Rho GTPases as targets of bacterial protein toxins

Biological Chemistry

Volumn 381, Issue 5-6, 2000, Pages 421-426

  Aktories, Klaus ^a   Schmidt, Gudula ^a   Just, Ingo ^a  

^a UNIVERSITY OF FREIBURG   (Germany)

Author keywords

Clostridium botulinum C3 ADP ribosyltransferase; CNF; DNT; ExoS; Large clostridial cytotoxins; SopE; SptP; YopE

Indexed keywords

ASPARAGINE; BACTERIAL PROTEIN; BACTERIAL TOXIN; CLOSTRIDIUM DIFFICILE TOXIN A; CLOSTRIDIUM DIFFICILE TOXIN B; CYTOTOXIN; GLUTAMINE; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; PROTEIN CDC42; RAC PROTEIN; RHO FACTOR; THREONINE; TRANSFERASE;

ADENOSINE DIPHOSPHATE RIBOSYLATION; BORDETELLA BRONCHISEPTICA; CONTROLLED STUDY; DEAMINATION; ENZYME ACTIVATION; ENZYME GLYCOSYLATION; ENZYME INHIBITION; ESCHERICHIA COLI; EUKARYOTIC CELL; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN TARGETING; PSEUDOMONAS AERUGINOSA; REVIEW; SALMONELLA; TARGET CELL; YERSINIA;

BACTERIA (MICROORGANISMS); BORDETELLA BRONCHISEPTICA; CLOSTRIDIUM BOTULINUM; CLOSTRIDIUM DIFFICILE; ESCHERICHIA COLI; EUKARYOTA; EXOS; PSEUDOMONAS; PSEUDOMONAS AERUGINOSA; SALMONELLA; YERSINIA;

EID: 0033924259     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2000.054     Document Type: Review

References (41)

1. Aeschlimann, D., and Paulsson, M. (1994). Transglutaminases: protein cross-linking enzymes in tissue and body fluids. Thromb. Haemost. 71, 402-415.
2. Aktories, K. (1997a). Bacterial toxins that target Rho proteins. J. Clin. Invest. 99, 827-829.
3. Aktories, K. (1997b). Rho proteins: targets for bacterial toxins. Trends Microbiol. 5, 282-288.
4. Aktories, K., Barth, H., and Just, I. (2000). Clostridium botulinum C3 exoenzyme and C3-like transferases. In: Handbook of Experimental Pharmacology, Vol. 145, K. Aktories and I. Just, eds. (Berlin, Germany: Springer Verlag), pp. 207-233.
5. Caprioli, A., Falbo, V., Roda, L.G., Ruggeri, F.M., and Zona, C. (1983). Partial purification and characterization of an Escherichia coli toxic factor that induces morphological cell alterations. Infect. Immun. 39, 1300-1306.
6. Chaves-Olarte, E., Löw, P., Freer, E., Norlin, T., Weidmann, M., von Eichel-Streiber, C., and Thelestam, M. (1999). A novel cytotoxin from Clostridium difficile serogroup F is a functional hybrid between two other large clostridial cytotoxins. J. Biol. Chem. 274, 11046-11052.
7. de Rycke, J., González, E.A., Blanco, J., Oswald, E., Blanco, M., and Boivin, R. (1990). Evidence for two types of cytotoxic necrotizing factor in human and animal clinical isolates of Escherichia coli. J. Clin. Microbiol. 28, 694-699.
8. Fiorentini, C., Donelli, G., Matarrese, P., Fabbri, A., Paradisi, S., and Boquet, P. (1995). Escherichia coli cytotoxic necrotizing factor 1: evidence for induction of actin assembly by constitutive activation of the p21 Rho GTPase. Infect. Immun. 63, 3936-3944.
9. Flatau, G., Lemichez, E., Gauthier, M., Chardin, P., Paris, S., Fiorentini, C., and Boquet, P. (1997). Toxin-induced activation of the G protein p21 Rho by deamidation of glutamine. Nature 387, 729-733.
10. Fu, Y., and Galán, J.E. (1999). A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion. Nature 401, 293-297.
11. Galán, J.E., and Bliska, J.B. (1996). Cross-talk between bacterial pathogens and their host cells. Annu. Rev. Cell Dev. Biol. 12, 221-225.
12. Genth, H., Aktories, K., and Just, I. (1999). Monoglucosylation of RhoA at Threonine-37 blocks cytosol-membrane cycling. J. Biol. Chem. 274, 29050-29056.
13. Goehring, U.-M., Schmidt, G., Pederson, K.J., Aktories, K., and Barbieri, J.T. (1999). The N-terminal domain of Pseudomonas aeruginosa exoenzyme S is a GTPase-activating protein for Rho GTPases. J. Biol. Chem. 274, 36369-36372.
14. Hall, A. (1998). Rho GTPases and the actin cytoskeleton. Science 279, 509-514.
15. Hardt, W.-D., Chen, L.-M., Schuebel, K.E., Bustelo, X.R., and Galán, J.E. (1998). S. typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells. Cell 93, 815-826.
16. Herrmann, C., Ahmadian, M.R., Hofmann, F., and Just, I. (1998). Functional consequences of monoglucosylation of H-Ras at effector domain amino acid threonine-35. J. Biol. Chem. 273, 16134-16139.
17. Horiguchi, Y., Inoue, N., Masuda, M., Kashimoto, T., Katahira, J., Sugimoto, N., and Matsuda, M. (1997). Bordetella bronchiseptica dermonecrotizing toxin induces reorganization of actin stress fibers through deamidation of Gln-63 of the GTP-binding protein Rho. Proc. Natl. Acad. Sci. USA 94, 11623-11626.
18. Just, I., Selzer, J., Wilm, M., Von Eichel-Streiber, C., Mann, M., and Aktories, K. (1995a). Glucosylation of Rho proteins by Clostridium difficile toxin B. Nature 375, 500-503.
19. Just, I., Wilm, M., Selzer, J., Rex, G., Von Eichel-Streiber, C., Mann, M., and Aktories, K. (1995b). The enterotoxin from Clostridium difficile (ToxA) monoglucosylates the Rho proteins. J. Biol. Chem. 270, 13932-13936.
20. Just, I., Selzer, J., Hofmann, F., Green, G.A., and Aktories, K. (1996). Inactivation of Ras by Clostridium sordellii lethal toxin-catalyzed glucosylation. J. Biol. Chem. 271, 10149-10153.
21. Kaniga, K., Uralil, J., Bliska, J.B., and Galandrini, R. (1996). A secreted protein tyrosine phosphatase with modular effector domains in the bacterial pathogen Salmonella typhimurium. Mol. Microbiol. 21, 633-641.
22. Lemichez, E., Flatau, G., Bruzzone, M., Boquet, P., and Gauthier, M. (1997). Molecular localization of the Escherichia coli cytotoxic necrotizing factor CNF1 cell-binding and catalytic domains. Mol. Microbiol. 24, 1061-1070.
23. Lerm, M., Schmidt, G., Goehring, U.-M., Schirmer, J., and Aktories, K. (1999). Identification of the region of Rho involved in substrate recognition by Escherichia coli cytotoxic necrotizing factor 1 (CNF1). J. Biol. Chem. 274, 28999-29004.
24. Masuda, M., Betancourt, L., Matsuzawa, T., Kashimoto, T., Takao, T., Shimonishi, Y., and Horiguchi, Y. (2000). Activation of Rho through a cross-link with polyamines catalyzed by Bordetella dermonecrotizingtoxin. EMBO J. 19, 521-530.
25. Oswald, E., Sugai, M., Labigne, A., Wu, H.C., Fiorentini, C., Boquet, P., and O'Brien, A.D. (1994). Cytotoxic necrotizing factor type 2 produced by virulent Escherichia coli modifies the small GTP-binding proteins Rho involved in assembly of actin stress fibers. Proc. Natl. Acad. Sci. USA 91, 3814-3818.
26. rho induces rapid changes in cell morphology. J. Cell Biol. 111, 1001-1007.
27. Pederson, K.J., Vallis, A.J., Aktories, K., Frank, D.W., and Barbieri, J.T. (1999). The amino-terminal domain of Pseudomonas aeruginosa ExoS disrupts actin filaments via small-molecular-weight GTP-binding proteins. Mol. Microbiol 32, 393-401.
28. Popoff, M.R., Chaves, O.E., Lemichez, E., Von Eichel-Streiber, C., Thelestam, M., Chardin, P., Cussac, D., Chavrier, P., Flatau, G., Giry, M., Gunzburg, J., and Boquet, P. (1996). Ras, Rap, and Rac small GTP-binding proteins are targets for Clostridium sordellii lethal toxin glucosylation. J. Biol. Chem. 271, 10217-10224.
29. Ridley, A. (2000). Rho. In: GTPases, A. Hall, ed. (Oxford, UK: Oxford University Press), pp. 89-136.
30. Schmidt, G., and Aktories, K. (1998). Bacterial cytotoxins target Rho GTPases. Naturwissenschaften 85, 253-261.
31. Schmidt, G., Sehr, P., Wilm, M., Selzer, J., Mann, M., and Aktories, K. (1997). Gln63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor 1. Nature 387, 725-729.
32. Schmidt, G., Selzer, J., Lerm, M., and Aktories, K. (1998). The Rho-deamidating cytotoxic-necrotizing factor CNF1 from Escherichia coli possesses transglutaminase activity - cysteine-866 and histidine-881 are essential for enzyme activity. J. Biol. Chem. 273, 13669-13674.
33. Schmidt, G., Goehring, U.-M., Schirmer, J., Lerm, M., and Aktories, K. (1999). Identification of the C-terminal part of Bordetella dermonecrotic toxin as a transglutaminase for Rho GTPases. J. Biol. Chem. 274, 31875-31881.
34. Sehr, P., Joseph, G., Genth, H., Just, I., Pick, E., and Aktories, K. (1998). Glucosylation and ADP-ribosylation of Rho proteins -effects on nucleotide binding, GTPase activity, and effector-coupling. Biochemistry 37, 5296-5304.
35. Sekine, A., Fujiwara, M., and Narumiya, S. (1989). Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase. J. Biol. Chem. 264, 8602-8605.
36. Selzer, J., Hofmann, F., Rex, G., Wilm, M., Mann, M., Just, I., and Aktories, K. (1996). Clostridium novyi α-toxin-catalyzed incorporation of GIcNAc into Rho subfamily proteins. J. Biol. Chem. 271, 25173-25177.
37. Van Aelst, L., and D'Souza-Schorey, C. (1997). Rho GTPases and signaling networks. Genes Dev. 11, 2295-2322.
38. von Eichel-Streiber, C., Boquet, P., Sauerborn, M., and Thelestam, M. (1996). Large clostridial cytotoxins - a family of glycosyltransferases modifying small GTP-binding proteins. Trends Microbiol. 4, 375-382.
39. von Pawel-Rammingen, U., Telepnev, M.V., Schmidt, G., Aktories, K., Wolf-Watz, H., and Rosqvist, R. (2000). GAP activity of the Yersinia YopE cytotoxin specifically targets the Rho pathway: a mechanism for disruption of actin microfilament structure. Mol. Microbiol., in press,
40. Walker, K.E., and Weiss, A.A. (1994). Characterization of the dermonecrotic toxin in members of the genus Bordetella. Infect. Immun. 62, 3817-3828.
41. Zumbihl, R., Aepfelbacher, M., Andor, A., Jacobi, C.A., Ruckdeschel, K., Ruout, B., and Heesemann, J. (1999). The cytotoxin YopT of Yersinia enterocolitica induces modification and cellular redistribution of the small GTP-binding protein RhoA. J. Biol. Chem. 274, 29289-29293.