2009, Number 1
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Rev Inst Nal Enf Resp Mex 2009; 22 (1)
Biogenesis of mycobacterial phagolysosome and its role in antigen processing and presentation
Bobadilla-Lozoya K, Rivas-Santiago B, Sada-Díaz E, Torres-Rojas M
Language: Spanish
References: 52
Page: 56-62
PDF size: 78.18 Kb.
ABSTRACT
Mycobacterium tuberculosis (M.tb) is an intracellular pathogen that survives within host macrophages.
M.tb is phagocytosed by receptors on the cell membrane such as the CR1 complement receptor, mannose receptor, fibrin receptor, etc. Once
M.tb is phagocytosed, a rearrangement of membranes occurs to form the phagosome. The phagosome is an intracellular organelle where
M.tb survives and where mycobacterial proteins are processed to bind to MHC class II proteins in endosomal compartments, so they can be presented at the cell membrane and activate CD4
+ T cells. It has been recently described that phagosome is not just the site of antigen degradation; it is also a competent organelle where peptide-MHC-II complexes are formed. Experimental evidences have shown that live M.tb decreases formation of these complexes in the phagosome, but the exact mechanism that determines the site of formation of the peptide-MHC-II complexes and its biological implications are unknown.
REFERENCES
OMS. TB global report. WHO, 2008.
Gruppo V, Orme IM. Dose of BCG does not influence the efficient generation of protective immunity in mice challenged with Mycobacterium tuberculosis. Tuberculosis (Edinb) 2002;82:267-273.
Schlesinger LS. Entry of Mycobacterium tuberculosis into mononuclear phagocytes. Curr Top Microbiol Immunology 1996;215:71-96.
Hirsch CS, Ellner JJ, Russell DG, Rich EA. Complement receptor-mediated uptake and tumor necrosis factor-alpha-mediated growth inhibition of Mycobacterium tuberculosis by human alveolar macrophages. J Immunol 1994;152:743-753.
Deretic V, Singh S, Master S, et ál. Mycobacterium tuberculosis inhibition of phagolysosome biogenesis and autophagy as a host defence mechanism. Cell Microbiol 2006;8:719-727.
Xu S, Cooper A, Sturgill-Koszycki S, et ál. Intracellular trafficking in Mycobacterium tuberculosis and Mycobacterium avium-infected macrophages. J Immunol 1994;153:2568-2578.
Armstrong JA, Hart PD. Phagosome-lysosome interactions in cultured macrophages infected with virulent tubercle bacilli. Reversal of the usual nonfusion pattern and observations on bacterial survival. J Exp Med 1975;142:1-16.
Holsti MA, Allen PM. Processing and presentation of an antigen of Mycobacterium avium require access to an acidified compartment with active proteases. Infect Immun 1996;64:4091-4098.
Ramachandra L, Chu RS, Askew D, et ál. Phagocytic antigen processing and effects of microbial products on antigen processing and T-cell responses. Immunol Rev 1999;168:217-239.
Ramachandra L, Noss E, Boom WH, Harding CV. Phagocytic processing of antigens for presentation by class II major histocompatibility complex molecules. Cell Microbiol 1999;1:205-214.
Boom WH, Canaday DH, Fulton SA, Gehring AJ, Rojas RE, Torres M. Human immunity to M. tuberculosis: T cell subsets and antigen processing. Tuberculosis (Edinb) 2003;83:98-106.
Flynn JL, Chan J. Immune evasion by Mycobacterium tuberculosis: living with the enemy. Curr Opin Immunol 2003;15:450-455.
Mellman I. Endocytosis and molecular sorting. Annu Rev Cell Dev Biol 1996;12:575-625.
Ernst JD. Macrophage receptors for Mycobacterium tuberculosis. Infect Immun 1998;66:1277-1281.
Wang XL, Lei JQ, Wang HH. The macrophage receptors for uptaking Mycobacterium tuberculosis. Zhonghua Jie He He Hu Xi Za Zhi 2003;26: 297-299.
Ozeki Y, Tsutsui H, Kawada N, et ál. Macrophage scavenger receptor down-regulates mycobacterial cord factor-induced proinflammatory cytokine production by alveolar and hepatic macrophages. Microbial Pathog 2006;40:171-176.
Schlesinger LS, Bellinger-Kawahara CG, Payne NR, Horwitz MA. Phagocytosis of Mycobacterium tuberculosis is mediated by human monocyte complement receptors and complement component C3. J Immunol 1990;144:2771-2780.
Schorey JS, Carroll MC, Brown EJ. A macrophage invasion mechanism of pathogenic mycobacteria. Science 1997;277:1091-1093.
Aderem A, Underhill DM. Mechanisms of phagocytosis in macrophages. Annu Rev Immunol 1999;17:593-623.
Pasula R, Downing JF, Wright JR, Kachel DL, Davis TE Jr, Martin WJ 2nd. Surfactant protein A (SP-A) mediates attachment of Mycobacterium tuberculosis to murine alveolar macrophages. Am J Respir Cell Mol Biol 1997;17:209-217.
Pasula R, Wright JR, Kachel DL, Martin WJ 2nd. Surfactant protein A suppresses reactive nitrogen intermediates by alveolar macrophages in response to Mycobacterium tuberculosis. J Clin Invest 1999;103: 483-490.
Schlesinger LS. Macrophage phagocytosis of virulent but not attenuated strains of Mycobacterium tuberculosis is mediated by mannose receptors in addition to complement receptors. J Immunol 1993;150: 2920-2930.
23, Zimmerli S, Edwards S, Ernst JD. Selective receptor blockade during phagocytosis does not alter the survival and growth of Mycobacterium tuberculosis in human macrophages. Am J Respir Cell Mol Biol 1996;15: 760-770.
Clemens DL, Horwitz MA. Characterization of the Mycobacterium tuberculosis phagosome and evidence that phagosomal maturation is inhibited. J Exp Med 1995;181:257-270.
Ramachandra L, Boom WH, Harding CV. Class II MHC antigen processing in phagosomes. Methods Mol Biol 2008;445:353-377.
Deretic V, Via LE, Fratti RA, Deretic D. Mycobacterial phagosome maturation, rab proteins, and intracellular trafficking. Electrophoresis 1997;18:2542-2547.
Fratti RA, Backer JM, Gruenberq J, Corvera S, Deretic V. Role of phosphatidylinositol 3-kinase and Rab5 effectors in phagosomal biogenesis and mycobacterial phagosome maturation arrest. J Cell Biol 2001;154: 631-644.
Desjardins M. Biogenesis of phagolysosomes: the ‘kiss and run’ hypothesis. Trends cell biol 1995;5:183-186.
Brumell JH, Scidmore MA. Manipulation of rab GTPase function by intracellular bacterial pathogens. Microbiol Mol Biol Rev 2007;71:636-652.
Clemens DL, Lee BY, Horwitz A. Mycobacterium tuberculosis and Legionella pneumophila phagosomes exhibit arrested maturation despite acquisition of Rab7. Infect Immun 2000;68:5154-5166.
Clemens DL, Horwitz MA. The Mycobacterium tuberculosis phagosome interacts with early endosomes and is accessible to exogenously administered transferrin. J Exp Med 1996;184:1349-1355.
Fenton MJ, Vermeulen MW. Immunopathology of tuberculosis: roles of macrophages and monocytes. Infect Immun 1996;64:683-690.
Chua J, Vergne I, Master S, Deretic V. A tale of two lipids: Mycobacterium tuberculosis phagosome maturation arrest. Curr Opin Microbiol 2004;7:71-77.
Hart PD, Armstrong JA, Brown CA, Draper P. Ultrastructural study of the behavior of macrophages toward parasitic mycobacteria. Infect Immun 1972;5: 803-807.
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.
Sturgill-Koszycki S, Schlesinger PH, Chakraborty P, et ál. Lack of acidification in Mycobacterium phagosomes produced by exclusion of the vesicular proton-ATPase. Science 1994;263:678-681.
Vergne I, Fratti RA, Hill PJ, Chua J, Belisle J, Deretic V. Mycobacterium tuberculosis phagosome maturation arrest: mycobacterial phosphatidylinositol analog phosphatidylinositol mannoside stimulates early endosomal fusion. Mol Biol Cell 2004;15:751-760.
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.
Fratti RA, Vergne I, Chua J, Skidmore J, Deretic V. Regulators of membrane trafficking and Mycobacterium tuberculosis phagosome maturation block. Electrophoresis 2000;21:3378-3385.
Via LE, Deretic D, Ulmer RJ, Hibler NS, Huber LA, Deretic V. Arrest of mycobacterial phagosome maturation is caused by a block in vesicle fusion between stages controlled by rab5 and rab7. J biol Chem 1997;272: 13326-13331.
Briken V, Porcelli SA, Besra GS, Kremer L. Mycobacterial lipoarabinomannan and related lipoglycans: from biogenesis to modulation of the immune response. Mol Microbiol 2004;53:391-403.
Noss EH, Pai RK, Sellati TJ, et ál. Toll-like receptor 2-dependent inhibition of macrophage class II MHC expression and antigen processing by 19-kDa lipoprotein of Mycobacterium tuberculosis. J Immunol 2001; 167:910-918.
Pai RK, Convery M, Hamilton TA, Boom WH, Harding CV. Inhibition of IFN-gamma-induced class II transactivator expression by a 19-kDa lipoprotein from Mycobacterium tuberculosis: a potential mechanism for immune evasion. J Immunol 2003;171:175-184.
Vergne I, Chua J, Singh SB, Deretic V. Cell biology of Mycobacterium tuberculosis phagosome. Annu Rev Cell Dev Biol 2004;20:367-394.
Pamer E, Cresswell P. Mechanisms of MHC class I-restricted antigen processing. Ann Rev Immunol 1998; 16:323-358.
Cresswell P. Antigen presentation. Getting peptides into MHC class II molecules. Curr Biol 1994;4:541-543.
Lehner PJ, Cresswell P. Recent developments in MHC-class-I-mediated antigen presentation. Curr Opin Immunol 2004;16:82-89.
Cresswell P. Invariant chain structure and MHC class II function. Cell 1996; 84:505-507.
Denzin LK, Cresswell P. HLA-DM induces CLIP dissociation from MHC class II alpha beta dimers and facilitates peptide loading. Cell 1995;82:155-165.
Ramachandra L, Song R, Harding CV. Phagosomes are fully competent antigen-processing organelles that mediate the formation of peptide: class II MHC complexes. J Immunol 1999;162:3263-3272.
Ramachandra L, Noss E, Boom WH, Harding CV. Processing of Mycobacterium tuberculosis antigen 85B involves intraphagosomal formation of peptide-major histocompatibility complex II complexes and is inhibited by live bacilli that decrease phagosome maturation. J Exp Med 2001;194:1421-1432.
Torres M, Ramachandra L, Rojas RE, et ál. Role of phagosomes and major histocompatibility complex class II (MHC-II) compartment in MHC-II antigen processing of Mycobacterium tuberculosis in human macrophages. Infect Immun 2006;74:1621-1630.