Cytotoxic glucosyltransferases of Legionella pneumophila

Current Topics in Microbiology and Immunology

Volumn 376, Issue , 2013, Pages 211-226

  Belyi, Yury ^a   Jank, Thomas ^b   Aktories, Klaus ^b  

^a GAMALEYA RESEARCH INSTITUTE OF EPIDEMIOLOGY AND MICROBIOLOGY   (Russian Federation)

^b UNIVERSITY OF FREIBURG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMINOACYL TRANSFER RNA; ELONGATION FACTOR 1ALPHA; GLUCOSYLTRANSFERASE; GUANOSINE TRIPHOSPHATE; LEGIONELLA GLUCOSYLTRANSFERASE 1; LEGIONELLA GLUCOSYLTRANSFERASE 2; LEGIONELLA GLUCOSYLTRANSFERASE 3; SERINE; SETA PROTEIN; SUBVERSION OF EUKARYOTIC TRAFFIC A; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE GLUCOSE;

ARTICLE; BACTERIAL REPRODUCTION; CELL VACUOLE; COMPLEX FORMATION; CRYSTAL STRUCTURE; CYTOTOXICITY; ENDOSOME; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; HUMAN; INTRACELLULAR BACTERIUM; LEGIONELLA PNEUMOPHILA; LEGIONNAIRE DISEASE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN GLYCOSYLATION; PROTEIN SYNTHESIS; PROTEIN SYNTHESIS INHIBITION; SACCHAROMYCES CEREVISIAE;

GLUCOSYLTRANSFERASES; GLYCOSYLATION; HUMANS; LEGIONELLA PNEUMOPHILA; PEPTIDE ELONGATION FACTOR 1; SUBSTRATE SPECIFICITY;

EID: 84886676094     PISSN: 0070217X     EISSN: None     Source Type: Book Series    
DOI: 10.1007/82-2013-338     Document Type: Article

References (75)

1. Abel K et al (1996) An alpha to beta conformational switch in EF-Tu. Structure 4(10):1153-1159
2. Abu-Zant A et al (2007) Anti-apoptotic signalling by the Dot/Icm secretion system of L. pneumophila Cell. Microbiol 9(1):246-264
3. Andersen GR et al (2000) Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha. Mol Cell 6(5):1261-1266
4. 2 protein family. Proc Natl Acad Sci USA 104(12):5121-5126
5. Bartfeld S et al (2009) Temporal resolution of two-tracked NF-kappaB activation by Legionella pneumophila. Cell Microbiol 11(11):1638-1651
6. Belyi I, Popoff MR, Cianciotto NP (2003) Purification and characterization of a UDP-glucosyltransferase produced by Legionella pneumophila. Infect Immun 71(1):181-186
7. Belyi Y, Aktories K (2010) Bacterial toxin and effector glycosyltransferases. Biochim Biophys Acta 1800(2):134-143
8. Belyi Y, Jank T, Aktories K (2011) Effector glycosyltransferases in Legionella. Front Microbiol 2:76
9. Belyi Y et al (2006) Legionella pneumophila glucosyltransferase inhibits host elongation factor 1A. Proc Natl Acad Sci USA 103(45):16953-16958
10. Belyi Y et al (2009) Region of elongation factor 1A1 involved in substrate recognition by Legionella pneumophila glucosyltransferase Lgt1: identification of Lgt1 as a retaining glucosyltransferase. J Biol Chem 284(30):20167-20174
11. Belyi Y et al (2008) Lgt: a family of cytotoxic glucosyltransferases produced by Legionella pneumophila. J Bacteriol 190(8):3026-3035
12. Belyi Y et al (2012) Elongation factor 1A is the target of growth inhibition in yeast caused by Legionella pneumophila glucosyltransferase Lgt1. J Biol Chem 287(31):26029-26037
13. Brombacher E et al (2009) Rab1 guanine nucleotide exchange factor SidM is a major phosphatidylinositol 4-phosphate-binding effector protein of Legionella pneumophila. J Biol Chem 284(8):4846-4856
14. Bruggemann H et al (2006) Virulence strategies for infecting phagocytes deduced from the in vivo transcriptional program of Legionella pneumophila. Cell Microbiol 8(8):1228-1240
15. Busch C et al (1998) A common motif of eukaryotic glycosyltransferases is essential for the enzyme activity of large clostridial cytotoxins. J Biol Chem 273(31):19566-19572
16. Byrne B, Swanson MS (1998) Expression of Legionella pneumophila virulence traits in response to growth conditions. Infect Immun 66(7):3029-3034
17. Cazalet C et al (2010) Analysis of the Legionella longbeachae genome and transcriptome uncovers unique strategies to cause Legionnaires' disease. PLoS Genet 6(2):e1000851
18. de Felipe KS et al (2008) Legionella eukaryotic-like type IV substrates interfere with organelle trafficking. PLoS Pathog 4(8):e1000117
19. de Felipe KS et al (2005) Evidence for acquisition of Legionella type IV secretion substrates via interdomain horizontal gene transfer. J Bacteriol 187(22):7716-7726
20. Diederen BM (2008) Legionella spp. and Legionnaires' disease. J Infect 56(1):1-12
21. Ensminger AW, Isberg RR (2009) Legionella pneumophila Dot/Icm translocated substrates: a sum of parts. Curr Opin Microbiol 12(1):67-73
22. Fontana MF et al (2011) Secreted bacterial effectors that inhibit host protein synthesis are critical for induction of the innate immune response to virulent Legionella pneumophila. PLoS Pathog 7(2):e1001289
23. Franco IS, Shuman HA, Charpentier X (2009) The perplexing functions and surprising origins of Legionella pneumophila type IV secretion effectors. Cell Microbiol 11(10):1435-1443
24. GeJetal(2009)A Legionella type IV effector activates the NF-kappaB pathway byphosphorylating the IkappaB family of inhibitors. Proc Natl Acad Sci USA 106(33):13725-13730
25. Gillooly DJ, Raiborg C, Stenmark H (2003) Phosphatidylinositol 3-phosphate is found in microdomains of early endosomes. Histochem Cell Biol 120(6):445-453
26. Goody PR et al (2012) Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins. EMBO J 31(7):1774-1784
27. Haenssler E, Isberg RR (2011) Control of host cell phosphorylation by legionella pneumophila. Front Microbiol 2:64
28. Heidtman M et al (2009) Large-scale identification of Legionella pneumophila Dot/Icm substrates that modulate host cell vesicle trafficking pathways. Cell Microbiol 11(2):230-248
29. Hilbi H, Weber S, Finsel I (2011) Anchors for effectors: subversion of phosphoinositide lipids by Legionella. Front Microbiol 2:91
30. Hsu F et al (2012) Structural basis for substrate recognition by a unique Legionella phosphoinositide phosphatase. Proc Natl Acad Sci USA 109(34):13567-13572
31. Huang L et al (2011) The E block motif is associated with Legionella pneumophila translocated substrates. Cell Microbiol 13(2):227-245
32. Hurtado-Guerrero R et al (2010) Molecular mechanism of elongation factor 1A inhibition by a Legionella pneumophila glycosyltransferase. Biochem J 426(3):281-292
33. Ingmundson A et al (2007) Legionella pneumophila proteins that regulate Rab1 membrane cycling. Nature 450(7168):365-369
34. Isberg RR, O'Connor TJ, Heidtman M (2009) The Legionella pneumophila replication vacuole: making a cosy niche inside host cells. Nat Rev Microbiol 7(1):13-24
35. Ivanov SS, Roy CR (2009) Modulation of ubiquitin dynamics and suppression of DALIS formation by the Legionella pneumophila Dot/Icm system. Cell Microbiol 11(2):261-278
36. Jank T et al (2012) Domain organization of Legionella effector SetA. Cell Microbiol 14(6):852-868
37. Jank T, Giesemann T, Aktories K (2007) Rho-glucosylating Clostridium difficile toxins A and B: new insights into structure and function. Glycobiology 17(4):15R-22R
38. Just I et al (1995) Glucosylation of Rho proteins by Clostridium difficile toxin B. Nature 375(6531):500-503
39. Kozak NA et al (2010) Virulence factors encoded by Legionella longbeachae identified on the basis of the genome sequence analysis of clinical isolate D-4968. J Bacteriol 192(4):1030-1044
40. Laguna RK et al (2006) A Legionella pneumophila-translocated substrate that is required for growth within macrophages and protection from host cell death. Proc Natl Acad Sci USA 103(49):18745-18750
41. Lairson LL et al (2008) Glycosyltransferases: structures, functions, and mechanisms. Annu Rev Biochem 77:521-555
42. Losick VP et al (2010) LnaB: a Legionella pneumophila activator of NF-kappaB. Cell Microbiol 12(8):1083-1097
43. Lu W et al (2010) Structural basis of the action of glucosyltransferase Lgt1 from Legionella pneumophila. J Mol Biol 396(2):321-331
44. Machner MP, Isberg RR (2007) A bifunctional bacterial protein links GDI displacement to Rab1 activation. Science 318(5852):974-977
45. Moliner C, Fournier PE, Raoult D (2010) Genome analysis of microorganisms living in amoebae reveals a melting pot of evolution. FEMS Microbiol Rev 34(3):281-294
46. Mukherjee S et al (2011) Modulation of Rab GTPase function by a protein phosphocholine transferase. Nature 477(7362):103-106
47. Murata T et al (2006) The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factor. Nat Cell Biol 8(9):971-977
48. Nagai H et al (2002) A bacterial guanine nucleotide exchange factor activates ARF on Legionella phagosomes. Science 295(5555):679-682
49. Nelson RJ et al (1992) The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell 71(1):97-105
50. Neunuebel MR et al (2011) De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila. Science 333(6041):453-456
51. O'Connor TJ et al (2012) Aggravating genetic interactions allow a solution to redundancy in a bacterial pathogen. Science 338(6113):1440-1444
52. Qasba PK, Ramakrishnan B, Boeggeman E (2005) Substrate-induced conformational changes in glycosyltransferases. Trends Biochem Sci 30(1):53-62
53. Ragaz C et al (2008) The Legionella pneumophila phosphatidylinositol-4 phosphate-binding type IV substrate SidC recruits endoplasmic reticulum vesicles to a replication-permissive vacuole. Cell Microbiol 10(12):2416-2433
54. Ramakrishnan V (2002) Ribosome structure and the mechanism of translation. Cell 108(4):557-572
55. Richards AM et al (2013) Cellular microbiology and molecular ecology of Legionella-amoeba interaction. Virulence 4(4):307-314
56. Sadretdinova OV et al (2012) Prevalence of glucosyl transferase Lgt among Legionella pneumophila strains isolated from various sources. Zh Mikrobiol Epidemiol Immunobiol 3:8-12
57. Sarge KD et al (1991) Cloning and characterization of two mouse heat shock factors with distinct inducible and constitutive DNA-binding ability. Genes Dev 5(10):1902-1911
58. Sasikumar AN, Perez WB, Kinzy TG (2012) The many roles of the eukaryotic elongation factor 1 complex. Wiley Interdiscip Rev RNA 3(4):543-555
59. Schoebel S et al (2010) High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA. EMBO Rep 11(8):598-604
60. Schoebel S et al (2011) Protein LidA from Legionella is a Rab GTPase supereffector. Proc Natl Acad Sci USA 108(44):17945-17950
61. Segal G (2013) Identification of Legionella effectors using bioinformatic approaches. Methods Mol Biol 954:595-602
62. Shen X et al (2009) Targeting eEF1A by a Legionella pneumophila effector leads to inhibition of protein synthesis and induction of host stress response. Cell Microbiol 11(6):911-926
63. Shoemaker CJ, Green R (2012) Translation drives mRNA quality control. Nat Struct Mol Biol 19(6):594-601
64. Tan Y, Arnold RJ, Luo ZQ (2011) Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination. Proc Natl Acad Sci USA 108(52):21212-21217
65. Tan Y, Luo ZQ (2011) Legionella pneumophila SidD is a deAMPylase that modifies Rab1. Nature 475(7357):506-509
66. Tzivelekidis T et al (2011) Aminoacyl-tRNA-charged eukaryotic elongation factor 1A is the bona fide substrate for Legionella pneumophila effector glucosyltransferases. PLoS ONE 6(12):e29525
67. Viner R et al (2012) Identification of two Legionella pneumophila effectors that manipulate host phospholipids biosynthesis. PLoS Pathog 8(11):e1002988
68. Weber SS, Ragaz C, Hilbi H (2009) Pathogen trafficking pathways and host phosphoinositide metabolism. Mol Microbiol 71(6):1341-1352
69. Weber SS et al (2006) Legionella pneumophila exploits PI(4)P to anchor secreted effector proteins to the replicative vacuole. PLoS Pathog 2(5):e46
70. Wiggins CA, Munro S (1998) Activity of the yeast MNN1 alpha-1, 3-mannosyltransferase requires a motif conserved in many other families of glycosyltransferases. Proc Natl Acad Sci USA 95(14):7945-7950
71. Xu L, Luo ZQ (2013) Cell biology of infection by Legionella pneumophila. Microbes Infect 15(2):157-167
72. Xu L et al (2010) Inhibition of host vacuolar H+-ATPase activity by a Legionella pneumophila effector. PLoS Pathog 6(3):e1000822
73. Zhu W et al (2011) Comprehensive identification of protein substrates of the Dot/Icm type IV transporter of Legionella pneumophila. PLoS ONE 6(3):e17638
74. Ziegler MO et al (2008) Conformational changes and reaction of clostridial glycosylating toxins. J Mol Biol 377(5):1346-1356
75. Zusman T et al (2007) The response regulator PmrA is a major regulator of the icm/dot type IV secretion system in Legionella pneumophila and Coxiella burnetii. Mol Microbiol 63(5):1508-1523