Cross Kingdom Activators of Five Classes of Bacterial Effectors

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Vyšlo v časopise: Cross Kingdom Activators of Five Classes of Bacterial Effectors. PLoS Pathog 11(7): e32767. doi:10.1371/journal.ppat.1004944
Kategorie: Pearls
prolekare.web.journal.doi_sk: 10.1371/journal.ppat.1004944


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1. Anderson DM, Schmalzer KM, Sato H, Casey M, Terhune SS, Haas AL, et al. Ubiquitin and ubiquitin-modified proteins activate the Pseudomonas aeruginosa T3SS cytotoxin, ExoU. Molecular microbiology. 2011;82(6):1454–67. doi: 10.1111/j.1365-2958.2011.07904.x 22040088

2. Anderson DM, Sato H, Dirck AT, Feix JB, Frank DW. Ubiquitin activates patatin-like phospholipases from multiple bacterial species. Journal of bacteriology. 2015;197(3):529–41. doi: 10.1128/JB.02402-14 25404699

3. Rahman MS, Ammerman NC, Sears KT, Ceraul SM, Azad AF. Functional characterization of a phospholipase A(2) homolog from Rickettsia typhi. Journal of bacteriology. 2010;192(13):3294–303. doi: 10.1128/JB.00155-10 20435729

4. Rahman MS, Gillespie JJ, Kaur SJ, Sears KT, Ceraul SM, Beier-Sexton M, et al. Rickettsia typhi possesses phospholipase A2 enzymes that are involved in infection of host cells. PLoS pathogens. 2013;9(6):e1003399. doi: 10.1371/journal.ppat.1003399 23818842

5. Housley NA, Winkler HH, Audia JP. The Rickettsia prowazekii ExoU homologue possesses phospholipase A1 (PLA1), PLA2, and lyso-PLA2 activities and can function in the absence of any eukaryotic cofactors in vitro. Journal of bacteriology. 2011;193(18):4634–42. doi: 10.1128/JB.00141-11 21764940

6. Silverman DJ, Santucci LA, Meyers N, Sekeyova Z. Penetration of host cells by Rickettsia rickettsii appears to be mediated by a phospholipase of rickettsial origin. Infection and immunity. 1992;60(7):2733–40. 1612741

7. Winkler HH, Daugherty RM. Phospholipase A activity associated with the growth of Rickettsia prowazekii in L929 cells. Infection and immunity. 1989;57(1):36–40. 2491840

8. Gaspar AH, Machner MP. VipD is a Rab5-activated phospholipase A1 that protects Legionella pneumophila from endosomal fusion. Proceedings of the National Academy of Sciences of the United States of America. 2014;111(12):4560–5. doi: 10.1073/pnas.1316376111 24616501

9. Christen M, Coye LH, Hontz JS, LaRock DL, Pfuetzner RA, Megha, et al. Activation of a bacterial virulence protein by the GTPase RhoA. Science signaling. 2009;2(95):ra71. doi: 10.1126/scisignal.2000430 19887681

10. Kolodziejek AM, Miller SI. Salmonella modulation of the phagosome membrane, role of SseJ. Cellular microbiology. 2015;17(3):333–41. doi: 10.1111/cmi.12420 25620407

11. Witowski SE, Walker KA, Miller VL. YspM, a newly identified Ysa type III secreted protein of Yersinia enterocolitica. Journal of bacteriology. 2008;190(22):7315–25. doi: 10.1128/JB.00861-08 18805975

12. Coburn J, Kane AV, Feig L, Gill DM. Pseudomonas aeruginosa exoenzyme S requires a eukaryotic protein for ADP-ribosyltransferase activity. The Journal of biological chemistry. 1991;266(10):6438–46. 1901061

13. Fu H, Coburn J, Collier RJ. The eukaryotic host factor that activates exoenzyme S of Pseudomonas aeruginosa is a member of the 14-3-3 protein family. Proceedings of the National Academy of Sciences of the United States of America. 1993;90(6):2320–4. 8460141

14. Sha J, Wang SF, Suarez G, Sierra JC, Fadl AA, Erova TE, et al. Further characterization of a type III secretion system (T3SS) and of a new effector protein from a clinical isolate of Aeromonas hydrophila—part I. Microbial pathogenesis. 2007;43(4):127–46. 17644303

15. Kodama T, Rokuda M, Park KS, Cantarelli VV, Matsuda S, Iida T, et al. Identification and characterization of VopT, a novel ADP-ribosyltransferase effector protein secreted via the Vibrio parahaemolyticus type III secretion system 2. Cellular microbiology. 2007;9(11):2598–609. 17645751

16. Yahr TL, Barbieri JT, Frank DW. Genetic relationship between the 53- and 49-kilodalton forms of exoenzyme S from Pseudomonas aeruginosa. Journal of bacteriology. 1996;178(5):1412–9. 8631719

17. Sun J, Barbieri JT. Pseudomonas aeruginosa ExoT ADP-ribosylates CT10 regulator of kinase (Crk) proteins. The Journal of biological chemistry. 2003;278(35):32794–800. 12807879

18. Vilches S, Wilhelms M, Yu HB, Leung KY, Tomas JM, Merino S. Aeromonas hydrophila AH-3 AexT is an ADP-ribosylating toxin secreted through the type III secretion system. Microbial pathogenesis. 2008;44(1):1–12. 17689917

19. Orth K, Palmer LE, Bao ZQ, Stewart S, Rudolph AE, Bliska JB, et al. Inhibition of the mitogen-activated protein kinase kinase superfamily by a Yersinia effector. Science. 1999;285(5435):1920–3. 10489373

20. Mittal R, Peak-Chew SY, Sade RS, Vallis Y, McMahon HT. The acetyltransferase activity of the bacterial toxin YopJ of Yersinia is activated by eukaryotic host cell inositol hexakisphosphate. The Journal of biological chemistry. 2010;285(26):19927–34. doi: 10.1074/jbc.M110.126581 20430892

21. Lee AH, Hurley B, Felsensteiner C, Yea C, Ckurshumova W, Bartetzko V, et al. A bacterial acetyltransferase destroys plant microtubule networks and blocks secretion. PLoS pathogens. 2012;8(2):e1002523. doi: 10.1371/journal.ppat.1002523 22319451

22. Lupardus PJ, Shen A, Bogyo M, Garcia KC. Small molecule-induced allosteric activation of the Vibrio cholerae RTX cysteine protease domain. Science. 2008;322(5899):265–8. doi: 10.1126/science.1162403 18845756

23. Pruitt RN, Chagot B, Cover M, Chazin WJ, Spiller B, Lacy DB. Structure-function analysis of inositol hexakisphosphate-induced autoprocessing in Clostridium difficile toxin A. The Journal of biological chemistry. 2009;284(33):21934–40. doi: 10.1074/jbc.M109.018929 19553670

24. Ray S, Taylor M, Banerjee T, Tatulian SA, Teter K. Lipid rafts alter the stability and activity of the cholera toxin A1 subunit. The Journal of biological chemistry. 2012;287(36):30395–405. doi: 10.1074/jbc.M112.385575 22787142

25. Kahn RA, Gilman AG. The protein cofactor necessary for ADP-ribosylation of Gs by cholera toxin is itself a GTP binding protein. The Journal of biological chemistry. 1986;261(17):7906–11. 3086320

26. Drum CL, Yan SZ, Bard J, Shen YQ, Lu D, Soelaiman S, et al. Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin. Nature. 2002;415(6870):396–402. 11807546

27. Tang WJ, Guo Q. The adenylyl cyclase activity of anthrax edema factor. Molecular aspects of medicine. 2009;30(6):423–30. doi: 10.1016/j.mam.2009.06.001 19560485

28. Guo Q, Jureller JE, Warren JT, Solomaha E, Florian J, Tang WJ. Protein-protein docking and analysis reveal that two homologous bacterial adenylyl cyclase toxins interact with calmodulin differently. The Journal of biological chemistry. 2008;283(35):23836–45. doi: 10.1074/jbc.M802168200 18583346

29. Yahr TL, Vallis AJ, Hancock MK, Barbieri JT, Frank DW. ExoY, an adenylate cyclase secreted by the Pseudomonas aeruginosa type III system. Proceedings of the National Academy of Sciences of the United States of America. 1998;95(23):13899–904. 9811898

30. Ochoa CD, Alexeyev M, Pastukh V, Balczon R, Stevens T. Pseudomonas aeruginosa exotoxin Y is a promiscuous cyclase that increases endothelial tau phosphorylation and permeability. The Journal of biological chemistry. 2012;287(30):25407–18. doi: 10.1074/jbc.M111.301440 22637478

31. Schneider EH, Seifert R. Report on the Third Symposium "cCMP and cUMP as New Second Messengers". Naunyn-Schmiedeberg's archives of pharmacology. 2015;388(1):1–3. doi: 10.1007/s00210-014-1072-3 25471064

32. Beckert U, Wolter S, Hartwig C, Bahre H, Kaever V, Ladant D, et al. ExoY from Pseudomonas aeruginosa is a nucleotidyl cyclase with preference for cGMP and cUMP formation. Biochemical and biophysical research communications. 2014;450(1):870–4. doi: 10.1016/j.bbrc.2014.06.088 24971548

33. Gottle M, Dove S, Kees F, Schlossmann J, Geduhn J, Konig B, et al. Cytidylyl and uridylyl cyclase activity of Bacillus anthracis edema factor and Bordetella pertussis CyaA. Biochemistry. 2010;49(26):5494–503. doi: 10.1021/bi100684g 20521845

34. Bahre H, Hartwig C, Munder A, Wolter S, Stelzer T, Schirmer B, et al. cCMP and cUMP occur in vivo. Biochemical and biophysical research communications. 2015.

35. Trasak C, Zenner G, Vogel A, Yuksekdag G, Rost R, Haase I, et al. Yersinia protein kinase YopO is activated by a novel G-actin binding process. The Journal of biological chemistry. 2007;282(4):2268–77. 17121817

36. Lee WL, Grimes JM, Robinson RC. Yersinia effector YopO uses actin as bait to phosphorylate proteins that regulate actin polymerization. Nature structural & molecular biology. 2015;22(3):248–55.

37. Grishin AM, Condos TE, Barber KR, Campbell-Valois FX, Parsot C, Shaw GS, et al. Structural basis for the inhibition of host protein ubiquitination by Shigella effector kinase OspG. Structure. 2014;22(6):878–88. doi: 10.1016/j.str.2014.04.010 24856362

38. Pruneda JN, Smith FD, Daurie A, Swaney DL, Villen J, Scott JD, et al. E2~Ub conjugates regulate the kinase activity of Shigella effector OspG during pathogenesis. The EMBO journal. 2014;33(5):437–49. doi: 10.1002/embj.201386386 24446487

39. Zhou Y, Dong N, Hu L, Shao F. The Shigella type three secretion system effector OspG directly and specifically binds to host ubiquitin for activation. PloS one. 2013;8(2):e57558. doi: 10.1371/journal.pone.0057558 23469023

40. Kim DW, Lenzen G, Page AL, Legrain P, Sansonetti PJ, Parsot C. The Shigella flexneri effector OspG interferes with innate immune responses by targeting ubiquitin-conjugating enzymes. Proceedings of the National Academy of Sciences of the United States of America. 2005;102(39):14046–51. 16162672

41. Calder T, Kinch LN, Fernandez J, Salomon D, Grishin NV, Orth K. Vibrio type III effector VPA1380 is related to the cysteine protease domain of large bacterial toxins. PloS one. 2014;9(8):e104387. doi: 10.1371/journal.pone.0104387 25099122

42. Coaker G, Falick A, Staskawicz B. Activation of a phytopathogenic bacterial effector protein by a eukaryotic cyclophilin. Science. 2005;308(5721):548–50. 15746386

43. Coaker G, Zhu G, Ding Z, Van Doren SR, Staskawicz B. Eukaryotic cyclophilin as a molecular switch for effector activation. Molecular microbiology. 2006;61(6):1485–96. 16968222

44. Aumuller T, Jahreis G, Fischer G, Schiene-Fischer C. Role of prolyl cis/trans isomers in cyclophilin-assisted Pseudomonas syringae AvrRpt2 protease activation. Biochemistry. 2010;49(5):1042–52. doi: 10.1021/bi901813e 20050698

45. Spitzer J, Poolman B. The role of biomacromolecular crowding, ionic strength, and physicochemical gradients in the complexities of life's emergence. Microbiology and molecular biology reviews: MMBR. 2009;73(2):371–88. doi: 10.1128/MMBR.00010-09 19487732

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