Diversion of cytoskeletal processes by Shigella during invasion of epithelial cells

Microbes and Infection

Volumn 2, Issue 7, 2000, Pages 813-819

  Bourdet Sicard, Raphaëlle ^a   Egile, Coumaran ^a   J Sansonetti, Philippe ^a   Tran Van Nhieu, Guy ^a  

^a INSERM   (France)

Author keywords

Actin; IcsA; Ipa protein; RhoGTPases; Shigella

Indexed keywords

ACTIN; CYTOSKELETON PROTEIN; GUANOSINE TRIPHOSPHATASE; PROTEIN TYROSINE KINASE; VINCULIN;

ACTIN FILAMENT; ACTIN POLYMERIZATION; ARTICLE; CELL INVASION; CELL MOTILITY; CYTOSKELETON; DEPOLYMERIZATION; EPITHELIUM CELL; NONHUMAN; PRIORITY JOURNAL; SHIGELLA; SHIGELLOSIS; SIGNAL TRANSDUCTION;

EID: 0033919670     PISSN: 12864579     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1286-4579(00)90366-6     Document Type: Review

References (45)

1. Sansonetti P. Molecular and cellular mechanisms of invasion of the intestinal barrier by enteric pathogens. The paradigm of Shigella. Folia Microbiol. 74:1998;239-246.
2. Parsot C., Sansonetti P.J. Miller V.L. Bacterial Invasiveness. 1996;25-42 Springer Verlag, Munchen.
3. Sansonetti P., Egile C. Molecular basis of cell invasion by Shigella flexneri. Int. J. Gen. Mol. Microbiol. 2:1998;191-197.
4. Tran Van Nhieu G., Sansonetti P.J. Mechanism of Shigella entry into epithelial cells. Curr. Op. Microbiol. 129:1999;51-55.
5. Adam T., Arpin M., Prévost M.C., Gounon P., Sansonetti P.J. Cytoskeletal rearrangements and the functional role for T-plastin during entry of Shigella flexneri into HeLa cells. J. Cell Biol. 16:1995;367-381.
6. Tran Van Nhieu G., Ben Ze'ev A., Sansonetti P.J. Modulation of bacterial entry into epithelial cells by interaction between vinculin and the Shigella IpaA invasin. EMBO J. 126:1997;2717-2729.
7. Tsukita S., Oishi K., Sato N., Sagara J., Kawai A., Tsukita S. ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons. J. Cell Biol. 112:1994;391-401.
8. Skoudy A., Tran Van Nhieu G., Mantis N., Arpin M., Mounier J., Gounon P., Sansonetti P.J. A functional role for ezrin during Shigella entry into epithelial cells. J. Cell Sci. 279:1999;2059-2068.
9. Hall A. Rho GTPase and the actin cytoskeleton. Science. 81:1998;509-514.
10. Nobes C.D., Hall A. Rho, Rac, Cdc42 GTPases regulate the assembly of multimolecular focal adhesion complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell. 112:1995;53-62.
11. Mounier J., Laurent V., Hall A., Fort P., Carlier M.F., Sansonetti P.J., Egile C. Rho family GTPases control entry of Shigella flexneri into epithelial cells but not intracellular motility. J. Cell. Sci. 113:1999;2069-2080.
12. Duménil G., Sansonetti P.J., Tran Van Nhieu G. Src tyrosine kinase activity downregulates Rho-dependent responses during Shigella entry into epithelial cells and stress fibres formation. J. Cell Science. 135:2000;71-80.
13. Fincham V.J., Unlu M., Brunton V.G., Pitts J.D., Wyke J.A., Frame M.C. Translocation of Src kinase to the cell periphery is mediated by the actin cytoskeleton under the control of the Rho family of small G proteins. J. Cell Biol. 14:1996;1551-1564.
14. Dehio C., Prévost M.C., Sansonetti P.J. Invasion of epithelial cells by Shigella flexneri induces tyrosine phosphorylation of cortactin by a pp60c-src mediated signalling pathway. EMBO J. 143:1995;2471-2482.
15. Duménil G., Olivo J.C., Pellegrini S., Fellous M., Sansonetti P.J., Tran Van Nhieu G. Interferon-alpha inhibits a Src-mediated pathway necessary for Shigella-induced cytoskeletal rearrangements during entry into epithelial cells. J. Cell Biol. 112:1998;1003-1012.
16. Fincham V.J., Chudleigh A., Frame M.C. Regulation of p190RhoGAP by v-Src is linked to cytoskeletal disruption during transformation. J. Cell Sci. 7:1999;947-956.
17. Burridge K., Chrzanowska-Wodnicka M., Zhong C. Focal adhesion assembly. Trends Cell Biol. 359:1997;342-347.
18. Settleman J., Albright C.F., Foster L.C., Weinberg R.A. Association between GTPase activators for Rho and Ras families. Nature. 147:1992;153-154.
19. Blocker A., Gounon P., Larquet E., Niebuhr K., Cabiaux V., Parsot C., Sansonetti P.J. The tripartite type III secreton of Shigella flexneri inserts IpaB and IpaC into host membranes. J. Cell Biol. 400:1999;1-11.
20. De Geyter C., Vogt B., Benjelloum-Touimi Z., Sansonetti P.J., Ruysschaert J.M., Parsot C., Cabiaux V. Purification of IpaC, a protein involved in entry of Shigella flexneri into epithelial cells and characterization of its interaction with lipid membranes. FEBS Letters. 23:1997;149-154.
21. Cornelis G., Wolf-Watz H. The Yersinia Yop virulon: a bacterial system for subverting eukaryotic cells. Mol. Microbiology. 62:1997;861-867.
22. Hueck C.J. Type III secretion systems in bacterial pathogens of animals and plants. Microbiol. Mol. Biol. Rev. 18:1998;379-433.
23. Tran Van Nhieu G., Caron E., Hall A., Sansonetti P.J. IpaC induces actin polymerization and filopodia formation during Shigella entry into epithelial cells. EMBO J. 93:1999;3249-3262.
24. Hardt W.D. S. typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells. Cell. 18:1998;815-826.
25. Hayward R.D., Koronakis V. Direct nucleation and bundling of actin by the SipC protein of invasive Salmonella. EMBO J. 18:1999;4926-4935.
26. Bourdet-Sicard R., Ruediger M., Jockusch B., Gounon P., Sansonetti P.J., Tran Van Nhieu G. Binding of the Shigella IpaA protein to vinculin induces actin depolymerization. EMBO J. 373:1999;5853-5862.
27. Johnson R.P., Craig S.W. F-actin binding site masked by the intramolecular association of vinculin head and tail domains. Nature. 381:1995;261-264.
28. Gilmore A.P., Burridge K. Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-biphosphate. Nature. 14:1996;531-535.
29. Dramsi S., Cossart P. Intracellular pathogens and the actin cytoskeleton. Annu. Rev. Cell Dev. Biol. 86:1998;137-166.
30. Bernardini M.L., Mounier J., D'Hauteville H., Coquis-Rondon M., Sansonetti P.J. Identification of icsA, a plasmid locus of Shigella flexneri that governs bacterial intra and intercellular spread through interaction with F-actin. Proc. Natl. Acad. Sci. USA. 171:1989;3867-3871.
31. Lett M.C., Sasakawa C., Okada N., Sakai T., Makino S., Yamada M., Komatsu K., Yoshikawa M. virG, a plasmid-coded virulence gene of Shigella flexneri: identification of the VirG protein and determination of the complete coding sequence. J. Bacteriol. 175:1989;353-359.
32. Goldberg M.B., Barzu O., Parsot C., Sansonetti P.J. Unipolar localization and ATPase activity of IcsA, a Shigella flexneri protein involved in intracellular movement. J. Bacteriol. 23:1993;2189-2196.
33. Egile C., D'Hauteville H., Parsot C., Sansonetti P.J. SopA, the outer membrane protease responsible for polar localization of IcsA in Shigella flexneri. Mol. Microbiol. 271:1997;1063-1073.
34. Suzuki T., Shinsuke S., Sasakawa C. Functional analysis of Shigella VirG domains essential for interaction with vinculin and actin-based motility. J. Biol. Chem. 17:1996;21878-21885.
35. Suzuki T., Miki H., Takenawa T., Sasakawa C. Neural Wiskott-Aldrich Syndrome Protein is implicated in the actin-based motility of Shigella flexneri. EMBO J. 112:1998;2767-2776.
36. Gouin E., Gantelet H., Egile C., Lasa I., Ohayon H., Villiers V., Gounon P., Sansonetti P.J., Cossart P. A comparative study of the actin-based motilities of the pathogenic bacteria Listeria monocytogenes, Shigella flexneri, and Rickettsia conorii. J. Cell Sci. 37:1999;1697-1708.
37. Goldberg M.B. Shigella actin-based motility in the absence of vinculin. Cell Motil. Cytoskeleton. 401:1997;44-53.
38. Loisel T.P., Boujemaa R., Pantaloni D., Carlier M.F. Reconstitution of actin-based motility of Listeria and Shigella using pure proteins. Nature. 146:1999;613-616.
39. Egile C., Loisel T.P., Laurent V., Li R., Pantaloni D., Sansonetti P.J., Carlier M.F. Activation of the Cdc42 effector N-WASP by the Shigella flexneri IcsA protein promotes actinnucleation by Arp2/3 complex and bacterial actin-based motility. J. Cell Biol. 15:1999;1319-1332.
40. Miki H., Miura K., Takenawa T. N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases. EMBO J. 146:1996;5326-5335.
41. Machesky L.M., Insall R.H. Signaling to actin dynamics. J. Cell Biol. 8:1999;267-272.
42. Machesky L.M., Insall R.H. Scar1 and the Wiskott-Aldrich syndrome protein WASP regulate the actin cytoskeleton through the Arp2/3 complex. Curr. Biol. 97:1998;1347-1356.
43. Rohatgi R.L., Ma L., Miki H., Lopez M., Kirchhausen T., Takenawa T., Kirschner M.W. The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell. 38:1999;221-231.
44. Higgs H.N., Blanchoin L., Pollard T.D. Influence of the C terminus of Wiskott-Aldrich Syndrome protein (WASp) and the Arp2/3 complex on actin polymerization. Biochemistry. 144:1999;15212-15222.
45. Laurent V., Loisel P.T., Harbeck B., Wehmann A., Gröbe L., Jockush B.M., Wehland J., Gertler F.G., Carlier M.-F. Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes. J. Cell Biol. 1999;1125-1245.