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Bacterial virulence factors targeting Rho GTPases: parasitism or symbiosis?

Boquet, Patrice, Lemichez, Emmanuel·2003·Trends in Cell Biology
DOI 10.1016/s0962-8924(03)00037-0
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Abstract

In the past few years, an important question in microbiology has arisen from reports indicating that several pathogenic bacteria have evolved virulence factors directed towards a Ras subfamily of GTPases, namely the Rho GTPases. Progress made in studying both the virulence factors and the signaling pathways involving Rho GTPases has shed light on this crosstalk. One central question is raised by the findings that both activating and inactivating virulence factors that target Rho GTPases coexist in some pathogenic bacteria. Further studies on this peculiar aspect of the bacteria-host cell interactions, which leads to the outbreak of infectious diseases, might clarify whether this aspect of Rho GTPase activation or inactivation represents a finely adapted response of the pathogen for its own benefit or might lead to a reaction of the host against the bacteria.

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Research works printed but not linked: 58

  1. Madaule, 1985, A novel Ras-related gene family, Cell, 41, 31, 10.1016/0092-8674(85)90058-3 · DOI
  2. Chardin, 1989, The mammalian G-protein RhoC is ADP-ribosylated by Clostridium botulinum exoenzyme C3 and affects microfilaments in Vero cells, EMBO J., 8, 1087, 10.1002/j.1460-2075.1989.tb03477.x · DOI
  3. Rubin, 1988, Functional modification of a 21 kilodalton G-protein when ADP-ribosylated by exoenzyme C3 of Clostridium botulinum, Mol. Cell. Biol., 8, 418, 10.1128/MCB.8.1.418 · DOI
  4. Aktories, 1987, Clostridium botulinum type C produces a novel ADP-ribosyltransferase distinct from botulinum C2 toxin, FEBS Lett., 212, 109, 10.1016/0014-5793(87)81566-1 · DOI
  5. Didsbury, 1989, Rac, a novel ras-related family of proteins that are botulinum toxin substrates, J. Biol. Chem., 264, 16378, 10.1016/S0021-9258(19)84716-6 · DOI · Paper page
  6. Hall, 1998, Rho GTPases and the actin cytoskeleton, Science, 279, 509, 10.1126/science.279.5350.509 · DOI
  7. Symons, 2000, Rho family GTPases: more than simple switches, Trends Cell Biol., 10, 415, 10.1016/S0962-8924(00)01832-8 · DOI · Paper page
  8. Machesky, 1999, The Arp2/3 complex: a multifunctional actin organizer, Curr. Opin. Cell Biol., 11, 117, 10.1016/S0955-0674(99)80014-3 · DOI
  9. Bishop, 2000, Rho GTPases and their effector proteins, Biochem. J., 348, 241, 10.1042/0264-6021:3480241 · DOI
  10. Chimini, 2000, Function of Rho family proteins in actin dynamics during phagocytosis and engulfment, Nat. Cell Biol., 2, E191, 10.1038/35036454 · DOI
  11. Van Aelst, 1997, Rho GTPases and signaling networks, Genes Dev., 11, 2295, 10.1101/gad.11.18.2295 · DOI
  12. Bishop, 2000, Rho GTPases and their effector proteins, Biochem. J., 348, 241, 10.1042/bj3480241 · DOI · Paper page
  13. Tato, 2002, Host-pathogen interactions: subversion and utilization of the NF-κB pathway during infection, Infect. Immun., 70, 3311, 10.1128/IAI.70.7.3311-3317.2002 · DOI
  14. Schneider, 2002, Plant immunity and fim noir: what gumshoe detectives can teach us about plant-pathogen interaction, Cell, 109, 537, 10.1016/S0092-8674(02)00764-X · DOI
  15. Janeway, 2001, How the immune system works to protect the host from infection: a personal view, Proc. Natl. Acad. Sci. U. S. A., 98, 7461, 10.1073/pnas.131202998 · DOI
  16. Imler, 2001, Toll receptor in innate immunity, Trends Cell Biol., 11, 304, 10.1016/S0962-8924(01)02004-9 · DOI
  17. Girardin, 2002, Intracellular vs extracellular recognition of pathogens – common concepts in mammals and flies, Trends Microbiol., 10, 193, 10.1016/S0966-842X(02)02334-X · DOI
  18. Hornef, 2002, Bacterial strategies for overcoming host innate and adaptive immune responses, Nat. Immun., 3, 1033, 10.1038/ni1102-1033 · DOI
  19. Hueck, 1998, Type III protein secretion systems in bacterial pathogens of animals and plants, Microbiol. Mol. Biol. Rev., 62, 379, 10.1128/MMBR.62.2.379-433.1998 · DOI
  20. Covacci, 2000, Tyrosine-phosphorylated bacterial proteins: trojan horses for the host cell, J. Exp. Med., 191, 587, 10.1084/jem.191.4.587 · DOI
  21. Madden, 2001, Cytolysin-mediated translocation: a functional equivalent of type III secretion in Gram positive bacteria, Cell, 104, 143, 10.1016/S0092-8674(01)00198-2 · DOI
  22. Falnes, 2000, Penetration of protein toxins into cells, Curr. Opin. Cell Biol., 12, 407, 10.1016/S0955-0674(00)00109-5 · DOI
  23. Doye, 2002, CNF1 exploits the ubiquitin-proteasome machinery to restrict Rho GTPase activation for bacterial host cell invasion, Cell, 111, 553, 10.1016/S0092-8674(02)01132-7 · DOI
  24. Lerm, 2002, Proteasomal degradation of cytotoxic necrotizing factor 1-activated Rac, Infect. Immun., 70, 4053, 10.1128/IAI.70.8.4053-4058.2002 · DOI
  25. Shao, 2002, A Yersinia effector and a Pseudomonas avirulence protein define a family of cysteine protease functioning in bacterial pathogenesis, Cell, 109, 575, 10.1016/S0092-8674(02)00766-3 · DOI
  26. Barbieri, 2002, Bacterial toxins that modify the actin cytoskeleton, Annu. Rev. Cell Dev. Biol., 18, 315, 10.1146/annurev.cellbio.18.012502.134748 · DOI
  27. Boquet, 2002, 225, 10.1016/S0580-9517(02)31013-4 · DOI
  28. Stebbins, 2000, Modulation of host signaling by bacterial mimic: structure of the Salmonella effector SptP bound to Rac1, Mol. Cell, 6, 1449, 10.1016/S1097-2765(00)00141-6 · DOI · Paper page
  29. Cornelis, 2002, Yersinia type III secretion: send in the effectors, J. Cell Biol., 158, 401, 10.1083/jcb.200205077 · DOI
  30. Rittinger, 1997, Structure at 1,65 A of RhoA and its GTPase-activating protein in complex with transition-state analogue, Nature, 389, 758, 10.1038/39651 · DOI
  31. Viboud, 2001, A bacterial type III secretion system inhibits actin polymerization to prevent pore formation in host cells membrane, EMBO J., 20, 5373, 10.1093/emboj/20.19.5373 · DOI
  32. Lockman, 2002, Yersinia tuberculosis produces a cytotoxic necrotizing factor, Infect. Immun., 70, 2708, 10.1128/IAI.70.5.2708-2714.2002 · DOI
  33. Collard, 1996, Signaling pathways regulated by Rho-like proteins: a possible role in tumor formation and metastasis, Int. J. Oncol., 8, 131
  34. Rihet, 2001, Mutation status of genes encoding RhoA, Rac1 and Cdc42 GTPases in a panel of invasive human colorectal and breast tumors, J. Cancer Res. Clin. Oncol., 127, 733, 10.1007/s004320100272 · DOI
  35. Hardt, 1998, Salmonella typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells, Cell, 93, 815, 10.1016/S0092-8674(00)81442-7 · DOI
  36. Buchwald, 2002, Structural basis for the reversible activation of a Rho protein by the bacterial toxin SopE, EMBO J., 21, 3286, 10.1093/emboj/cdf329 · DOI · Paper page
  37. Friebel, 2001, SopE and SopE2 from Salmonella typhimurium activate different sets of Rho GTPases of host cell, J. Biol. Chem., 276, 34035, 10.1074/jbc.M100609200 · DOI
  38. Galàn, 2000, Striking balance: modulation of the actin cytoskeleton by Salmonella, Proc. Natl. Acad. Sci. U. S. A., 97, 8754, 10.1073/pnas.97.16.8754 · DOI
  39. Zhou, 2001, A Salmonella inositol polyphosphatase acts in conjunction with other bacterial effectors to promote host cell actin cytoskeleton rearrangements and bacterial internalization, Mol. Microbiol., 39, 248, 10.1046/j.1365-2958.2001.02230.x · DOI
  40. Marcus, 2002, Salmonella enterica serovar typhimurium effector SigD/SopB is membrane associated and ubiquitinated inside host cells, Cell. Microbiol., 4, 435, 10.1046/j.1462-5822.2002.00202.x · DOI
  41. May, 2000, Phagocytosis and the actin cytoskeleton, J. Cell Sci., 114, 1061, 10.1242/jcs.114.6.1061 · DOI · Paper page
  42. Bajno, 2000, Focal exocytosis of VAMP3-containing vesicles at sites of phagosome formation, J. Cell Biol., 149, 697, 10.1083/jcb.149.3.697 · DOI
  43. Gagnon, 2002, Endoplasmic reticulum-mediated phagocytosis is a mechanism of entry into macrophages, Cell, 110, 119, 10.1016/S0092-8674(02)00797-3 · DOI
  44. Tran Van Nhieu, 1999, IpaC induces actin polymerization and filopodia formation during Shigella entry into epithelial cells, EMBO J., 18, 3249, 10.1093/emboj/18.12.3249 · DOI
  45. Bourdet-Sicard, 1999, Binding of the Shigella IpaA to vinculin induces F-actin depolymerization, EMBO J., 18, 5853, 10.1093/emboj/18.21.5853 · DOI
  46. Duménil, 2000, Src tyrosine kinase activity down-regulates Rho-dependent responses during Shigella entry into epithelial cells and stress fibre formation, J. Cell Sci., 113, 71, 10.1242/jcs.113.1.71 · DOI
  47. Staskawitcz, 2001, Common and contrasting themes of plant and animal diseases, Science, 292, 2285, 10.1126/science.1062013 · DOI
  48. Fiorentini, C. et al. Hijacking Rho GTPases by protein toxins: molecular strategies of pathogenic bacteria. Cell Death Differ. (in press). · DOI
  49. Dukuzumuremyi, 2000, The Yersinia protein kinase A is a host factor inducible RhoA/Rac-binding virulence factor, J. Biol. Chem., 275, 35281, 10.1074/jbc.M003009200 · DOI
  50. Churin, 2001, Pathogenicity island-dependent activation of Rho GTPases Rac1 and Cdc42 in Helicobacterpylori infection, Mol. Microbiol., 40, 815, 10.1046/j.1365-2958.2001.02443.x · DOI
  51. Von Pawell-Rammingen, 2000, GAP activity of the Yersinia YopE eytotoxin specifically targets the Rho pathway: a mechanism for disruption of actin microfilament structure, Mol. Microbiol., 36, 737, 10.1046/j.1365-2958.2000.01898.x · DOI
  52. Hauck, 1998, CD66-mediated phagocytosis of Opa52 Nesseria gonorrhoeae requires a Src-like tyrosine kinase and Rac1-dependent signaling pathway, EMBO J., 17, 443, 10.1093/emboj/17.2.443 · DOI
  53. Eugène, 2002, Microvilli-like structures are associated with the internalization of virulent capsulated Neisseria meningitidis into vascular endothelium, J. Cell Sci., 115, 1231, 10.1242/jcs.115.6.1231 · DOI
  54. Martinez, 2002, Requirement of Rho-family GTPases in the invasion of type 1-piliated uropathogenic Escherichia coli, Cell. Microbiol., 4, 19, 10.1046/j.1462-5822.2002.00166.x · DOI
  55. Gallo, 2002, Mixed-lineage kinase control of JNK and p38 MAPK pathways, Nat. Rev. Mol. Cell Biol., 3, 663, 10.1038/nrm906 · DOI
  56. Geneste, 2002, LIM kinase and diaphanous cooperate to regulate serum responsive factors and actin dynamics, J. Cell Biol., 157, 831, 10.1083/jcb.200203126 · DOI
  57. Buetow, 2001, Structure of the Rho-activating domain of Escherichia coli cytotoxic necrotizing factor, Nat. Struct. Biol., 8, 584, 10.1038/89610 · DOI
  58. Würtele, 2001, How Pseudomonas aeruginosa ExoS toxin downregulates Rac, Nat. Struct. Biol., 8, 23, 10.1038/83007 · DOI

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Metadata

Authors
Boquet, P., & Lemichez, E.
Venue
Trends in Cell Biology
Publisher
Elsevier BV
Published
2003-05
Volume
13
Issue
5
Pages
238-246
ISSN
0962-8924
DOI
10.1016/s0962-8924(03)00037-0
Cited by
149
References
2
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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