Mycobacterium tuberculosis Eis protein initiates suppression of host immune responses by acetylation of DUSP16/MKP-7

Proceedings of the National Academy of Sciences of the United States of America

Volumn 109, Issue 20, 2012, Pages 7729-7734

  Kim, Kyoung Hoon ^a   An, Doo Ri ^a   Song, Jinsu ^a   Yoon, Ji Young ^a   Kim, Hyoun Sook ^a   Yoon, Hye Jin ^a   Im, Ha Na ^a   Kim, Jieun ^a   Kim, Do Jin ^a   Lee, Sang Jae ^a   Kim, Ki Hye ^b   Lee, Hye Mi ^b   Kim, Hie Joon ^a   Jo, Eun Kyeong ^b   Lee, Jae Young ^c   Suh, Se Won ^a  

^a Seoul National University   (South Korea)

^b Chungnam National University   (South Korea)

^c Dongguk University   (South Korea)

Author keywords

Antituberculosis drug; Lysine acetylation; Rv2416c

Indexed keywords

ACYLTRANSFERASE; AMIKACIN; BACTERIAL PROTEIN; BACTERIUM LIPOPOLYSACCHARIDE; DUAL SPECIFICITY PROTEIN PHOSPHATASE 16; KANAMYCIN A; MITOGEN ACTIVATED PROTEIN KINASE PHOSPHATASE 7; PAROMOMYCIN; PROTEIN EIS; REACTIVE OXYGEN METABOLITE; TOBRAMYCIN; UNCLASSIFIED DRUG;

ACETYLATION; ARTICLE; AUTOPHAGY; CELL MATURATION; CONTROLLED STUDY; HOST; IMMUNE RESPONSE; MACROPHAGE; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PHAGOSOME; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE; SURVIVAL;

ACETYLATION; ANIMALS; ANTIGENS, BACTERIAL; BACTERIAL PROTEINS; BASE SEQUENCE; BLOTTING, WESTERN; CLONING, MOLECULAR; CRYSTALLIZATION; DUAL-SPECIFICITY PHOSPHATASES; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME-LINKED IMMUNOSORBENT ASSAY; ESCHERICHIA COLI; HOST-PATHOGEN INTERACTIONS; HUMANS; KINETICS; MACROPHAGES; MICE; MITOGEN-ACTIVATED PROTEIN KINASE PHOSPHATASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MYCOBACTERIUM SMEGMATIS; PROTEIN CONFORMATION; SEQUENCE ANALYSIS, DNA; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; X-RAY DIFFRACTION;

MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS;

EID: 84861210566     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1120251109     Document Type: Article

References (45)

1. Dye C, Williams BG (2010) The population dynamics and control of tuberculosis. Science 328:856-861.
2. Chiang CY, Centis R, Migliori GB (2010) Drug-resistant tuberculosis: Past, present, future. Respirology 15:413-432.
3. Dahl JL, Wei J, Moulder JW, Laal S, Friedman RL (2001) Subcellular localization of the Iitracellular survival-enhancing Eis protein of Mycobacterium tuberculosis. Infect Immun 69:4295-4302. (Pubitemid 32574425)
4. Lin PL, Flynn JL (2010) Understanding latent tuberculosis: A moving target. J Immunol 185:15-22.
5. Getahun H, Gunneberg C, Granich R, Nunn P (2010) HIV infection-associated tuberculosis: The epidemiology and the response. Clin Infect Dis 50(Suppl 3):S201-S207.
6. Jo EK, Yang CS, Choi CH, Harding CV (2007) Intracellular signalling cascades regulating innate immune responses to Mycobacteria: Branching out from Toll-like receptors. Cell Microbiol 9:1087-1098. (Pubitemid 46547129)
7. Wei J, et al. (2000) Identification of a Mycobacterium tuberculosis gene that enhances mycobacterial survival in macrophages. J Bacteriol 182:377-384. (Pubitemid 30030121)
8. Meena LS, Rajni (2010) Survival mechanisms of pathogenic Mycobacterium tuberculosis H37Rv. FEBS J 277:2416-2427.
9. Ehrt S, Schnappinger D (2009) Mycobacterial survival strategies in the phagosome: Defence against host stresses. Cell Microbiol 11:1170-1178.
10. Vergne I, Chua J, Singh SB, Deretic V (2004) Cell biology of Mycobacterium tuberculosis phagosome. Annu Rev Cell Dev Biol 20:367-394. (Pubitemid 39488643)
11. Vergne I, et al. (2006) Autophagy in immune defense against Mycobacterium tuberculosis. Autophagy 2:175-178. (Pubitemid 44030880)
12. Kang R, Zeh HJ, Lotze MT, Tang D (2011) The Beclin 1 network regulates autophagy and apoptosis. Cell Death Differ 18:571-580.
13. Wu S, et al. (2009) Activation of the eis gene in a W-Beijing strain of Mycobacterium tuberculosis correlates with increased SigA levels and enhanced intracellular growth. Microbiology 155:1272-1281.
14. Lella RK, Sharma C (2007) Eis (enhanced intracellular survival) protein of Mycobacterium tuberculosis disturbs the cross regulation of T-cells. J Biol Chem 282:18671-18675. (Pubitemid 47100130)
15. Samuel LP, et al. (2007) Expression, production and release of the Eis protein by Mycobacterium tuberculosis during infection of macrophages and its effect on cytokine secretion. Microbiology 153:529-540.
16. Shin DM, et al. (2010) Mycobacterium tuberculosis eis regulates autophagy, inflammation, and cell death through redox-dependent signaling. PLoS Pathog 6:e1001230.
17. Masuda K, Shima H, Watanabe M, Kikuchi K (2001) MKP-7, a novel mitogen-activated protein kinase phosphatase, functions as a shuttle protein. J Biol Chem 276:39002-39011.
18. Neuwald AF, Landsman D (1997) GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends Biochem Sci 22:154-155. (Pubitemid 27199313)
19. Zaunbrecher MA, Sikes RD, Jr., Metchock B, Shinnick TM, Posey JE (2009) Overexpression of the chromosomally encoded aminoglycoside acetyltransferase eis confers kanamycin resistance in Mycobacterium tuberculosis. Proc Natl Acad Sci USA 106:20004-20009.
20. Chen W, Biswas T, Porter VR, Tsodikov OV, Garneau-Tsodikova S (2011) Unusual regioversatility of acetyltransferase Eis, a cause of drug resistance in XDR-TB. Proc Natl Acad Sci USA 108:9804-9808.
21. Crossman DK (2007) Characterization of a novel acetylatransferase found only in pathogenic strains of Mycobacterium tuberculosis. PhD thesis (Univ of Alabama, Tuscaloosa, AL).
22. Cao W, Bao C, Padalko E, Lowenstein CJ (2008) Acetylation of mitogen-activated protein kinase phosphatase-1 inhibits Toll-like receptor signaling. J Exp Med 205:1491-1503. (Pubitemid 351831502)
23. Chi H, Flavell RA (2008) Acetylation of MKP-1 and the control of inflammation. Sci Signal 1:pe44.
24. Tanoue T, Yamamoto T, Maeda R, Nishida E (2001) A Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and p38 alpha and beta MAPKs. J Biol Chem 276:26629-26639.
25. Han SY, Kim SH, Heasley LE (2002) Differential gene regulation by specific gain-of-function JNK1 proteins expressed in Swiss 3T3 fibroblasts. J Biol Chem 277:47167-47174.
26. Matsuguchi T, Musikacharoen T, Johnson TR, Kraft AS, Yoshikai Y (2001) A novel mitogen-activated protein kinase phosphatase is an important negative regulator of lipopolysaccharide-mediated c-Jun N-terminal kinase activation in mouse macrophage cell lines. Mol Cell Biol 21:6999-7009. (Pubitemid 32911259)
27. Weston CR, Davis RJ (2007) The JNK signal transduction pathway. Curr Opin Cell Biol 19:142-149. (Pubitemid 46386399)
28. Kondoh K, Nishida E (2007) Regulation of MAP kinases by MAP kinase phosphatases. Biochim Biophys Acta 1773:1227-1237. (Pubitemid 47125976)
29. Assi K, Pillai R, Gómez-Muñoz A, Owen D, Salh B (2006) The specific JNK inhibitor SP600125 targets tumour necrosis factor-α production and epithelial cell apoptosis in acute murine colitis. Immunology 118:112-121.
30. Jang S, Kelley KW, Johnson RW (2008) Luteolin reduces IL-6 production in microglia by inhibiting JNK phosphorylation and activation of AP-1. Proc Natl Acad Sci USA 105:7534-7539. (Pubitemid 351830053)
31. Russell DG (2001) Mycobacterium tuberculosis: Here today, and here tomorrow. Nat Rev Mol Cell Biol 2:569-577.
32. Gutierrez MG, et al. (2004) Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages. Cell 119:753-766. (Pubitemid 40017683)
33. Funderburk SF, Wang QJ, Yue Z (2010) The Beclin 1-VPS34 complex - at the crossroads of autophagy and beyond. Trends Cell Biol 20:355-362.
34. Wei Y, Pattingre S, Sinha S, Bassik M, Levine B (2008) JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy. Mol Cell 30:678-688. (Pubitemid 351818252)
35. Chambers JW, LoGrasso PV (2011) Mitochondrial c-Jun N-terminal kinase (JNK) signaling initiates physiological changes resulting in amplification of reactive oxygen species generation. J Biol Chem 286:16052-16062.
36. Djavaheri-Mergny M, Maiuri MC, Kroemer G (2010) Cross talk between apoptosis and autophagy by caspase-mediated cleavage of Beclin 1. Oncogene 29:1717-1719.
37. Wirawan E, et al. (2010) Caspase-mediated cleavage of Beclin-1 inactivates Beclin-1-induced autophagy and enhances apoptosis by promoting the release of proapoptotic factors from mitochondria. Cell Death Dis 1:e18.
38. Mukherjee S, et al. (2006) Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation. Science 312:1211-1214. (Pubitemid 43801146)
39. Mukherjee S, Hao YH, Orth K (2007) A newly discovered post-translational modification - the acetylation of serine and threonine residues. Trends Biochem Sci 32:210-216. (Pubitemid 46694332)
40. Close P, et al. (2010) The emerging role of lysine acetylation of non-nuclear proteins. Cell Mol Life Sci 67:1255-1264.
41. Kim GW, Yang XJ (2011) Comprehensive lysine acetylomes emerging from bacteria to humans. Trends Biochem Sci 36:211-220.
42. Norris KL, Lee JY, Yao TP (2009) Acetylation goes global: The emergence of acetylation biology. Sci Signal 2:pe76.
43. Walburger A, et al. (2004) Protein kinase G from pathogenic mycobacteria promotes survival within macrophages. Science 304:1800-1804. (Pubitemid 38787896)
44. Nguyen L, Pieters J (2009) Mycobacterial subversion of chemotherapeutic reagents and host defense tactics: Challenges in tuberculosis drug development. Annu Rev Pharmacol Toxicol 49:427-453.
45. Roepstorff P, Fohlman J (1984) Proposal for a common nomenclature for sequence ions in mass spectra of peptides. Biomed Mass Spectrom 11:601.