2009, Número 4
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Gac Med Mex 2009; 145 (4)
Principales mecanismos de evasión de la respuesta inmune por Mycobacterium tuberculosis
Chávez-Galán L, Arenas-Del Ángel MC, Sada-Ovalle I, Lascurain R
Idioma: Español
Referencias bibliográficas: 91
Paginas: 323-330
Archivo PDF: 157.44 Kb.
RESUMEN
En la actualidad, la tuberculosis pulmonar es considerada un problema grave de salud mundial. Para entender el proceso infeccioso de la tuberculosis es necesario conocer las interacciones entre la respuesta inmune del hospedero y su agente causal. Actualmente se han realizado grandes avances en la identificación de nuevas moléculas y genes que participan activamente en los mecanismos de evasión, generando la posibilidad de que en un futuro próximo se diseñen diversos compuestos químicos para el desarrollo de vacunas o terapias que tengan como blanco estas moléculas o genes. Sin embargo, no se han esclarecido completamente los diversos mecanismos con que cuenta la micobacteria para evadir la respuesta inmune del hospedero. En esta revisión se discute la evidencia experimental reciente sobre los mecanismos propuestos para el éxito de la bacteria.
REFERENCIAS (EN ESTE ARTÍCULO)
World Heath Organization. Global TB control report 2008. Geneve, Switzerland: WHO; 2008.
Martino A. Mycobacteria and innate cells: critical encounter for immunogenicity. J Biosci 2008;33:137-144.
Stenger S. Immunological control of tuberculosis: role of tumour necrosis factor and more. Ann Rheum Dis 2005;64:iv24- iv28.
Brown AK, Bhatt A, Singh A, Saparia E, Evans AF, Besra GS. Identification of the dehydratase component of the mycobacterial mycolic acid-synthesizing fatty acid synthase-II complex. Microbiology 2007;153:4166-4173.
Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, et al. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 1998;393:537-544.
Bhatt A, Fujiwara N, Bhatt K, Gurcha SS, Kremer L, Chen B, et al. Deletion of kasB in Mycobacterium tuberculosis causes loss of acid-fastness and subclinical latent tuberculosis in immunocompetent mice. Proc Natl Acad Sci USA 2007;104:5157-5162.
Bulut Y, Michelsen KS, Hayrapetian L, Naiki Y, Spallek R, Singh M, et al. Mycobacterium tuberculosis heat shock proteins use diverse Toll-like receptor pathways to activate pro-inflammatory signals. J Biol Chem 2005;280:20961-20967.
Pompei L, Jang S, Zamlynny B, Ravikumar S, McBride A, Hickman SP, et al. Disparity in IL-12 release in dendritic cells and macrophages in response to Mycobacterium tuberculosis is due to use of distinct TLRs. J Immunol 2007;178:5192-5199.
Puissegur MP, Lay G, Gilleron M, Botella L, Nigou J, Marrakchi H, et al. Mycobacterial lipomannan induces granuloma macrophage fusion via a TLR2- dependent, ADAM9- and beta integrin-mediated pathway. J Immunol 2007;178:3161-3169.
Aliprantis AO, Yang RB, Mark MR, Suggett S, Devaux B, Radolf JD, et al. Cell activation and apoptosis by bacterial lipoproteins through toll-like receptor-2. Science 1999;285:736-739.
Brightbill HD, Libraty DH, Krutzik SR, Yang RB, Belisle JT, Bleharski JR, et al. Host defense mechanisms triggered by microbial lipoproteins through toll-like receptors. Science 1999;285:732-736.
Russell DG. Who puts the tubercle in tuberculosis? Nat Rev Microbiol 2007;5:39-47.
Huang D, Shen Y, Qiu L, Chen CY, Shen L, Estep J, et al. Immune distribution and localization of phosphoantigen-specific Vγ2Vδ2 T cells in lymphoid and nonlymphoid tissues in Mycobacterium tuberculosis infection. Infect Immun 2008;76:426-436.
Kulpraneet M, Sukwit S, Sumransurp K, Chuenchitra T, Santiwatanakul S, Srisurapanon S. Cytokine production in NK and NKT cells from Mycobacterium tuberculosis infected patients. Southeast Asian J Trop Med Public Health 2007;38:370-375.
Hernández-Pando R, Jeyanathan M, Mengistu G, Aguilar D, Orozco H, Harboe M, et al. Persistence of DNA from Mycobacterium tuberculosis in superficially normal lung tissue during latent infection. Lancet 2000;356:2133-2138.
Iles KE, Forman HJ. Macrophage signaling and respiratory burst. Immunol Res 2002;26:95-105.
Singh R, Wiseman B, Deemagarn T, Donald LJ, Duckworth HW, Carpena X, et al. Catalase-peroxidases (KatG) exhibit NADH oxidase activity. J Biol Chem 2004;279:43098-43106.
MacMicking JD, North RJ, LaCourse R, Mudgett JS, Shah SK, Nathan CF. Identification of nitric oxide synthase as a protective locus against tuberculosis. Proc Natl Acad Sci U S A 1997;94:5243-5248.
Ehrt S, Shiloh MU, Ruan J, Choi M, Gunzburg S, Nathan C, et al. A novel antioxidant gene from Mycobacterium tuberculosis. J Exp Med 1997;186:1885-1896.
Lin QY, Jin LJ, Cao ZH, Xu YP. Inhibition of inducible nitric oxide synthase by Acanthopanax senticosus extract in RAW264.7 macrophages. J Ethnopharmacol 2008;118:231-236.
Miller BH, Fratti RA, Poschet JF, Timmins GS, Master SS, Burgos M, et al. Mycobacteria inhibit nitric oxide synthase recruitment to phagosomes during macrophage infection. Infect Immun 2004;72:2872-2878.
Davis AS, Vergne I, Master SS, Kyei GB, Chua J, Deretic V. Mechanism of Inducible Nitric Oxide Synthase Exclusion from Mycobacterial Phagosomes. PLoS Pathog 2007;3:e186.
Braunstein M, Espinosa BJ, Chan J, Belisle JT, Jacobs WR Jr. SecA2 functions in the secretion of superoxide dismutase A and in the virulence of Mycobacterium tuberculosis. Mol Microbiol 2003;48:453-464.
McLaughlin B, Chon JS, MacGurn JA, Carlsson F, Cheng TL, Cox JS, et al. A mycobacterium ESX-1-secreted virulence factor with unique requirements for export. PLoS Pathog 2007;3:e105.
Ng VH, Cox JS, Sousa AO, MacMicking JD, McKinney JD. Role of KatG catalase-peroxidase in mycobacterial pathogenesis: countering the phagocyte oxidative burst. Mol Microbiol 2004;52:1291-1302.
Kurtz S, McKinnon KP, Runge MS, Ting JP, Braunstein M. The SecA2 secretion factor of Mycobacterium tuberculosis promotes growth in macrophages and inhibits the host immune response. Infect Immun 2006;74:6855-6864.
Scanga CA, Bafica A, Feng CG, Cheever AW, Hieny S, Sher A. MyD88- deficient mice display a profound loss in resistance to Mycobacterium tuberculosis associated with partially impaired Th1 cytokine and nitric oxide synthase 2 expression. Infect Immun 2004;72:2400-2404.
Shimada K, Takimoto H, Yano I, Kumazawa Y. Involvement of mannose receptor in glycopeptidolipid-mediated inhibition of phagosome-lysosome fusion. Microbiol Immunol 2006;50:243-251.
Le Cabec V, Carréno S, Moisand A, Bordier C, Maridonneau-Parini I. Complement receptor 3 (CD11b/CD18) mediates type I and type II phagocytosis during nonopsonic and opsonic phagocytosis, respectively. J Immunol 2002;169:2003-2009.
Tailleux L, Schwartz O, Herrmann JL, Pivert E, Jackson M, Amara A, et al. DC-SIGN is the major Mycobacterium tuberculosis receptor on human dendritic cells. J Exp Med 2003;197:121-127.
Caron E, Hall A. Identification of two distinct mechanisms of phagocytosis controlled by different Rho GTPases. Science 1998;282:1717-1721.
Harrison RE, Bucci C, Vieira OV, Schroer TA, Grinstein S. Phagosomes fuse with late endosomes and/or lysosomes by extension of membrane protrusions along microtubules: role of Rab7 and RILP. Mol Cell Biol 2003;23:6494-6506.
Clemens DL, Horwitz MA. Characterization of the Mycobacterium tuberculosis phagosome and evidence that phagosomal maturation is inhibited. J Exp Med 1995;181:257-270.
Sturgill-Koszycki S, Schlesinger PH, Chakraborty P, Haddix PL, Collins HL, Fok AK, et al. Lack of acidification in Mycobacterium phagosomes produced by exclusion of the vesicular proton-ATPase. Science 1994;263(5147):678-681.
Singh CR, Moulton RA, Armitige LY, Bidani A, Snuggs M, Dhandayuthapani S, et al. Processing and presentation of a mycobacterial antigen 85B epitope by murine macrophages is dependent on the phagosomal acquisition of vacuolar proton ATPase and in situ activation of cathepsin D. J Immunol 2006;177:3250-3259.
Ferrari G, Langen H, Naito M, Pieters J. A coat protein on phagosomes involved in the intracellular survival of mycobacteria. Cell 1999;97:435-447.
Gatfield J, Albrecht I, Zanolari B, Steinmetz MO, Pieters J. Association of the leukocyte plasma membrane with the actin cytoskeleton through coiled coil-mediated trimeric coronin 1 molecules. Mol Biol Cell 2005;16:2786-2798.
Jayachandran R, Sundaramurthy V, Combaluzier B, Mueller P, Korf H, Huygen K, et al. Survival of mycobacteria in macrophages is mediated by coronin 1-dependent activation of calcineurin. Cell 2007;130:37-50.
Suzuki K, Takeshita F, Nakata N, Ishii N, Makino M. Localization of CORO1A in the macrophages containing Mycobacterium leprae. Acta Histochem Cytochem 2006;39:107-112.
Deghmane AE, Soualhine H, Bach H, Sendide K, Itoh S, Tam A, et al. Lipoamide dehydrogenase mediates retention of coronin-1 on BCG vacuoles, leading to arrest in phagosome maturation. J Cell Sci 2007;120:2796-806.
Wickner W, Schekman R. Membrane fusion. Nat Struct Mol Biol 2008;15:658-664.
Vieira OV, Bucci C, Harrison RE, Trimble WS, Lanzetti L, Gruenberg J, et al. Modulation of Rab5 and Rab7 recruitment to phagosomes by phosphatidylinositol 3-kinase. Mol Cell Biol 2003;23:2501-2514.
Bucci C, Parton RG, Mather IH, Stunnenberg H, Simons K, Hoflack B, et al. The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway. Cell 1992;70:715-728.
Sun J, Deghmane AE, Soualhine H, Hong T, Bucci C, Solodkin A, et al. Mycobacterium bovis BCG disrupts the interaction of Rab7 with RILP contributing to inhibition of phagosome maturation. J Leukoc Biol 2007;82:1437-1445.
Kyei GB, Vergne I, Chua J, Roberts E, Harris J, Junutula JR, et al. Rab14 is critical for maintenance of Mycobacterium tuberculosis phagosome maturation arrest. EMBO J 2006;25:5250-5259.
Master SS, Rampini SK, Davis AS, Keller C, Ehlers S, Springer B, et al. Mycobacterium tuberculosis prevents inflammasome activation. Cell Host Microbe 2008;3:224-232.
Makino M, Maeda Y, Mukai T, Kaufmann SH. Impaired maturation and function of dendritic cells by mycobacteria through IL-1beta. Eur J Immunol 2006;36:1443-1452.
Fratti RA, Chua J, Deretic V. Induction of p38 mitogen-activated protein kinase reduces early endosome autoantigen 1 (EEA1) recruitment to phagosomal membranes. J Biol Chem 2003;278:46961-46967.
Jung SB, Yang CS, Lee JS, Shin AR, Jung SS, Son JW, et al. The mycobacterial 38-kilodalton glycolipoprotein antigen activates the mitogenactivated protein kinase pathway and release of proinflammatory cytokines through Toll-like receptors 2 and 4 in human monocytes. Infect Immun 2006;74:2686-2696.
Souza CD, Evanson OA, Weiss DJ. Role of cell membrane receptors in the suppression of monocyte anti-microbial activity against Mycobacterium avium subsp. paratuberculosis. Microb Pathog 2008;44:215-223.
Bhattacharya M, Ojha N, Solanki S, Mukhopadhyay CK, Madan R, Patel N, et al. IL-6 and IL-12 specifically regulate the expression of Rab5 and Rab7 via distinct signaling pathways. EMBO J 2006;25:2878-2888.
Nagabhushanam V, Solache A, Ting LM, Escaron CJ, Zhang JY, Ernst JD. Innate inhibition of adaptive immunity: Mycobacterium tuberculosisinduced IL-6 inhibits macrophage responses to IFN-gamma. J Immunol 2003;171:4750-4757.
Sibley LD, Hunter SW, Brennan PJ, Krahenbuhl JL. Mycobacterial lipoarabinomannan inhibits gamma interferon-mediated activation of macrophages. Infect Immun 1988;56:1232-1236.
Hayakawa E, Tokumasu F, Nardone GA, Jin AJ, Hackley VA, Dvorak JA. A Mycobacterium tuberculosis-derived lipid inhibits membrane fusion by modulating lipid membrane domains. Biophys J 2007;93:4018-4030.
De Chastellier C, Thilo L. Cholesterol depletion in Mycobacterium aviuminfected macrophages overcomes the block in phagosome maturation and leads to the reversible sequestration of viable mycobacteria in phagolysosome- derived autophagic vacuoles. Cell Microbiol 2006;8:242-256.
Kaul D, Anand PK, Verma I. Cholesterol-sensor initiates M. tuberculosis entry into human macrophages. Mol Cell Biochem 2004;258:219-222.
Raiborg C, Bache KG, Mehlum A, Stang E, Stenmark H. Hrs recruits clathrin to early endosomes. EMBO J 2001;20:5008-5021.
Patki V, Virbasius J, Lane WS, Toh BH, Shpetner HS, Corvera S. Identification of an early endosomal protein regulated by phosphatidylinositol 3-kinase. Proc Natl Acad Sci USA 1997;94:7326-7330.
Vergne I, Chua J, Lee HH, Lucas M, Belisle J, Deretic V. Mechanism of phagolysosome biogenesis block by viable Mycobacterium tuberculosis. Proc Natl Acad Sci USA 2005;102:4033-4038.
Fratti RA, Chua J, Vergne I, Deretic V. Mycobacterium tuberculosis glycosylated phosphatidylinositol causes phagosome maturation arrest. Proc Natl Acad Sci USA 2003;100:5437-5442.
Walburger A, Koul A, Ferrari G, Nguyen L, Prescianotto-Baschong C, Huygen K, et al. Protein kinase G from pathogenic mycobacteria promotes survival within macrophages. Science 2004;304:1800-1804.
Majlessi L, Combaluzier B, Albrecht I, Garcia JE, Nouze C, Pieters J, et al. Inhibition of phagosome maturation by mycobacteria does not interfere with presentation of mycobacterial antigens by MHC molecules. J Immunol 2007;179:1825-1833.
MacGurn JA, Cox JS. A genetic screen for Mycobacterium tuberculosis mutants defective for phagosome maturation arrest identifies components of the ESX-1 secretion system. Infect Immun 2007;75:2668-2678.
Xu J, Laine O, Masciocchi M, Manoranjan J, Smith J, Du SJ, et al. A unique Mycobacterium ESX-1 protein co-secretes with CFP-10/ESAT-6 and is necessary for inhibiting phagosome maturation. Mol Microbiol 2007;66:787-800.
Antas PR, Sales JS, Pereira KC, Oliveira EB, Cunha KS, Sarno EN, et al. Patterns of intracellular cytokines in CD4 and CD8 T cells from patients with mycobacterial infections. Braz J Med Biol Res 2004;37:1119-1129.
Millington KA, Innes JA, Hackforth S, Hinks TS, Deeks JJ, Dosanjh DP, et al. Dynamic relationship between IFN-gamma and IL-2 profile of Mycobacterium tuberculosis-specific T cells and antigen load. J Immunol 2007;178:5217-5226.
Hmama Z, Gabathuler R, Jefferies WA, de Jong G, Reiner NE. Attenuation of HLA-DR expression by mononuclear phagocytes infected with Mycobacterium tuberculosis is related to intracellular sequestration of immature class II heterodimers. J Immunol 1998;161:4882-4893.
Sánchez MD, García Y, Montes C, París SC, Rojas M, Barrera LF, et al. Functional and phenotypic changes in monocytes from patients with tuberculosis are reversed with treatment. Microbes Infect 2006;8:2492-2500.
Rajeswari DN, Selvaraj P, Raghavan S, Jawahar MS, Narayanan PR. Influence of HLA-DR2 on perforin-positive cells in pulmonary tuberculosis. Int J Immunogenet 2007;34:379-384.
Wolf AJ, Linas B, Trevejo-Núñez GJ, Kincaid E, Tamura T, Takatsu K, et al. Mycobacterium tuberculosis infects dendritic cells with high frequency and impairs their function in vivo. J Immunol 2007;179:2509-2519.
Kincaid EZ, Wolf AJ, Desvignes L, Mahapatra S, Crick DC, Brennan PJ, et al. Codominance of TLR2-dependent and TLR2-independent modulation of MHC class II in Mycobacterium tuberculosis infection in vivo. J Immunol 2007;179:3187-3195.
Lafuse WP, Álvarez GR, Curry HM, Zwilling BS. Mycobacterium tuberculosis and Mycobacterium avium inhibit IFN- gamma -induced gene expression by TLR2-dependent and independent pathways. J Interferon Cytokine Res 2006;26:548-561.
Fortune SM, Solache A, Jaeger A, Hill PJ, Belisle JT, Bloom BR, et al. Mycobacterium tuberculosis inhibits macrophage responses to IFN-gamma through myeloid differentiation factor 88-dependent and -independent mechanisms. J Immunol 2004;172:6272-6280.
Banaiee N, Kincaid EZ, Buchwald U, Jacobs WR Jr, Ernst JD. Potent inhibition of macrophage responses to IFN-gamma by live virulent Mycobacterium tuberculosis is independent of mature mycobacterial lipoproteins but dependent on TLR2. J Immunol 2006;176:3019-3027.
Gehring AJ, Dobos KM, Belisle JT, Harding CV, Boom WH. Mycobacterium tuberculosis LprG (Rv1411c): a novel TLR-2 ligand that inhibits human macrophage class II MHC antigen processing. J Immunol 2004;173:2660-2668.
Pecora ND, Gehring AJ, Canaday DH, Boom WH, Harding CV. Mycobacterium tuberculosis LprA is a lipoprotein agonist of TLR2 that regulates innate immunity and APC function. J Immunol 2006;177:422-429.
Placido R, Mancino G, Amendola A, Mariani F, Vendetti S, Piacentini M, et al. Apoptosis of human monocytes/macrophages in Mycobacterium tuberculosis infection. J Pathol 1997;181:31-38.
Danelishvili L, McGarvey J, Li YJ, Bermúdez LE. Mycobacterium tuberculosis infection causes different levels of apoptosis and necrosis in human macrophages and alveolar epithelial cells. Cell Microbiol 2003;5:649-660.
Edinger AL, Thompson CB. Death by design: apoptosis, necrosis and autophagy. Curr Opin Cell Biol 2004;16:663-669.
Keane J, Remold HG, Kornfeld H. Virulent Mycobacterium tuberculosis strains evade apoptosis of infected alveolar macrophages. J Immunol 2000;164:2016-2020.
Schaible UE, Winau F, Sieling PA, Fischer K, Collins HL, Hagens K, et al. Apoptosis facilitates antigen presentation to T lymphocytes through MHC-I and CD1 in tuberculosis. Nat Med 2003;9:1039-1046.
Winau F, Weber S, Sad S, de Diego J, Hoops SL, Breiden B, et al. Apoptotic vesicles crossprime CD8 T cells and protect against tuberculosis. Immunity 2006;24:105-117.
López M, Sly LM, Luu Y, Young D, Cooper H, Reiner NE. The 19-kDa Mycobacterium tuberculosis protein induces macrophage apoptosis through Toll-like receptor-2. J Immunol 2003;170:2409-2416.
Lee J, Remold HG, Ieong MH, Kornfeld H. Macrophage apoptosis in response to high intracellular burden of Mycobacterium tuberculosis is mediated by a novel caspase-independent pathway. J Immunol 2006;176:4267-4274.
O’Sullivan MP, O’Leary S, Kelly DM, Keane J. A caspase-independent pathway mediates macrophage cell death in response to Mycobacterium tuberculosis infection. Infect Immun 2007;75:1984-1993.
Chen M, Gan H, Remold HG. A mechanism of virulence: virulent Mycobacterium tuberculosis strain H37Rv, but not attenuated H37Ra, causes significant mitochondrial inner membrane disruption in macrophages leading to necrosis. J Immunol 2006;176:3707-3716.
Park JS, Tamayo MH, González-Juarrero M, Orme IM, Ordway DJ. Virulent clinical isolates of Mycobacterium tuberculosis grow rapidly and induce cellular necrosis but minimal apoptosis in murine macrophages. J Leukoc Biol 2006;79:80-86.
Velmurugan K, Chen B, Miller JL, Azogue S, Gurses S, Hsu T, et al. Mycobacterium tuberculosis nuoG is a virulence gene that inhibits apoptosis of infected host cells. PLoS Pathog 2007;3:e110.
Sly LM, Hingley-Wilson SM, Reiner NE, McMaster WR. Survival of Mycobacterium tuberculosis in host macrophages involves resistance to apoptosis dependent upon induction of antiapoptotic Bcl-2 family member Mcl-1. J Immunol 2003;170:430-437.
Zhang J, Jiang R, Takayama H, Tanaka Y. Survival of virulent Mycobacterium tuberculosis involves preventing apoptosis induced by Bcl-2 upregulation and release resulting from necrosis in J774 macrophages. Microbiol Immunol 2005;49:845-852.
Hasan Z, Ashraf M, Tayyebi A, Hussain R. M. leprae inhibits apoptosis in THP-1 cells by downregulation of bad and bak and upregulation of Mcl-1 gene expression. BMC Microbiol 2006;6:78.