{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,21]],"date-time":"2026-10-21T16:38:06Z","timestamp":1792600686329,"version":"4.5.0"},"reference-count":37,"publisher":"MyJove Corporation","issue":"216","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["JoVE"],"DOI":"10.3791\/67745","type":"journal-article","created":{"date-parts":[[2025,2,28]],"date-time":"2025-02-28T19:00:26Z","timestamp":1740769226000},"source":"Crossref","is-referenced-by-count":0,"title":["Fluorescence Assays for the Study of <em>Mycobacterium tuberculosis<\/em> Interaction with the Immune Receptor SLAMF1"],"prefix":"10.3791","author":[{"given":"Angela Mar\u00eda","family":"Barbero","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rodrigo Emanuel","family":"Hern\u00e1ndez Del Pino","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ver\u00f3nica Edith","family":"Garc\u00eda","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Virginia","family":"Pasquinelli","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"2098","published-online":{"date-parts":[[2025,2,28]]},"reference":[{"key":"ref1","volume-title":"Global Tuberculosis Report 2023","year":"2023","unstructured":"World Health Organization. Global Tuberculosis Report 2023. Available at: https:\/\/www.who.int\/tb\/publications\/global_report\/en\/ (2023)."},{"key":"ref2","doi-asserted-by":"crossref","first-page":"882130","DOI":"10.3389\/fimmu.2022.747799","type":"journal-article","article-title":"Macrophage: A cell with many faces and functions in tuberculosis","volume":"13","author":"Ahmad","year":"2022","unstructured":"Ahmad, F. et al. Macrophage: A cell with many faces and functions in tuberculosis. Front Immunol. 13, 882130 (2022).","journal-title":"Front Immunol"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"1187205","DOI":"10.3389\/fcimb.2023.1062963","type":"journal-article","article-title":"Mycobacterium tuberculosis-macrophage interaction: Molecular updates","volume":"13","author":"Bo","year":"2023","unstructured":"Bo, H. et al. Mycobacterium tuberculosis-macrophage interaction: Molecular updates. Front Cell Infect Microbiol. 13, 1187205 (2023).","journal-title":"Front Cell Infect Microbiol"},{"issue":"5","key":"ref4","doi-asserted-by":"crossref","first-page":"e0198069","DOI":"10.1371\/journal.pone.0198221","type":"journal-article","article-title":"AmpliSeq transcriptome analysis of human alveolar and monocyte-derived macrophages over time in response to Mycobacterium tuberculosis infection","volume":"13","author":"Papp","year":"2018","unstructured":"Papp, A. C. et al. AmpliSeq transcriptome analysis of human alveolar and monocyte-derived macrophages over time in response to Mycobacterium tuberculosis infection. PLoS One. 13 (5), e0198069 (2018).","journal-title":"PLoS One"},{"issue":"2","key":"ref5","doi-asserted-by":"crossref","first-page":"340","DOI":"10.3390\/ijms20020340","type":"journal-article","article-title":"The immune escape mechanisms of Mycobacterium tuberculosis","volume":"20","author":"Zhai","year":"2019","unstructured":"Zhai, W., Wu, F., Zhang, Y., Fu, Y., Liu, Z. The immune escape mechanisms of Mycobacterium tuberculosis. Int J Mol Sci. 20 (2), 340 (2019).","journal-title":"Int J Mol Sci"},{"issue":"2","key":"ref6","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1128\/CMR.15.2.294-309.2002","type":"journal-article","article-title":"Innate immunity to Mycobacterium tuberculosis","volume":"15","author":"Van Crevel","year":"2002","unstructured":"Van Crevel, R., Ottenhoff, T. H. M., Van der Meer, J. W. M. Innate immunity to Mycobacterium tuberculosis. Clin Microbiol Rev. 15 (2), 294-309 (2002).","journal-title":"Clin Microbiol Rev"},{"issue":"1","key":"ref7","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s10875-014-0103-7","type":"journal-article","article-title":"Interaction of pattern recognition receptors with Mycobacterium tuberculosis","volume":"35","author":"Mortaz","year":"2015","unstructured":"Mortaz, E. et al. Interaction of pattern recognition receptors with Mycobacterium tuberculosis. J Clin Immunol. 35 (1), 1-10 (2015).","journal-title":"J Clin Immunol"},{"issue":"1","key":"ref8","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1111\/imr.12263","type":"journal-article","article-title":"Sensing of Mycobacterium tuberculosis and consequences to both host and bacillus","volume":"264","author":"Stamm","year":"2015","unstructured":"Stamm, C. E., Collins, A. C., Shiloh, M. U. Sensing of Mycobacterium tuberculosis and consequences to both host and bacillus. Immunol Rev. 264 (1), 204-219 (2015).","journal-title":"Immunol Rev"},{"issue":"10","key":"ref9","doi-asserted-by":"crossref","first-page":"e20636","DOI":"10.1016\/j.heliyon.2023.e20636","type":"journal-article","article-title":"Role of pattern recognition receptors in sensing Mycobacterium tuberculosis","volume":"9","author":"Zihad","year":"2023","unstructured":"Zihad, S. M. N. K. et al. Role of pattern recognition receptors in sensing Mycobacterium tuberculosis. Heliyon. 9 (10), e20636 (2023).","journal-title":"Heliyon"},{"issue":"8","key":"ref10","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1002\/JLB.4MA0820-655RR","type":"journal-article","article-title":"SLAMF1 signaling induces Mycobacterium tuberculosis uptake leading to endolysosomal maturation in human macrophages","volume":"109","author":"Barbero","year":"2021","unstructured":"Barbero, A. M. et al. SLAMF1 signaling induces Mycobacterium tuberculosis uptake leading to endolysosomal maturation in human macrophages. J Leukoc Biol. 109 (8), 257-273 (2021).","journal-title":"J Leukoc Biol"},{"issue":"2","key":"ref11","doi-asserted-by":"crossref","first-page":"1177","DOI":"10.4049\/jimmunol.172.2.1177","type":"journal-article","article-title":"Expression of signaling lymphocytic activation molecule-associated protein interrupts IFN-\u03b3 production in human tuberculosis","volume":"172","author":"Pasquinelli","year":"2004","unstructured":"Pasquinelli, V. et al. Expression of signaling lymphocytic activation molecule-associated protein interrupts IFN-\u03b3 production in human tuberculosis. J Immunol. 172 (2), 1177-1185 (2004).","journal-title":"J Immunol"},{"issue":"2","key":"ref12","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1093\/infdis\/jis672","type":"journal-article","article-title":"Phosphorylation of mitogen-activated protein kinases contributes to interferon-\u03b3 production in response to Mycobacterium tuberculosis","volume":"207","author":"Pasquinelli","year":"2012","unstructured":"Pasquinelli, V. et al. Phosphorylation of mitogen-activated protein kinases contributes to interferon-\u03b3 production in response to Mycobacterium tuberculosis. J Infect Dis. 207 (2), 340-350 (2012).","journal-title":"J Infect Dis"},{"issue":"5","key":"ref13","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1086\/596742","type":"journal-article","article-title":"IFN-\u03b3 production during active tuberculosis is regulated by mechanisms that involve IL-17, SLAM, and CREB","volume":"199","author":"Pasquinelli","year":"2009","unstructured":"Pasquinelli, V. et al. IFN-\u03b3 production during active tuberculosis is regulated by mechanisms that involve IL-17, SLAM, and CREB. J Infect Dis. 199 (5), 661-665 (2009).","journal-title":"J Infect Dis"},{"issue":"2","key":"ref14","first-page":"423","type":"journal-article","article-title":"Neutrophil autophagy during human active tuberculosis is modulated by SLAMF1","volume":"17","author":"Pellegrini","year":"2021","unstructured":"Pellegrini, J. M. et al. Neutrophil autophagy during human active tuberculosis is modulated by SLAMF1. Autophagy. 17 (2), 423-426 (2021).","journal-title":"Autophagy"},{"issue":"6","key":"ref15","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1016\/j.ijmm.2015.07.006","type":"journal-article","article-title":"Signaling lymphocyte-activation molecule SLAMF1 augments mycobacteria BCG-induced inflammatory response and facilitates bacterial clearance","volume":"305","author":"Song","year":"2015","unstructured":"Song, T., Dong, C., Xiong, S. Signaling lymphocyte-activation molecule SLAMF1 augments mycobacteria BCG-induced inflammatory response and facilitates bacterial clearance. Int J Med Microbiol. 305 (6), 572-580 (2015).","journal-title":"Int J Med Microbiol"},{"issue":"132","key":"ref16","first-page":"e57032","type":"journal-article","article-title":"Titration ELISA as a method to determine the dissociation constant of receptor-ligand interaction","author":"Eble","year":"2018","unstructured":"Eble, J. A. Titration ELISA as a method to determine the dissociation constant of receptor-ligand interaction. J Vis Exp. 132, e57032 (2018).","journal-title":"J Vis Exp"},{"issue":"1","key":"ref17","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.bbamem.2013.04.028","type":"journal-article","article-title":"Surface plasmon resonance spectroscopy for characterization of membrane protein-ligand interactions and its potential for drug discovery","volume":"1838","author":"Patching","year":"2014","unstructured":"Patching, S. G. Surface plasmon resonance spectroscopy for characterization of membrane protein-ligand interactions and its potential for drug discovery. Biochim Biophys Acta Biomembr. 1838 (1), 43-55 (2014).","journal-title":"Biochim Biophys Acta Biomembr"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"296","DOI":"10.1016\/j.jpba.2013.09.003","type":"journal-article","article-title":"Isothermal titration calorimetry in membrane protein research","volume":"87","author":"Draczkowski","year":"2014","unstructured":"Draczkowski, P., Matosiuk, D., Jozwiak, K. Isothermal titration calorimetry in membrane protein research. J Pharm Biomed Anal. 87, 296-304 (2014).","journal-title":"J Pharm Biomed Anal"},{"issue":"5","key":"ref19","doi-asserted-by":"crossref","first-page":"1499","DOI":"10.1007\/s00216-008-1897-z","type":"journal-article","article-title":"Fluorescence polarization immunoassays and related methods for simple, high-throughput screening of small molecules","volume":"391","author":"Smith","year":"2008","unstructured":"Smith, D. S., Eremin, S. A. Fluorescence polarization immunoassays and related methods for simple, high-throughput screening of small molecules. Anal Bioanal Chem. 391 (5), 1499-1507 (2008).","journal-title":"Anal Bioanal Chem"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1146\/annurev-pharmtox-010919-023545","type":"journal-article","article-title":"Cryo-electron microscopy: Moving beyond X-ray crystal structures for drug receptors and drug development","volume":"60","author":"Garc\u00eda-Nafr\u00eda","year":"2020","unstructured":"Garc\u00eda-Nafr\u00eda, J., Tate, C. G. Cryo-electron microscopy: Moving beyond X-ray crystal structures for drug receptors and drug development. Annu Rev Pharmacol Toxicol. 60, 51-71 (2020).","journal-title":"Annu Rev Pharmacol Toxicol"},{"issue":"4","key":"ref21","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1002\/pro.4043","type":"journal-article","article-title":"Structural and functional understanding of the toll-like receptors","volume":"30","author":"Asami","year":"2021","unstructured":"Asami, J., Shimizu, T. Structural and functional understanding of the toll-like receptors. Protein Sci. 30 (4), 761-772 (2021).","journal-title":"Protein Sci"},{"issue":"6","key":"ref22","doi-asserted-by":"crossref","first-page":"683","DOI":"10.1139\/bcb-2021-0052","type":"journal-article","article-title":"On-cell nuclear magnetic resonance spectroscopy to probe cell surface interactions","volume":"99","author":"Ph\u1ea1m","year":"2021","unstructured":"Ph\u1ea1m, T. T. T., Rainey, J. K. On-cell nuclear magnetic resonance spectroscopy to probe cell surface interactions. Biochem Cell Biol. 99 (6), 683-692 (2021).","journal-title":"Biochem Cell Biol"},{"issue":"4","key":"ref23","doi-asserted-by":"crossref","first-page":"045001","DOI":"10.1088\/2050-6120\/ac82a6","type":"journal-article","article-title":"Microscale thermophoresis as a powerful growing analytical technique for the investigation of biomolecular interaction and the determination of binding parameters","volume":"10","author":"El Deeb","year":"2022","unstructured":"El Deeb, S. et al. Microscale thermophoresis as a powerful growing analytical technique for the investigation of biomolecular interaction and the determination of binding parameters. Methods Appl Fluoresc. 10 (4), 045001 (2022).","journal-title":"Methods Appl Fluoresc"},{"issue":"3","key":"ref24","doi-asserted-by":"crossref","first-page":"505","DOI":"10.3390\/molecules24030537","type":"journal-article","article-title":"Bioluminescence resonance energy transfer as a method to study protein-protein interactions: Application to G protein-coupled receptor biology","volume":"24","author":"El Khamlichi","year":"2019","unstructured":"El Khamlichi, C. et al. Bioluminescence resonance energy transfer as a method to study protein-protein interactions: Application to G protein-coupled receptor biology. Molecules. 24 (3), 505 (2019).","journal-title":"Molecules"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/B978-0-12-801430-1.00005-6","type":"journal-article","article-title":"Tools and techniques to study ligand-receptor interactions and receptor activation by TNF superfamily members","volume":"545","author":"Schneider","year":"2014","unstructured":"Schneider, P., Willen, L., Smulski, C.R. Tools and techniques to study ligand-receptor interactions and receptor activation by TNF superfamily members. Methods Enzymol. 545, 103-125 (2014).","journal-title":"Methods Enzymol"},{"issue":"1","key":"ref26","first-page":"74","type":"journal-article","article-title":"Atomic force microscopy: A multifaceted tool to study membrane proteins and their interactions with ligands","volume":"1838","author":"Park","year":"2014","unstructured":"Park, A. M. W., Schirmer, P. S. H. Atomic force microscopy: A multifaceted tool to study membrane proteins and their interactions with ligands. Biochim Biophys Acta Biomembr. 1838 (1), 74-89 (2014).","journal-title":"Biochim Biophys Acta Biomembr"},{"issue":"9","key":"ref27","doi-asserted-by":"crossref","first-page":"183","DOI":"10.3390\/jimaging9090192","type":"journal-article","article-title":"Unravelling the mystery inside cells by using single-molecule fluorescence imaging","volume":"9","author":"Zalejski","year":"2023","unstructured":"Zalejski, J., Sun, J., Sharma, A. Unravelling the mystery inside cells by using single-molecule fluorescence imaging. J Imaging. 9 (9), 183 (2023).","journal-title":"J Imaging"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"1075587","DOI":"10.3389\/fmolb.2023.1154074","type":"journal-article","article-title":"Two-dimensional measurements of receptor-ligand interactions","volume":"10","author":"Zheng","year":"2023","unstructured":"Zheng, S., Zou, M., Shao, Y., Wu, H., Wang, X. Two-dimensional measurements of receptor-ligand interactions. Front Mol Biosci. 10, 1075587 (2023).","journal-title":"Front Mol Biosci"},{"issue":"1","key":"ref29","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1134\/S0006297922010059","type":"journal-article","article-title":"Computer simulation of the receptor-ligand interactions of mannose receptor CD206 in comparison with the lectin concanavalin A model","volume":"87","author":"Zlotnikov","year":"2022","unstructured":"Zlotnikov, I. D., Kudryashova, E. V. Computer simulation of the receptor-ligand interactions of mannose receptor CD206 in comparison with the lectin concanavalin A model. Biochemistry (Moscow). 87 (1), 54-69 (2022).","journal-title":"Biochemistry (Moscow)"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"7604567","DOI":"10.1155\/2018\/3502514","type":"journal-article","article-title":"Insights into the molecular mechanisms of protein-ligand interactions by molecular docking and molecular dynamics simulation: A case of oligopeptide binding protein","volume":"2018","author":"Fu","year":"2018","unstructured":"Fu, Y., Zhao, J., Chen, Z. Insights into the molecular mechanisms of protein-ligand interactions by molecular docking and molecular dynamics simulation: A case of oligopeptide binding protein. Comput Math Methods Med. 2018, 7604567 (2018).","journal-title":"Comput Math Methods Med"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"3303","DOI":"10.1016\/j.csbj.2021.05.047","type":"journal-article","article-title":"A novel approach for studying receptor-ligand interactions on living cells' surface by using NUS\/T1\u03c1-NMR methodologies combined with computational techniques: The RGDechi15D-\u03b1v\u03b25 integrin complex","volume":"19","author":"Farina","year":"2021","unstructured":"Farina, B. et al. A novel approach for studying receptor-ligand interactions on living cells' surface by using NUS\/T1\u03c1-NMR methodologies combined with computational techniques: The RGDechi15D-\u03b1v\u03b25 integrin complex. Comput Struct Biotechnol J. 19, 3303-3318 (2021).","journal-title":"Comput Struct Biotechnol J"},{"issue":"10","key":"ref32","doi-asserted-by":"crossref","first-page":"4538","DOI":"10.1128\/IAI.01256-08","type":"journal-article","article-title":"Role of phosphatidylinositol mannosides in the interaction between mycobacteria and DC-SIGN","volume":"77","author":"Driessen","year":"2009","unstructured":"Driessen, N. N. et al. Role of phosphatidylinositol mannosides in the interaction between mycobacteria and DC-SIGN. Infect Immun. 77 (10), 4538-4547 (2009).","journal-title":"Infect Immun"},{"issue":"47","key":"ref33","doi-asserted-by":"crossref","first-page":"36511","DOI":"10.1074\/jbc.M110.158055","type":"journal-article","article-title":"Src homology 3-interacting domain of Rv1917c of Mycobacterium tuberculosis induces selective maturation of human dendritic cells by regulating PI3K-MAPK-NF-\u03baB signaling and drives Th2 immune responses","volume":"285","author":"Bansal","year":"2010","unstructured":"Bansal, K. et al. Src homology 3-interacting domain of Rv1917c of Mycobacterium tuberculosis induces selective maturation of human dendritic cells by regulating PI3K-MAPK-NF-\u03baB signaling and drives Th2 immune responses. J Biol Chem. 285 (47), 36511-36522 (2010).","journal-title":"J Biol Chem"},{"issue":"6","key":"ref34","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1007\/s00109-014-1243-1","type":"journal-article","article-title":"PPE57 induces activation of macrophages and drives Th1-type immune responses through TLR2","volume":"93","author":"Xu","year":"2015","unstructured":"Xu, Y. et al. PPE57 induces activation of macrophages and drives Th1-type immune responses through TLR2. J Mol Med. 93 (6), 645-662 (2015).","journal-title":"J Mol Med"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1038\/sj.gene.6364410","type":"journal-article","article-title":"DC-SIGN (CD209), pentraxin 3 and vitamin D receptor gene variants associate with pulmonary tuberculosis risk in West Africans","volume":"8","author":"Olesen","year":"2007","unstructured":"Olesen, R. et al. DC-SIGN (CD209), pentraxin 3 and vitamin D receptor gene variants associate with pulmonary tuberculosis risk in West Africans. Genes Immun. 8, 456-467 (2007).","journal-title":"Genes Immun"},{"issue":"10","key":"ref36","doi-asserted-by":"crossref","first-page":"920","DOI":"10.1038\/ni.1931","type":"journal-article","article-title":"SLAM is a microbial sensor that regulates bacterial phagosome functions in macrophages","volume":"11","author":"Berger","year":"2010","unstructured":"Berger, S. B. et al. SLAM is a microbial sensor that regulates bacterial phagosome functions in macrophages. Nat Immunol. 11 (10), 920-927 (2010).","journal-title":"Nat Immunol"},{"issue":"4","key":"ref37","doi-asserted-by":"crossref","first-page":"e13156","DOI":"10.1111\/cmi.13164","type":"journal-article","article-title":"Omp25-dependent engagement of SLAMF1 by Brucella abortus in dendritic cells limits acute inflammation and favours bacterial persistence in vivo","volume":"22","author":"Degos","year":"2020","unstructured":"Degos, C. et al. Omp25-dependent engagement of SLAMF1 by Brucella abortus in dendritic cells limits acute inflammation and favours bacterial persistence in vivo. Cell Microbiol. 22 (4), e13156 (2020).","journal-title":"Cell Microbiol"}],"container-title":["Journal of Visualized Experiments"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/app.jove.com\/t\/67745\/fluorescence-assays-for-study-mycobacterium-tuberculosis-interaction","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,10,21]],"date-time":"2026-10-21T15:38:00Z","timestamp":1792597080000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.jove.com\/t\/67745\/fluorescence-assays-for-study-mycobacterium-tuberculosis-interaction"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,2,28]]},"references-count":37,"journal-issue":{"issue":"216","published-online":{"date-parts":[[2025]]}},"URL":"https:\/\/doi.org\/10.3791\/67745","relation":{},"ISSN":["1940-087X"],"issn-type":[{"value":"1940-087X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,2,28]]}}}