Medical Microbiology · doi:10.1099/jmm.0.000238 · Cited by 20

Cyclic di-AMP-mediated interaction between Mycobacterium tuberculosis ΔcnpB and macrophages implicates a novel strategy for improving BCG vaccination

Zhang, Y., Yang, J., & Bai, G. (2018) · Pathogens and Disease · doi:10.1093/femspd/fty008 · Cited by 18

A systematic approach to simultaneously evaluate safety, immunogenicity, and efficacy of novel tuberculosis vaccination strategies

Muruganandah, V., Sathkumara, H. D., Pai, S., Rush, C. M., Brosch, R., Waardenberg, A. J., & Kupz, A. (2020) · Science Advances · doi:10.1126/sciadv.aaz1767 · Cited by 19

An N-acetyltransferase required for ESAT-6 N-terminal acetylation and virulence in Mycobacterium marinum

Collars, O. A., Jones, B. S., Hu, D. D., Weaver, S. D., Sherman, T. A., Champion, M. M., & Champion, P. A. D. (2023) · mBio · doi:10.1128/mbio.00987-23 · Cited by 18

Immunomagnetic Isolation of Pathogen‐Containing Phagosomes and Apoptotic Blebs from Primary Phagocytes

Steinhäuser, C., Dallenga, T. K., Tchikov, V., Schaible, U. E., Schütze, S., & Reiling, N. (2014) · Current Protocols in Immunology · doi:10.1002/0471142735.im1436s105 · Cited by 20

LpqM, a Mycobacterial Lipoprotein-Metalloproteinase, Is Required for Conjugal DNA Transfer inMycobacterium smegmatis

Nguyen, K. T., Piastro, K., & Derbyshire, K. M. (2009) · Journal of Bacteriology · doi:10.1128/jb.00024-09 · Cited by 18

The PE and PPE Protein Families ofMycobacterium tuberculosis

Delogu, G., Cole, S. T., & Brosch, R. (2008) · Wiley eBooks · doi:10.1002/9783527611614.ch7 · Cited by 18

A Three-Hybrid System to Probe In Vivo Protein-Protein Interactions: Application to the Essential Proteins of the RD1 Complex of M. tuberculosis

Tharad, M., Samuchiwal, S. K., Bhalla, K., Ghosh, A., Kumar, K., Kumar, S., & Ranganathan, A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027503 · Cited by 17

ESX-3 secretion system in Mycobacterium: An overview

Granados-Tristán, A. L., Hernández-Luna, C. E., González-Escalante, L. A., Camacho-Moll, M. E., Silva-Ramírez, B., de León, M. B., & Peñuelas-Urquides, K. (2023) · Biochimie · doi:10.1016/j.biochi.2023.10.013 · Cited by 19

Interbacterial competition mediated by the type VIIb secretion system

Boardman, E., Palmer, T., & Alcock, F. (2023) · Microbiology · doi:10.1099/mic.0.001420 · Cited by 17

Evaluation of the anti-tuberculosis activity generated by different multigene DNA vaccine constructs

Sali, M., Clarizio, S., Pusceddu, C., Zumbo, A., Pecorini, G., Rocca, S., Zanetti, S., Delogu, G., & Fadda, G. (2008) · Microbes and Infection · doi:10.1016/j.micinf.2008.02.012 · Cited by 17

The RD1 locus in theMycobacterium tuberculosisgenome contributes to the maturation and secretion of IL-1α from infected macrophages through the elevation of cytoplasmic calcium levels and calpain activation

Yang, R., Chen, X., Dewamitta, S. R., Sakai, S., Tsuchiya, K., Hara, H., Shen, Y., Qu, H., Fang, R., Mitsuyama, M., et al. (2013) · Pathogens and Disease · doi:10.1111/2049-632x.12075 · Cited by 17

A metabolomics investigation of the function of the ESX-1 gene cluster in mycobacteria

Loots, D. T., Swanepoel, C. C., Newton-Foot, M., & van Pittius, N. C. G. (2016) · Microbial Pathogenesis · doi:10.1016/j.micpath.2016.10.008 · Cited by 17

A computational model of ESAT-6 complex in membrane

Karki, C. B., Xian, Y., Xie, Y., Sun, S., Lopez-Hernandez, A. E., Juarez, B. Y., Wang, J., Sun, J., & Li, L. (2020) · Journal of Theoretical and Computational Chemistry · doi:10.1142/s0219633620400027 · Cited by 17

Advances in the development of molecular genetic tools for Mycobacterium tuberculosis

Chhotaray, C., Tan, Y., Mugweru, J., Islam, M. M., Hameed, H. M. A., Wang, S., Lu, Z., Wang, C., Li, X., Tan, S., et al. (2018) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2018.06.003 · Cited by 17

Mycobacterium marinum down-regulates miR-148a in macrophages in an EsxA-dependent manner

Wu, H., Bao, Y., Wang, L., Li, X., & Sun, J. (2019) · International Immunopharmacology · doi:10.1016/j.intimp.2019.04.056 · Cited by 18

Characterization of human cellular immune responses toMycobacterium tuberculosisproteins encoded by genes predicted in RD15 genomic region that is absent inMycobacterium bovisBCG

Al‐Attiyah, R., & Mustafa, A. S. (2010) · FEMS Immunology & Medical Microbiology · doi:10.1111/j.1574-695x.2010.00677.x · Cited by 17

Developing whole mycobacteria cell vaccines for tuberculosis: Workshop proceedings, Max Planck Institute for Infection Biology, Berlin, Germany, July 9, 2014

Whole Mycobacteria Cell Vaccines for Tuberculosis Summary Group (2015) · Vaccine · doi:10.1016/j.vaccine.2015.03.056 · Cited by 16

Mycobacterium tuberculosis ESAT6 modulates host innate immunity by downregulating miR-222-3p target PTEN

Zonghai, C., Luò, T., Ma, P., Ge, L., Rongchuan, Z., Xinyan, W., Ni, W.-Y., Wei, L., Wang, Y., & Lang, B. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2021.166292 · Cited by 17

Mycobacterium tuberculosis Genes Involved in Regulation of Host Cell Death

Briken, V. (2013) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-6111-1_5 · Cited by 19

Mycobacterial Shuttle Vectors Designed for High-Level Protein Expression in Infected Macrophages

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

Tuberculosis vaccine development: research, regulatory and clinical strategies

Brennan, M. J., Morris, S. L., & Sizemore, C. F. (2004) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.4.9.1493 · Cited by 16

Real-time visualization reveals Mycobacterium tuberculosis ESAT-6 disrupts phagosome-like compartment via fibril-mediated vesiculation

Koiri, D., Nandi, M., Abik Hameem, P. M., Bhausaheb, A. J., Kumar, A., Behura, A., Meher, G., Choudhary, V., Choubey, S., & Saleem, M. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115328 · Cited by 17

Exploiting the mycobacterial cell wall to design improved vaccines against tuberculosis

Morandi, M., Sali, M., Manganelli, R., & Delogu, G. (2013) · The Journal of Infection in Developing Countries · doi:10.3855/jidc.3114 · Cited by 15

Effects of membrane lipid composition on Mycobacterium tuberculosis EsxA membrane insertion: A dual play of fluidity and charge

Ray, S., Reyes, S. V., Xiao, C., & Sun, J. (2019) · Tuberculosis · doi:10.1016/j.tube.2019.07.005 · Cited by 16

The Mycobacterium tuberculosis PhoPR virulence system regulates expression of the universal second messenger c-di-AMP and impacts vaccine safety and efficacy

Pérez, I., Campos‐Pardos, E., Díaz, C., Uranga, S., Sayes, F., Vicente, F., Aguiló, N., Brosch, R., Martı́n, C., & Gonzalo‐Asensio, J. (2022) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2022.02.011 · Cited by 17

Plasma CXCL8 and MCP-1 as surrogate plasma biomarkers of latent tuberculosis infection among household contacts–A cross-sectional study

Selvavinayagam, S. T., Aswathy, B., Yong, Y. K., Frederick, A., Murali, L., Kalaivani, V., Karishma, S. J., Rajeshkumar, M., Anusree, A., Kannan, M., et al. (2023) · PLOS Global Public Health · doi:10.1371/journal.pgph.0002327 · Cited by 15

How do mycobacteria activate CD8+ T cells?

Weerdenburg, E. M., Peters, P. J., & van der Wel, N. N. (2009) · Trends in Microbiology · doi:10.1016/j.tim.2009.10.004 · Cited by 16

Demonstration of In vivo Expression of a Hypothetical Open Reading Frame (ORF‐14) Encoded by the RD1 Region of Mycobacterium tuberculosis

Amoudy, H. A., Ahmad, S., Thole, J. E. R., & Mustafa, A. S. (2007) · Scandinavian Journal of Immunology · doi:10.1111/j.1365-3083.2007.01961.x · Cited by 15

The role of Mycobacterium tuberculosis complex species on apoptosis and necroptosis state of macrophages derived from active pulmonary tuberculosis patients

Yanti, B., Mulyadi, M., Amin, M., Harapan, H., Mertaniasih, N. M., & Soetjipto, S. (2020) · BMC Research Notes · doi:10.1186/s13104-020-05256-2 · Cited by 15

Impact of proteomics on anti-Mycobacterium tuberculosis (MTB) vaccine development.

Jagusztyn-Krynicka, E. K., Roszczenko, P., & Grabowska, A. D. (2009) · PubMed · Cited by 15

DisconnectingIn VitroESX-1 Secretion from Mycobacterial Virulence

Champion, P. A. D. (2013) · Journal of Bacteriology · doi:10.1128/jb.01145-13 · Cited by 15

Editorial: Cellular and Molecular Mechanisms of Mycobacterium tuberculosis Virulence

Sun, J., Champion, P. A. D., & Bigi, F. (2019) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2019.00331 · Cited by 15

Polarly Localized EccE 1 Is Required for ESX-1 Function and Stabilization of ESX-1 Membrane Proteins in Mycobacterium tuberculosis

Soler-Arnedo, P., Sala, C., Zhang, M., Cole, S. T., & Piton, J. (2019) · Journal of Bacteriology · doi:10.1128/jb.00662-19 · Cited by 15

ESAT-6 Protein of Mycobacterium tuberculosis Increases Holotransferrin-Mediated Iron Uptake in Macrophages by Downregulating Surface Hemochromatosis Protein HFE

Jha, V., Pal, R. K., Kumar, D., & Mukhopadhyay, S. (2020) · The Journal of Immunology · doi:10.4049/jimmunol.1801357 · Cited by 14

ESX1-dependent fractalkine mediates chemotaxis and Mycobacterium tuberculosis infection in humans

Hingley‐Wilson, S., Connell, D. W., Pollock, K. M., Hsu, T., Tchilian, E. Z., Sykes, A., Grass, L., Potiphar, L., Bremang, S., Kon, O. M., et al. (2014) · Tuberculosis · doi:10.1016/j.tube.2014.01.004 · Cited by 14

Immune-evasion Strategies of Mycobacteria and Their Implications for the Protective Immune Response

Fraga, A. G., Barbosa, A. M., Ferreira, C. M., Fevereiro, J., Pedrosa, J., & Torrado, E. (2017) · Current Issues in Molecular Biology · doi:10.21775/cimb.025.169 · Cited by 14

Progress in understanding the human immune responses to Mycobacterium tuberculosis

Barnes, P. F., Samten, B., Shams, H., & Vankayalapatib, R. (2009) · Tuberculosis · doi:10.1016/s1472-9792(09)70004-6 · Cited by 14

Mycobacterium tuberculosis secreted protein ESAT-6 interacts with the human protein syntenin-1

SCHUMANN, G., Schleier, S., Rosenkrands, I., Nehmann, N., Hälbich, S., Zipfel, P. F., de Jonge, M. I., Cole, S. T., Münder, T., & Möllmann, U. (2006) · Open Life Sciences · doi:10.2478/s11535-006-0018-2 · Cited by 14

Characteristic genes in THP‑1 derived macrophages infected with Mycobacterium tuberculosis H37Rv strain identified by integrating bioinformatics methods

Zhang, Y., Lin, Y., Yu, H., Tian, R., & Li, F. (2019) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2019.4293 · Cited by 14

The loss of the PDIM/PGL virulence lipids causes differential secretion of ESX-1 substrates in Mycobacterium marinum

Jones, B. S., Hu, D. D., Nicholson, K. R., Cronin, R. M., Weaver, S. D., Champion, M. M., & Champion, P. A. D. (2024) · mSphere · doi:10.1128/msphere.00005-24 · Cited by 13

Elimination of intracellularly residingMycobacterium tuberculosisthrough targeting of host and bacterial signaling mechanisms

Jayachandran, R., Scherr, N., & Pieters, J. (2012) · Expert Review of Anti-infective Therapy · doi:10.1586/eri.12.95 · Cited by 14

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

MyBASE: a database for genome polymorphism and gene function studies of Mycobacterium

Zhu, X., Chang, S., Fang, K., Cui, S., Liu, J., Wu, Z., Yu, X., Gao, G. F., Yang, H., Zhu, B., et al. (2009) · BMC Microbiology · doi:10.1186/1471-2180-9-40 · Cited by 13

Early Secreted Antigenic Target of 6 kD a of Mycobacterium tuberculosis Stimulates Macrophage Chemoattractant Protein‐1 Production by Macrophages and Its Regulation by p38 Mitogen‐Activated Protein Kinases and Interleukin‐4

Ma, J., Jung, B., Yi, N., & Samten, B. (2016) · Scandinavian Journal of Immunology · doi:10.1111/sji.12447 · Cited by 13

Mycobacterium tuberculosis effectors involved in host–pathogen interaction revealed by a multiple scales integrative pipeline

Li, W., Fan, X., Long, Q., Xie, L., & Xie, J. (2015) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2015.02.014 · Cited by 13

Autophagy and Bacterial infections

Cadwell, K., Abraham, C., Bel, S., Chauhan, S., Coers, J., Colombo, M. I., Davis, J. R., Hofius, D., Nguyen, H. T. T., Ogawa, M., et al. (2025) · Autophagy Reports · doi:10.1080/27694127.2025.2542904 · Cited by 12

Intragranuloma Accumulation and Inflammatory Differentiation of Neutrophils Underlie Mycobacterial ESX-1-Dependent Immunopathology

Lienard, J., Munke, K., Wulff, L., Silva, C. D., Vandamme, J., Laschanzky, K., Joeris, T., Agace, W. W., & Carlsson, F. (2023) · mBio · doi:10.1128/mbio.02764-22 · Cited by 13

Phosphorylation of CFP10 modulates Mycobacterium tuberculosis virulence

Malakar, B., Chauhan, K., Sanyal, P., Naz, S., Kalam, H., Vivek-Ananth, R. P., Singh, L. V., Samal, A., Kumar, D., & Nandicoori, V. K. (2023) · mBio · doi:10.1128/mbio.01232-23 · Cited by 12

Insight into the drug resistance whole genome of Mycobacterium tuberculosis isolates from Khyber Pakhtunkhwa, Pakistan

Khan, M. T., Ali, S., Khan, A. S., Ali, A., Khan, A., Kaushik, A. C., Irfan, M., Chinnasamy, S., Zhang, S., Zhang, Y., et al. (2021) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2021.104861 · Cited by 12

IMB-BZ as an Inhibitor Targeting ESX-1 Secretion System to Control Mycobacterial Infection

Jia, P., Zhang, Y., Xu, J., Zhu, M., Peng, S., Zhang, Y., Zhao, J., Li, X., Mi, K., Yan, D., et al. (2021) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiab486 · Cited by 12

Effect of serial subculturing on the genetic composition and cytotoxicactivity of Mycobacterium tuberculosis

Molina-Torres, C. A., Castro‐Garza, J., Ocampo‐Candiani, J., Monot, M., Cole, S. T., & Cabrera, L. V. (2010) · Journal of Medical Microbiology · doi:10.1099/jmm.0.015966-0 · Cited by 12

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

An exit strategy for the tubercle bacillus?

Hingley‐Wilson, S., & Lalvani, A. (2008) · Nature Reviews Microbiology · doi:10.1038/nrmicro1821-c1 · Cited by 1

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

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

Region of Difference 2 Contributes to Virulence ofMycobacterium tuberculosis

Kozak, R. A., Alexander, D. C., Liao, R., Sherman, D. R., & Behr, M. A. (2010) · Infection and Immunity · doi:10.1128/iai.00824-10 · Cited by 43