Inflammatory signaling in human tuberculosis granulomas is spatially organized (original) (raw)
World Health Organization. World Health Organization tuberculosis fact sheet no. 104 (World Health Organization, 2015).
Taylor, J.L. et al. Role for matrix metalloproteinase 9 in granuloma formation during pulmonary Mycobacterium tuberculosis infection. Infect. Immun.74, 6135–6144 (2006). ArticleCASPubMedPubMed Central Google Scholar
Volkman, H.E. et al. Tuberculous granuloma induction via interaction of a bacterial secreted protein with host epithelium. Science327, 466–469 (2010). ArticleCASPubMed Google Scholar
Ulrichs, T. et al. Human tuberculous granulomas induce peripheral lymphoid follicle-like structures to orchestrate local host defense in the lung. J. Pathol.204, 217–228 (2004). ArticlePubMed Google Scholar
Ehlers, S. & Schaible, U.E. The granuloma in tuberculosis: dynamics of a host–pathogen collusion. Front. Immunol.3, 411 (2012). PubMed Google Scholar
Guirado, E. & Schlesinger, L.S. Modeling the Mycobacterium tuberculosis granuloma—the critical battlefield in host immunity and disease. Front. Immunol.4, 98 (2013). ArticlePubMedPubMed CentralCAS Google Scholar
Mattila, J.T. et al. Microenvironments in tuberculous granulomas are delineated by distinct populations of macrophage subsets and expression of nitric oxide synthase and arginase isoforms. J. Immunol.191, 773–784 (2013). ArticleCASPubMed Google Scholar
Ramakrishnan, L. Revisiting the role of the granuloma in tuberculosis. Nat. Rev. Immunol.12, 352–366 (2012). ArticleCASPubMed Google Scholar
Cardona, P.-J. A spotlight on liquefaction: evidence from clinical settings and experimental models in tuberculosis. Clin. Dev. Immunol.2011, 868246–868249 (2011). ArticlePubMedPubMed Central Google Scholar
Kim, M.-J. et al. Caseation of human tuberculosis granulomas correlates with elevated host lipid metabolism. EMBO Mol. Med.2, 258–274 (2010). ArticleCASPubMedPubMed Central Google Scholar
Kaplan, G. et al. Mycobacterium tuberculosis growth at the cavity surface: a microenvironment with failed immunity. Infect. Immun.71, 7099–7108 (2003). ArticleCASPubMedPubMed Central Google Scholar
Subbian, S. et al. Lesion-specific immune response in granulomas of patients with pulmonary tuberculosis: a pilot study. PLoS One10, e0132249 (2015). ArticlePubMedPubMed CentralCAS Google Scholar
Davis, J.M. & Ramakrishnan, L. The role of the granuloma in expansion and dissemination of early tuberculous infection. Cell136, 37–49 (2009). ArticleCASPubMedPubMed Central Google Scholar
Peyron, P. et al. Foamy macrophages from tuberculous patients' granulomas constitute a nutrient-rich reservoir for M. tuberculosis persistence. PLoS Pathog.4, e1000204 (2008). ArticlePubMedPubMed CentralCAS Google Scholar
Saunders, B.M. & Cooper, A.M. Restraining mycobacteria: role of granulomas in mycobacterial infections. Immunol. Cell Biol.78, 334–341 (2000). ArticleCASPubMed Google Scholar
Via, L.E. et al. Infection dynamics and response to chemotherapy in a rabbit model of tuberculosis using 2-[18F]fluoro-deoxy-D-glucose positron emission tomography and computed tomography. Antimicrob. Agents Chemother.56, 4391–4402 (2012). ArticleCASPubMedPubMed Central Google Scholar
Lin, P.L. et al. Sterilization of granulomas is common in active and latent tuberculosis despite within-host variability in bacterial killing. Nat. Med.20, 75–79 (2014). ArticleCASPubMed Google Scholar
Gideon, H.P. et al. Variability in tuberculosis granuloma T cell responses exists, but a balance of pro- and anti-inflammatory cytokines is associated with sterilization. PLoS Pathog.11, e1004603 (2015). ArticlePubMedPubMed CentralCAS Google Scholar
Mayer-Barber, K.D. et al. Host-directed therapy of tuberculosis based on interleukin-1 and type I interferon cross-talk. Nature511, 99–103 (2014). ArticleCASPubMedPubMed Central Google Scholar
Tobin, D.M. et al. Host genotype-specific therapies can optimize the inflammatory response to mycobacterial infections. Cell148, 434–446 (2012). ArticleCASPubMedPubMed Central Google Scholar
Chen, M. et al. Lipid mediators in innate immunity against tuberculosis: opposing roles of PGE2 and LXA4 in the induction of macrophage death. J. Exp. Med.205, 2791–2801 (2008). ArticleCASPubMedPubMed Central Google Scholar
Divangahi, M. et al. Mycobacterium tuberculosis evades macrophage defenses by inhibiting plasma membrane repair. Nat. Immunol.10, 899–906 (2009). ArticleCASPubMedPubMed Central Google Scholar
Divangahi, M., Desjardins, D., Nunes-Alves, C., Remold, H.G. & Behar, S.M. Eicosanoid pathways regulate adaptive immunity to Mycobacterium tuberculosis. Nat. Immunol.11, 751–758 (2010). ArticleCASPubMedPubMed Central Google Scholar
Serhan, C.N., Chiang, N. & Van Dyke, T.E. Resolving inflammation: dual anti-inflammatory and pro-resolution lipid mediators. Nat. Rev. Immunol.8, 349–361 (2008). ArticleCASPubMedPubMed Central Google Scholar
Clay, H., Volkman, H.E. & Ramakrishnan, L. Tumor necrosis factor signaling mediates resistance to mycobacteria by inhibiting bacterial growth and macrophage death. Immunity29, 283–294 (2008). ArticleCASPubMedPubMed Central Google Scholar
Flynn, J.L. et al. Tumor necrosis factor–α is required in the protective immune response against Mycobacterium tuberculosis in mice. Immunity2, 561–572 (1995). ArticleCASPubMed Google Scholar
Roca, F.J. & Ramakrishnan, L. TNF dually mediates resistance and susceptibility to mycobacteria via mitochondrial reactive oxygen species. Cell153, 521–534 (2013). ArticleCASPubMedPubMed Central Google Scholar
Tobin, D.M. et al. The Lta4h locus modulates susceptibility to mycobacterial infection in zebrafish and humans. Cell140, 717–730 (2010). ArticleCASPubMedPubMed Central Google Scholar
Fallahi-Sichani, M., El-Kebir, M., Marino, S., Kirschner, D.E. & Linderman, J.J. Multiscale computational modeling reveals a critical role for TNF-α receptor 1 dynamics in tuberculosis granuloma formation. J. Immunol.186, 3472–3483 (2011). ArticleCASPubMed Google Scholar
Cilfone, N.A. et al. Computational modeling predicts IL-10 control of lesion sterilization by balancing early host-immunity-mediated antimicrobial responses with caseation during Mycobacterium tuberculosis infection. J. Immunol.194, 664–677 (2015). ArticleCASPubMed Google Scholar
Cilfone, N.A., Perry, C.R., Kirschner, D.E. & Linderman, J.J. Multiscale modeling predicts a balance of tumor necrosis factor–α and interleukin-10 controls the granuloma environment during Mycobacterium tuberculosis infection. PLoS One8, e68680 (2013). ArticleCASPubMedPubMed Central Google Scholar
McNab, F., Mayer-Barber, K., Sher, A., Wack, A. & O'Garra, A. Type I interferons in infectious disease. Nat. Rev. Immunol.15, 87–103 (2015). ArticleCASPubMedPubMed Central Google Scholar
Prideaux, B. et al. The association between sterilizing activity and drug distribution into tuberculosis lesions. Nat. Med.21, 1223–1227 (2015). ArticleCASPubMedPubMed Central Google Scholar
Cox, J. et al. Accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction, termed MaxLFQ. Mol. Cell. Proteomics13, 2513–2526 (2014). ArticleCASPubMedPubMed Central Google Scholar
Prideaux, B. et al. High-sensitivity MALDI–MRM–MS imaging of moxifloxacin distribution in tuberculosis-infected rabbit lungs and granulomatous lesions. Anal. Chem.83, 2112–2118 (2011). ArticleCASPubMedPubMed Central Google Scholar
Via, L.E. et al. A sterilizing tuberculosis treatment regimen is associated with faster clearance of bacteria in cavitary lesions in marmosets. Antimicrob. Agents Chemother.59, 4181–4189 (2015). ArticleCASPubMedPubMed Central Google Scholar
Leong, F., Eum, S. & Via, L.E. in A Color Atlas of Comparative Pathology of Pulmonary Tuberculosis (eds. Leong, F.J., Dartois, V. & Dick, T.) 53–81 (CRC Press, 2011).
National Research Council. Guide for the Care and Use of Laboratory Animals 8th edn. (The National Academies Press, 2011).
Ostasiewicz, P., Zielinska, D.F., Mann, M. & Wiśniewski, J.R. Proteome, phosphoproteome and _N_-glycoproteome are quantitatively preserved in formalin-fixed paraffin-embedded tissue and analyzable by high-resolution mass spectrometry. J. Proteome Res.9, 3688–3700 (2010). ArticleCASPubMed Google Scholar
Sharma, K. et al. Quantitative analysis of kinase-proximal signaling in lipopolysaccharide-induced innate immune response. J. Proteome Res.9, 2539–2549 (2010). ArticleCASPubMed Google Scholar
D'Souza, R.C.J. et al. Time-resolved dissection of early phosphoproteome and ensuing proteome changes in response to TGF-β. Sci. Signal.7, rs5 (2014). PubMed Google Scholar
Michalski, A. et al. Mass-spectrometry-based proteomics using Q Exactive, a high-performance benchtop quadrupole Orbitrap mass spectrometer. Mol. Cell. Proteomics10, 011015 (2011). ArticlePubMed Google Scholar
Cox, J. et al. Andromeda: a peptide search engine integrated into the MaxQuant environment. J. Proteome Res.10, 1794–1805 (2011). ArticleCASPubMed Google Scholar
Guan, Y.Q., Cai, Y.Y., Zhang, X., Lee, Y.T. & Opas, M. Adaptive correction technique for 3D reconstruction of fluorescence microscopy images. Microsc. Res. Tech.71, 146–157 (2008). ArticleCASPubMed Google Scholar
Mietla, J.A. et al. Characterization of eicosanoid synthesis in a genetic ablation model of ceramide kinase. J. Lipid Res.54, 1834–1847 (2013). ArticleCASPubMedPubMed Central Google Scholar