Alteraciones en el reclutamiento y activación de proteínas Rab durante la infección micobacteriana
Palabras clave:
tuberculosis, Mycobacterium tuberculosis, proteínas de unión a GTP rab, proteínas SNARE, fagosomas, endosomas
Resumen
En el fagosoma, Mycobacterium spp. altera la activación y reclutamiento de diferentes proteínas "del gen Ras de cerebro de rata", comúnmente conocidas como Rab. En este manuscrito se revisa una serie de reportes que han demostrado que los fagosomas que contienen micobacterias tienen una expresión mayor y sostenida de Rab5, Rab11, Rab14 y Rab22a, y menor o ninguna expresión de Rab7, Rab9 y Rab6. Esto se correlaciona con aumento de la fusión de estos fagosomas con endosomas tempranos y de reciclaje, lo que les permite mantener ciertas características de compartimentos tempranos, permite que las bacterias obtengan acceso a nutrientes y previene la activación de mecanismos contra la micobacteria.La expresión de mutantes constitutivamente activos de las Rab de endosomas tempranos impide la maduración de fagosomas que contienen esferas de látex o micobacterias inactivadas por calor. Mientras que su silenciamiento, mediante ARN de interferencia o mediante dominantes negativos, induce la maduración de fagosomas micobacterianos. Los mecanismos exactos por los que las micobacterias alteran la dinámica de expresión de estas GTPasas, afectando la maduración fagolisosómica, no se han establecido. El problema podría explicarse por defectos en el reclutamiento de las proteínas que interactúan con Rab, como la cinasa-3 del fosfatidilinositol y el antígeno endosómico temprano 1. La identificación de los mecanismos empleados por Mycobacterium spp. para interrumpir el ciclo de activación de las Rab, será esencial para comprender la fisiopatología de la infección micobacteriana y útil como posibles blancos farmacológicos.
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Referencias bibliográficas
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6. Le Roy C, Wrana JL. Clathrin- and non-clathrin-mediated endocytic regulation of cell signalling. Nat Rev Mol Cell Biol. 2005;6:112-26.
7. Seaman MN. Membrane traffic in the secretory pathway: Endosome protein sorting: motifs and machinery. Cell Mol Life Sci. 2008;65:2842-58.
8. Grosshans BL, Ortiz D, Novick P. Rabs and their effectors: achieving specificity in membrane traffic. Proc Natl Acad Sci USA. 2006;103:11821-7.
9. Aderem A, Underhill DM. Mechanisms of phagocytosis in macrophages. Annu Rev Immunol. 1999;17:593-623.
10. Haas A. The phagosome: compartment with a license to kill. Traffic. 2007;8:311-30.
11. Vieira OV, Botelho RJ, Grinstein S. Phagosome maturation: aging gracefully. Biochem J. 2002;366:689-704.
12. Scott CC, Botelho RJ, Grinstein S. Phagosome maturation: a few bugs in the system. J Membr Biol. 2003;193:137-52.
13. Underhill DM, Ozinsky A. Phagocytosis of microbes: complexity in action. Annu Rev Immunol. 2002;20:825-52.
14. Clemens DL. Characterization of the Mycobacterium tuberculosis phagosome. Trends Microbiol. 1996;4:113-8.
15. Chua J, Deretic V. Mycobacterium tuberculosis reprograms waves of phosphatidylinositol 3-phosphate on phagosomal organelles. J Biol Chem. 2004;279:36982-92.
16. Kusner DJ. Mechanisms of mycobacterial persistence in tuberculosis. Clin Immunol. 2005;114:239-47.
17. Deretic V, Singh S, Master S, Harris J, Roberts E, Kyei G, et al. Mycobacterium tuberculosis inhibition of phagolysosome biogenesis and autophagy as a host defense mechanism. Cell Microbiol. 2006;8:719-27.
18. Spiegel S, Kolesnick R. Sphingosine 1-phosphate as a therapeutic agent. Leukemia. 2002;16:1596-602.
19. Yadav M, Clark L, Schorey JS. Macrophage's proinflammatory response to a mycobacterial infection is dependent on sphingosine kinase-mediated activation of phosphatidylinositol phospholipase C, protein kinase C, ERK1/2, and phosphatidylinositol 3-kinase. J Immunol. 2006;176:5494-503.
20. Colombo MI, Beron W, Stahl PD. Calmodulin regulates endosome fusion. J Biol Chem. 1997;272:7707-12.
21. Lindmo K, Stenmark H. Regulation of membrane traffic by phosphoinositide 3-kinases. J Cell Sci. 2006;119:605-14.
22. Deretic V, Fratti RA. Mycobacterium tuberculosis phagosome. Mol Microbiol. 1999;31:1603-9.
23. Chua J, Vergne I, Master S, Deretic V. A tale of two lipids: Mycobacterium tuberculosis phagosome maturation arrest. Curr Opin Microbiol. 2004;7:71-7.
24. Garin J, Diez R, Kieffer S, Dermine JF, Duclos S, Gagnon E, et al. The phagosome proteome: insight into phagosome functions. J Cell Biol. 2001;152:165-80.
25. Gagnon E, Duclos S, Rondeau C, Chevet E, Cameron PH, Steele-Mortimer O, et al. Endoplasmic reticulum-mediated phagocytosis is a mechanism of entry into macrophages. Cell. 2002;110:119-31.
26. 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;23:2501-14.
27. Stow JL, Manderson AP, Murray RZ. SNAREing immunity: the role of SNAREs in the immune system. Nat Rev Immunol. 2006;6:919-29.
28. Zhao C, Slevin JT, Whiteheart SW. Cellular functions of NSF: not just SNAPs and SNAREs. FEBS Lett. 2007;581:2140-9.
29. Hong W. Cytotoxic T lymphocyte exocytosis: bring on the SNAREs! Trends Cell Biol. 2005;15:644-50.
30. Leabu M. Membrane fusion in cells: molecular machinery and mechanisms. J Cell Mol Med. 2006;10:423-7.
31. Pereira-Leal JB, Seabra MC. Evolution of the Rab family of small GTP-binding proteins. J Mol Biol. 2001;313:889-901.
32. Zerial M, McBride H. Rab proteins as membrane organizers. Nat Rev Mol Cell Biol. 2001;2:107-17.
33. Stenmark H, Olkkonen VM. The Rab GTPase family. Genome Biol. 2001;2:3007.
34. Seabra MC, Wasmeier C. Controlling the location and activation of Rab GTPases. Curr Opin Cell Biol. 2004;16:451-7.
35. Heo WD, Inoue T, Park WS, Kim ML, Park BO, Wandless TJ, et al. PI(3,4,5)P3 and PI(4,5)P2 lipids target proteins with polybasic clusters to the plasma membrane. Science. 2006;314:1458-61.
36. Yeung T, Terebiznik M, Yu L, Silvius J, Abidi WM, Philips M, et al. Receptor activation alters inner surface potential during phagocytosis. Science. 2006;313:347-51.
37. Segev N. Ypt and Rab GTPases: insight into functions through novel interactions. Curr Opin Cell Biol. 2001;13: 500-11.
38. Echard A, Jollivet F, Martinez O, Lacapere JJ, Rousselet A, Janoueix-Lerosey I, et al. Interaction of a Golgi-associated kinesin-like protein with Rab6. Science. 1998;279:580-5.
39. Wu X, Rao K, Bowers MB, Copeland NG, Jenkins NA, Hammer JA 3rd. Rab27a enables myosin Va-dependent melanosome capture by recruiting the myosin to the organelle. J Cell Sci. 2001;114:1091-100.
40. Pan H, Yan BS, Rojas M, Shebzukhov YV, Zhou H, Kobzik L, et al. Ipr1 gene mediates innate immunity to tuberculosis. Nature. 2005;434:767-72.
41. Gil DP, Leon LG, Correa LI, Maya JR, Paris SC, Garcia LF, et al. Differential induction of apoptosis and necrosis in monocytes from patients with tuberculosis and healthy control subjects. J Infect Dis. 2004;189:2120-8.
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Cómo citar
1.
Castaño D, Rojas M. Alteraciones en el reclutamiento y activación de proteínas Rab durante la infección micobacteriana. biomedica [Internet]. 4 de agosto de 2010 [citado 16 de abril de 2024];30(2):283-308. Disponible en: https://revistabiomedica.org/index.php/biomedica/article/view/192
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