Interaction of Ipa proteins of Shigella flexneri with α5β1 integrin promotes entry of the bacteria into mammalian cells

Journal of Experimental Medicine

Volumn 183, Issue 3, 1996, Pages 991-999

  Watarai, Masahisa ^a   Funato, Sumiko ^b   Sasakawa, Chihiro ^a  

^a UNIVERSITY OF TOKYO   (Japan)

^b Nippon Bio Rad Laboratories   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; INTEGRIN; IPA PROTEIN; UNCLASSIFIED DRUG;

ACTIN POLYMERIZATION; ANIMAL CELL; ARTICLE; BACTERIAL COLONIZATION; CELL INVASION; CHO CELL; ENDOCYTOSIS; INTESTINE EPITHELIUM CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; SHIGELLA FLEXNERI;

ADHESINS, BACTERIAL; ANIMALS; BACTERIAL PROTEINS; CELL ADHESION MOLECULES; CHO CELLS; CRICETINAE; FOCAL ADHESION KINASE 1; FOCAL ADHESION PROTEIN-TYROSINE KINASES; HUMANS; MICROSCOPY, CONFOCAL; PHOSPHOTYROSINE; PROTEIN-TYROSINE KINASES; RECEPTORS, FIBRONECTIN; RECOMBINANT PROTEINS; SHIGELLA FLEXNERI; TRANSFECTION;

EID: 0029915666     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.183.3.991     Document Type: Article

References (35)

1. Andrews, G.P., and A.T. Maurelli. 1992. mxiA of Shigella flexneri 2a, which facilitates export of invasion plasmid antigens, encodes a homolog of the low-calcium response protein, LcrD, of Yersinia pestis. Infect. Immunol. 60:3287-3295
2. Venkatesan, M.M., J.M. Buysse, and E.V. Oaks. 1992. Surface presentation of Shigella flexneri invasion plasmid antigens requires the products of the spa locus. J. Bacteriol. 174:1990-2001.
3. Ménard, R., P.J. Sansonetti, and C. Parsot. 1993. Nonpolar mutagenesis of the ipa genes defines IpaB, IpaC, and IpaD as effectors of Shigella flexneri entry into epithelial cells. J. Bacteriol. 175:5899-5906.
4. Sasakawa, C., B. Adler, T. Tobe, N. Okada, S. Nagai, K. Komatsu, and M. Yoshikawa. 1989. Functional organization and nucleotide sequence of virulence Region-2 on the large virulence plasmid in Shigella flexneri 2a. Mol. Microbiol. 3: 1191-1201.
5. High, N., J. Mounier, M.-C. Prévost, and P.J. Sansonetti. 1992. IpaB of Shigella flexneri causes entry into epithelial cells and escape from the phagocytic vacuole. EMBO (Eur. Mol. Biol. Organ.) J. 11:1991-1999.
6. Clerc, P., and P.J. Sansonetti. 1987. Entry of Shigella flexneri into HeLa cells: evidence for directed phagocytosis involving actin polymerization and myosin accumulation. Infect. Immunol. 55:2681-2688.
7. Venkatesan, M.M., J.M. Buysse, and D.J. Kopecko. 1988. Characterization of invasion plasmid antigen genes (ipaBCD) from Shigella flexneri. Proc. Natl. Acad. Sci. USA. 85:9317-9321.
8. Andrews, G.P., A.E. Hromockyj, C. Coker, and A.T Maurelli. 1991. Two novel virulence loci, mxiA and mxiB, in Shigella flexneri 2a facilitate excretion of invasion plasmid antigens. Infect. Immunol. 59:1997-2005.
9. Allaoui, A., P.J. Sansonetti, and C. Parsot. 1992. MxiJ, a lipoprotein involved in secretion of Shigella Ipa invasins, is homologous to YscJ, a secretion factor of the Yersinia Yop proteins. J. Bacteriol. 174:7661-7669.
10. Ménard, R., P.J. Sansonetti, and C. Parsot. 1994. The secretion of the Shigella flexneri Ipa invasins is activated by epithelial cells and controlled by IpaB and IpaC. EMBO (Eur. Mol. Biol. Organ.) J. 13:5293-5302.
11. Watarai, M., T. Tobe, M. Yoshikawa, and C. Sasakawa. 1995. Contact of Shigella with host cells triggers release of Ipa invasins and is an essential function of invasiveness. EMBO (Eur. Mol. Biol. Organ.) J. 14:2461-2470.
12. Watarai, M., T. Tobe, M. Yoshikawa, and C Sasakawa. 1995. Disulfide oxidoreductase activity of Shigella flexneri is required for release of Ipa proteins and invasion of epithelial cells. Proc. Natl. Acad. Sci. USA. 92:4927-4931.
13. Parsot, C., R. Ménard, P. Gounon, and P.J. Sansonetti. 1995. Enhanced secretion through the Shigella flexneri Mxi-Spa translocon leads to assembly of extracellular proteins into macromolecular structures. Mol. Microbiol 16:291-300.
14. Mounier, J., T. Vasselon, R. Hellio, M. Lesourd, and P.J. Sansonetti. 1992. Shigella flexneri enters human colonic Caco-2 epithelial cells through the basolateral pole. Infect. Immunol. 60:237-248.
15. Vasselon, T., J. Mounier, M.-C. Prévost, R. Hellio, and P.J. Sansonetti. 1991. Stress fiber-based movement of Shigella flexneri within cells. Infect. Immunol. 59:1723-1732.
16. Clark, E A , and J.S. Brugge. 1995. Integrin and signal transduction pathways: the road taken. Science (Wash. DC). 268: 233-239.
17. FAK, a structurally distinctive protein-tyrosine kinase associated with focal adhesions. Proc. Natl. Acad. Sci. USA. 89:5192-5196.
18. FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly. J. Cell Biol. 119:893-903.
19. Morla, A., Z. Zhang, and E. Ruoslahti. 1994 Superfibronectin is a functionally distinct form of fibronectin. Nature (Lond.). 367:193-196
20. Nakata, N., C. Sasakawa, N. Okada, T. Tobe, I. Fukuda, T. Suzuki, K. Komatsu, and M. Yoshikawa. 1992. Identification and characterization of virK, a virulence-associated large plasmid gene essential for intercellular spreading of Shigella flexneri. Mol Microbiol. 2:2387-2395.
21. 1 fibronectin receptor suppress the transformed phenotype of Chinese hamster ovary cells. Cell. 60:849-859.
22. Schreiner, C.L., J.S. Bauer, Y.N. Danilov, S. Hussein, M.M. Sczekan, and R.L. Juliano. 1989. Isolation and characterization of Chinese hamster ovary cell variants deficient in the expression of fibronectin receptor. J. Cell Biol. 109:3157-3167
23. 1 chain integrins are receptor for invasin, a protein that promotes bacterial penetration into mammalian cells. Cell. 60:861-871.
24. Sasakawa, C., K. Komatsu, T. Tobe, T. Suzuki, and M. Yoshikawa. 1993. Eitht genes in region 5 that form an operon are essential for invasion of epithelial cells by Shigella flexneri 2a. J. Bacteriol. 175:2334-2346.
25. Pierschbacher, M.D., and E. Ruoslahti. 1984. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature (Lond.). 309:30-33.
26. Ruoslahti, E., and M.D. Pierschbacher. 1987. New perspectives in cell adhesion: RGD and integrins. Science (Wash. DC). 238:491-497.
27. Hynes, R.O. 1992. Integrins: versatility, modulation, and signaling in cell adhesion. Cell. 69:11-25.
28. Ménard, R., P. Sansonetti, C. Parsot, and T. Vasselon. 1994. Extracellular association and cytoplasmic partitioning of the IpaB and IpaC invasins of S. flexneri. Cell. 79:515-525.
29. Miyamoto, S., S.K Akiyama, and K.M. Yamada. 1995. Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science (Wash. DC). 267:883-885.
30. 1 integrin receptor. J. Biol. Chem. 266:24367-24375.
31. Rosenshine, I., V. Duronio, and B.B. Finlay. 1992. Tyrosine protein kinase inhibitors block invasin-promoted bacterial uptake by epithelial cells. Infect. Immunol. 60:2211-2217.
32. Ginocchio, C., J. Pace, and J.E. Galan. 1992. Identification and molecular characterization of a Salmonella typhimurium gene involved in triggering the internalization of Salmonellae into cultured epithelial cells. Proc. Natl. Acad. Sci. USA. 89:5976-5980.
33. Francis, C.L., T.A. Ryan, B.D. Jones, S.J. Smith, and S. Falkow. 1993. Ruffles induced by Salmonella and other stimuli direct macropinocytosis of bacteria. Nature (Lond.). 364: 639-642.
34. Rosenshine, I., M.S. Donnenberg, J.B. Kaper, and B.B. Finlay. 1992. Signal transduction between enteropathogenic Escherichia coli (EPEC) and epithelial cells: EPEC induces tyrosine phosphorylation of host cell proteins to initiate cytoskeletal rearrangement and bacterial uptake. EMBO (Eur. Mol. Biol. Organ.) J. 11:3551-3560.
35. c-src-mediated signaling pathway. EMBO (Eur. Mol. Biol. Organ.) J. 14:2471-2482.