1887

Chapter 17 : Enteric Microbial Toxins and the Intestinal Epithelial Cytoskeleton

Authors: James P. Nataro1, Cynthia Sears2, Alessio Fasano3, Robert J. Bloch4
VIEW AFFILIATIONS HIDE AFFILIATIONS
Affiliations: 1: Center for Vaccine Development, Departments of Pediatrics and Medicine, University of Maryland School of Medicine, Baltimore, MD 21201; 2: Department of Medicine, The Johns Hopkins School of Medicine, Baltimore, MD 21205; 3: Center for Vaccine Development, Departments of Pediatrics and Medicine and Department of Physiology, University of Maryland School of Medicine, Baltimore, MD 21201; 4: Department of Physiology, University of Maryland School of Medicine, Baltimore, MD 21201
Content Type: Monograph
Publication Year: 2003

Category: Clinical Microbiology

MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price.

Preview this chapter:
Preview Magnify
Zoom in
Zoomout

Enteric Microbial Toxins and the Intestinal Epithelial Cytoskeleton, Page 1 of 2

| /docserver/preview/fulltext/10.1128/9781555817848/9781555812614_Chap17-1.gif /docserver/preview/fulltext/10.1128/9781555817848/9781555812614_Chap17-2.gif

Abstract:

The cytoskeleton provides structure and organization to the epithelial cell. In addition to providing support and rigidity on demand, the cytoskeleton mediates adhesion of cells to surfaces and to each other, anchoring of proteins into the plasma membrane, and, to a large extent, control of cellular processes. The cytoskeleton of epithelial cells, as in most mammalian cells, is composed of three major structures: microtubules, intermediate filaments, and microfilaments. Epithelial cells adhere to one another at their lateral surfaces through desmosomes, adherens junctions, and tight junctions (TJs) and to a surrounding basal lamina through hemidesmosomes and focal contacts. Given the many important roles of the epithelial cytoskeleton, it should come as no surprise that bacterial toxins have evolved to subvert these functions. toxin (BFT) was the first bacterial toxin identified to remodel the intestinal epithelial cytoskeleton and F-actin architecture via cleavage of a cell surface molecule. Enteric toxins now provide a remarkable set of tools with which to dissect the complex interactions of the epithelial cytoskeleton. The field lies at the nexus of bacteriology, protein chemistry, and cell biology and provides a prominent example of synergistic research among scientific disciplines.

Citation: Nataro J, Sears C, Fasano A, Bloch R. 2003. Enteric Microbial Toxins and the Intestinal Epithelial Cytoskeleton, p 301-332. In Hecht G (ed), Microbial Pathogenesis and the Intestinal Epithelial Cell. ASM Press, Washington, DC. doi: 10.1128/9781555817848.ch17
Highlighted Text: Show | Hide
Loading full text...

Full text loading...

Figures

Enteric Microbial Toxins and the Intestinal Epithelial Cytoskeleton
[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/10.1128/9781555817848.chap17-1,webId=/content/author/10.1128/9781555817848.chap17-1,properties={foaf_givenname=James P., foaf_name=James P. Nataro, foaf_surname=Nataro, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/10.1128/9781555817848.chap17-aff1]]}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/10.1128/9781555817848.chap17-2,webId=/content/author/10.1128/9781555817848.chap17-2,properties={foaf_givenname=Cynthia, foaf_name=Cynthia Sears, foaf_surname=Sears, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/10.1128/9781555817848.chap17-aff2]]}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/10.1128/9781555817848.chap17-3,webId=/content/author/10.1128/9781555817848.chap17-3,properties={foaf_givenname=Alessio, foaf_name=Alessio Fasano, foaf_surname=Fasano, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/10.1128/9781555817848.chap17-aff3]]}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/10.1128/9781555817848.chap17-4,webId=/content/author/10.1128/9781555817848.chap17-4,properties={foaf_givenname=Robert J., foaf_name=Robert J. Bloch, foaf_surname=Bloch, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/10.1128/9781555817848.chap17-aff4]]}]]
Citation: Nataro J, Sears C, Fasano A, Bloch R. 2003. Enteric Microbial Toxins and the Intestinal Epithelial Cytoskeleton, p 301-332. In Hecht G (ed), Microbial Pathogenesis and the Intestinal Epithelial Cell. ASM Press, Washington, DC. doi: 10.1128/9781555817848.ch17
/content/10.1128/9781555817848.chap17.fig17-1
FIGURE 1

The enterocyte cytoskeleton. The enterocyte is supported by three major structural polymers. (i) Actin microfilaments are prominent in the microvilli, the terminal web, and the membrane cytoskeleton. Actin filaments connect to several proteins and protein complexes on the inner face of the cytoplasmic membrane, including adherens junctions, focal adhesions, and transporters in the basolateral membrane. (ii) Intermediate filaments connect to desmosomes on the basolateral membrane, giving rigidity and resistance to shear forces. (iii) Microtubules provide support and serve as tracks for molecular motors. Proteins illustrated at the adherens junction are the -and -catenins and the transmembrane protein E-cadherin (“E”). TJs comprise integral membrane proteins (“1” in Fig.), including occludins and claudins, and signaling proteins (“2” in Fig.).

10.1128/9781555817848/fig17-1_thmb.gif
10.1128/9781555817848/fig17-1.gif
Image of FIGURE 1
FIGURE 1

The enterocyte cytoskeleton. The enterocyte is supported by three major structural polymers. (i) Actin microfilaments are prominent in the microvilli, the terminal web, and the membrane cytoskeleton. Actin filaments connect to several proteins and protein complexes on the inner face of the cytoplasmic membrane, including adherens junctions, focal adhesions, and transporters in the basolateral membrane. (ii) Intermediate filaments connect to desmosomes on the basolateral membrane, giving rigidity and resistance to shear forces. (iii) Microtubules provide support and serve as tracks for molecular motors. Proteins illustrated at the adherens junction are the -and -catenins and the transmembrane protein E-cadherin (“E”). TJs comprise integral membrane proteins (“1” in Fig.), including occludins and claudins, and signaling proteins (“2” in Fig.).

Citation: Nataro J, Sears C, Fasano A, Bloch R. 2003. Enteric Microbial Toxins and the Intestinal Epithelial Cytoskeleton, p 301-332. In Hecht G (ed), Microbial Pathogenesis and the Intestinal Epithelial Cell. ASM Press, Washington, DC. doi: 10.1128/9781555817848.ch17
Permissions and Reprints Request Permissions
Download as Powerpoint
/content/10.1128/9781555817848.chap17.fig17-2
FIGURE 2

The epithelial junctional complex. TJs (zonula occludens or ZO) comprise transmembrane proteins (occludin, claudins, and JAM), which form a tight barrier in the paracellular space. Occludin and the claudins interact with the cytoskeleton via ZO-1, ZO-2, and ZO-3, and a series of downstream adapter and signaling proteins, ultimately interfacing with actin and actin-binding proteins. Basal to the ZO is the zonula adherens (ZA). This complex is attached to the apical actin belt via catenins and also to the junctional actin strands of the ZO. Catenins are involved in cellular signaling reactions–(see text).

10.1128/9781555817848/fig17-2_thmb.gif
10.1128/9781555817848/fig17-2.gif
Image of FIGURE 2
FIGURE 2

The epithelial junctional complex. TJs (zonula occludens or ZO) comprise transmembrane proteins (occludin, claudins, and JAM), which form a tight barrier in the paracellular space. Occludin and the claudins interact with the cytoskeleton via ZO-1, ZO-2, and ZO-3, and a series of downstream adapter and signaling proteins, ultimately interfacing with actin and actin-binding proteins. Basal to the ZO is the zonula adherens (ZA). This complex is attached to the apical actin belt via catenins and also to the junctional actin strands of the ZO. Catenins are involved in cellular signaling reactions–(see text).

Citation: Nataro J, Sears C, Fasano A, Bloch R. 2003. Enteric Microbial Toxins and the Intestinal Epithelial Cytoskeleton, p 301-332. In Hecht G (ed), Microbial Pathogenesis and the Intestinal Epithelial Cell. ASM Press, Washington, DC. doi: 10.1128/9781555817848.ch17
Permissions and Reprints Request Permissions
Download as Powerpoint
/content/10.1128/9781555817848.chap17.fig17-3
FIGURE 3

The activation cycle of Rho family GTPases. Rho family GTPases are active when bound to GTP and inactive when bound to GDP. They possess intrinsic GTPase activity, which is accelerated by GAP proteins or inhibited by GEF proteins. GDI proteins stabilize the GDP-bound state. Activated GTPases are commonly bound to the plasma membrane, but become detached on inactivation. The effect shown here for Rho is activation of an effector, illustrated with an asterisk. Many effectors exist, including kinases, phosphatases, phospholipases, and adaptor proteins. See text for details.

10.1128/9781555817848/fig17-3_thmb.gif
10.1128/9781555817848/fig17-3.gif
Image of FIGURE 3
FIGURE 3

The activation cycle of Rho family GTPases. Rho family GTPases are active when bound to GTP and inactive when bound to GDP. They possess intrinsic GTPase activity, which is accelerated by GAP proteins or inhibited by GEF proteins. GDI proteins stabilize the GDP-bound state. Activated GTPases are commonly bound to the plasma membrane, but become detached on inactivation. The effect shown here for Rho is activation of an effector, illustrated with an asterisk. Many effectors exist, including kinases, phosphatases, phospholipases, and adaptor proteins. See text for details.

Citation: Nataro J, Sears C, Fasano A, Bloch R. 2003. Enteric Microbial Toxins and the Intestinal Epithelial Cytoskeleton, p 301-332. In Hecht G (ed), Microbial Pathogenesis and the Intestinal Epithelial Cell. ASM Press, Washington, DC. doi: 10.1128/9781555817848.ch17
Permissions and Reprints Request Permissions
Download as Powerpoint

References

/content/book/10.1128/9781555817848.chap17
1. Adam, T.,, M. Arpin,, M. C. Prevost,, P. Gounon,, and P. J. Sansonetti. 1995. Cytoskeletal rearrangements and the functional role of T-plastin during entry of Shigella flexneri into HeLa cells. J. Cell. Biol. 129: 367– 381.
2. Adam, T.,, M. Giry,, P. Boquet,, and P. Sansonetti. 1996. Rho-dependent membrane folding causes Shigella entry into epithelial cells. EMBO J. 15: 3315– 3321.
3. Aepfelbacher, M.,, and J. Heesemann. 2001. Modulation of Rho GTPases and the actin cytoskeleton by Yersinia outer proteins (Yops). Int. J. Med. Microbiol. 291: 269– 276.
4. Aizawa, S. I. 2001. Bacterial flagella and type III secretion systems. FEMS Microbiol. Lett. 202: 157– 164.
5. Aktories, K.,, G. Schmidt,, and I. Just. 2000. Rho GTPases as targets of bacterial protein toxins. Biol. Chem. 381: 421– 426.
6. Alcantara, C.,, W. F. Stenson,, T. S. Steiner,, and R. L. Guerrant. 2001. Role of inducible cyclooxygenase and prostaglandins in Clostridium difficile toxin A-induced secretion and inflammation in an animal model. J. Infect. Dis. 184: 648– 652.
7. Anastasiadis, P. Z.,, S. Y. Moon,, M. A. Thoreson,, D. J. Mariner,, H. C. Crawford,, Y. Zheng,, and A. B. Reynolds. 2000. Inhibition of RhoA by p120 catenin. Nat. Cell. Biol. 2: 637– 644.
8. Anastasiadis, P. Z.,, and A. B. Reynolds. 2000. The p120 catenin family: complex roles in adhesion, signaling and cancer. J. Cell. Sci. 113(Part 8): 1319– 1334.
9. Anastasiadis, P. Z.,, and A. B. Reynolds. 2001. Regulation of Rho GTPases by p120-catenin. Curr. Opin. Cell Biol. 13: 604– 610.
10. Anderson, D. M.,, and O. Schneewind. 1999. Yersinia enterocolitica type III secretion: an mRNA signal that couples translation and secretion of YopQ. Mol. Microbiol. 31: 1139– 1148.
11. Andreu, A.,, A. E. Stapleton,, C. Fennell,, H. A. Lockman,, M. Xercavins,, F. Fernandez,, and W. E. Stamm. 1997. Urovirulence determinants in Escherichia coli strains causing prostatitis. J. Infect. Dis. 176: 464– 469.
12. Balda, M. S.,, and K. Matter. 1998. Tight junctions. J. Cell. Sci. 111: 541– 547.
13. Barker, N.,, and H. Clevers. 2000. Catenins, Wnt signaling and cancer. Bioessays 22: 961– 965.
14. Barker, N.,, P. J. Morin,, and H. Clevers. 2000. The Yin-Yang of TCF/beta-catenin signaling. Adv. Cancer Res. 77: 1– 24.
15. Bartles, J. R.,, L. Zheng,, A. Li,, A. Wierda,, and B. Chen. 1998. Small espin: a third actinbundling protein and potential forked protein ortholog in brush border microvilli. J. Cell Biol. 143: 107– 119.
16. Baudry, B.,, A. Fasano,, J. Ketley,, and J. B. Kaper. 1992. Cloning of a gene (zot) encoding a new toxin produced by Vibrio cholerae. Infect. Immun. 60: 428– 434.
17. Bennett, V.,, and L. Chen. 2001. Ankyrins and cellular targeting of diverse membrane proteins to physiological sites. Curr. Opin. Cell Biol. 13: 61– 67.
18. Ben-Ze’ev, A.,, M. Shtutman,, and J. Zhurinsky. 2000. The integration of cell adhesion with gene expression: the role of beta-catenin. Exp. Cell Res. 261: 75– 82.
19. Bleves, S.,, and G. R. Cornelis. 2000. How to survive in the host: the Yersinia lesson. Microbes Infect. 2: 1451– 1460.
20. Bliska, J. B. 2000. Yop effectors of Yersinia spp. and actin rearrangements. Trends Microbiol. 8: 205– 208.
21. Blocker, A.,, N. Jouihri,, E. Larquet,, P. Gounon,, F. Ebel,, C. Parsot,, P. Sansonetti,, and A. Allaoui. 2001. Structure and composition of the Shigella flexneri "needle complex, " a part of its type III secreton. Mol. Microbiol. 39: 652– 663.
22. Boquet, P. 2001. The cytotoxic necrotizing factor 1 (CNF1) from Escherichia coli. Toxicon 39: 1673– 1680.
23. Bourdet-Sicard, R.,, M. Rudiger,, B. M. Jockusch,, P. Gounon,, P. J. Sansonetti,, and G. T. Nhieu. 1999. Binding of the Shigella protein IpaA to vinculin induces F-actin depolymerization. EMBO J. 18: 5853– 5862.
24. Buchrieser, C.,, P. Glaser,, C. Rusniok,, H. Nedjari,, H. D’Hauteville,, F. Kunst,, P. Sansonetti,, and C. Parsot. 2000. The virulence plasmid pWR100 and the repertoire of proteins secreted by the type III secretion apparatus of Shigella flexneri. Mol. Microbiol. 38: 760– 771.
25. Burridge, K. 1999. Crosstalk between Rac and Rho. Science 283: 2028– 2029.
26. Busch, C.,, and K. Aktories. 2000. Microbial toxins and the glycosylation of rho family GTPases. Curr. Opin. Struct. Biol. 10: 528– 535.
27. Cambronne, E. D.,, L. W. Cheng,, and O. Schneewind. 2000. LcrQ/YscM1, regulators of the Yersinia yop virulon, are injected into host cells by a chaperone-dependent mechanism. Mol. Microbiol. 37: 263– 273.
28. Cantarelli, V. V.,, A. Takahashi,, I. Yanagihara,, Y. Akeda,, K. Imura,, T. Kodama,, G. Kono,, Y. Sato,, and T. Honda. 2001. Talin, a host cell protein, interacts directly with the translocated intimin receptor, Tir, of enteropathogenic Escherichia coli, and is essential for pedestal formation. Cell Microbiol. 3: 745– 751.
29. Chambers, F. G.,, S. S. Koshy,, R. F. Saidi,, D. P. Clark,, R. D. Moore,, and C. L. Sears. 1997. Bacteroides fragilis toxin exhibits polar activity on monolayers of human intestinal epithelial cells (T84 cells) in vitro. Infect. Immun. 65: 3561– 3570.
30. Chappuis-Flament, S.,, E. Wong,, L. D. Hicks,, C. M. Kay,, and B. M. Gumbiner. 2001. Multiple cadherin extracellular repeats mediate homophilic binding and adhesion. J. Cell Biol. 154: 231– 243.
30a. Chen, L. M.,, S. Hobbie,, and J. E. Galan. 1996. Requirement of CDC42 for Salmonella-induced cytoskeletal and nuclear responses. Science 274: 2115– 2118.
31. Cherfils, J.,, and P. Chardin. 1999. GEFs: structural basis for their activation of small GTP-binding proteins. Trends Biochem. Sci. 24: 306– 311.
32. Clements, W. M.,, J. Wang,, A. Sarnaik,, O. J. Kim,, J. MacDonald,, C. Fenoglio-Preiser,, J. Groden,, and A. M. Lowy. 2002. beta-Catenin mutation is a frequent cause of Wnt pathway activation in gastric cancer. Cancer Res. 62: 3503– 3506.
33. Condeelis, J. 2001. How is actin polymerization nucleated in vivo? Trends Cell Biol. 11: 288– 293.
34. Craig, S. W.,, and R. P. Johnson. 1996. Assembly of focal adhesions: progress, paradigms, and portents. Curr. Opin. Cell Biol. 8: 74– 85.
35. Crane, J.,, B. McNamara,, and M. Donnenberg. 2001. Role of EspF in host cell death induced by enteropathogenic Escherichia coli. Cell. Microbiol. 3: 197– 211.
36. Daniell, S. J.,, N. Takahashi,, R. Wilson,, D. Friedberg,, I. Rosenshine,, F. P. Booy,, R. K. Shaw,, S. Knutton,, G. Frankel,, and S. Aizawa. 2001. The filamentous type III secretion translocon of enteropathogenic Escherichia coli. Cell Microbiol. 3: 865– 871.
37. de Grado, M.,, A. Abe,, A. Gauthier,, O. Steele-Mortimer,, R. DeVinney,, and B. B. Finlay. 1999. Identification of the intimin-binding domain of Tir of enteropathogenic Escherichia coli. Cell. Microbiol. 1: 7– 17.
38. De Matteis, M. A.,, and J. S. Morrow. 1998. The role of ankyrin and spectrin in membrane transport and domain formation. Curr. Opin. Cell Biol. 10: 542– 549.
39. De Matteis, M. A.,, and J. S. Morrow. 2000. Spectrin tethers and mesh in the biosynthetic pathway. J. Cell Sci. 113: 2331– 2343.
40. DeVinney, R.,, J. L. Puente,, A. Gauthier,, D. Goosney,, and B. B. Finlay. 2001. Enterohaemorrhagic and enteropathogenic Escherichia coli use a different Tir-based mechanism for pedestal formation. Mol. Microbiol. 41: 1445– 1458.
41. Di Pierro, M.,, R. Lu,, S. Uzzau,, W. Wang,, K. Margaretten,, C. Pazzani,, F. Maimone,, and A. Fasano. 2001. Zonula occludens toxin structure-function analysis. Identification of the fragment biologically active on tight junctions and of the zonulin receptor binding domain. J. Biol. Chem. 276: 19160– 19165.
42. Eslava, C.,, F. Navarro-Garcia,, J. R. Czeczulin,, I. R. Henderson,, A. Cravioto,, and J. P. Nataro. 1998. Pet, an autotransporter enterotoxin from enteroaggregative Escherichia coli. Infect. Immun. 66: 3155– 3163.
43. Fagotto, F.,, and B. M. Gumbiner. 1996. Cell contact-dependent signaling. Dev. Biol. 180: 445– 454.
44. Fasano, A. 1999. Cellular microbiology: can we learn cell physiology from microorganisms? Am. J. Physiol. 276: C765– C776.
45. Fasano, A.,, C. Fiorentini,, G. Donelli,, S. Uzzau,, J. B. Kaper,, K. Margaretten,, X. Ding,, S. Guandalini,, L. Comstock,, and S. E. Goldblum. 1995. Zonula occludens toxin modulates tight junctions through protein kinase Cdependent actin reorganization, in vitro. J. Clin. Invest. 96: 710– 720.
46. Fasano, A.,, S. Uzzau,, C. Fiore,, and K. Margaretten. 1997. The enterotoxic effect of zonula occludens toxin on rabbit small intestine involves the paracellular pathway. Gastroenterology 112: 839– 846.
47. Fath, K. R.,, and D. R. Burgess. 1995. Microvillus assembly. Not actin alone. Curr. Biol. 5: 591– 593.
48. Fath, K. R.,, S. N. Mamajiwalla,, and D. R. Burgess. 1993. The cytoskeleton in development of epithelial cell polarity. J. Cell Sci. Suppl. 17: 65– 73.
49. Feng, Y.,, S. R. Wente,, and P. W. Majerus. 2001. Overexpression of the inositol phosphatase SopB in human 293 cells stimulates cellular chloride influx and inhibits nuclear mRNA export. Proc. Natl. Acad. Sci. USA 98: 875– 879.
50. Filali, M.,, N. Cheng,, D. Abbott,, V. Leontiev,, and J. F. Engelhardt. 2002. Wnt-3A/beta-catenin signaling induces transcription from the LEF-1 promoter. J. Biol. Chem. 277: 33398– 33410.
51. Fincham, V. J.,, A. Chudleigh,, and M. C. Frame. 1999. Regulation of p190 Rho-GAP by v-Src is linked to cytoskeletal disruption during transformation. J. Cell Sci. 112(Pt. 6): 947– 956.
52. Frankel, G.,, O. Lider,, R. Hershkoviz,, A. Mould,, S. Kachalsky,, D. Candy,, L. Cahalon,, M. Humphries,, and G. Dougan. 1996. The cell-binding domain of intimin from enteropathogenic Escherichia coli binds to beta1 integrins. J. Biol. Chem. 23: 20359– 20364.
53. Freeman, N. L.,, D. V. Zurawski,, P. Chowrashi,, J. C. Ayoob,, L. Huang,, B. Mittal,, J. M. Sanger,, and J. W. Sanger. 2000. Interaction of the enteropathogenic Escherichia coli protein, translocated intimin receptor (Tir), with focal adhesion proteins. Cell Motil. Cytoskel. 47: 307– 318.
54. Fu, Y.,, and J. E. Galan. 1999. A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion. Nature 401: 293– 297.
55. Fu, Y.,, and J. E. Galan. 1998. The Salmonella typhimurium tyrosine phosphatase SptP is translocated into host cells and disrupts the actin cytoskeleton. Mol. Microbiol. 27: 359– 368.
56. Fuchs, E.,, and K. Weber. 1994. Intermediate filaments: structure, dynamics, function, and disease. Annu. Rev. Biochem. 63: 345– 382.
57. Fullner, K. J.,, W. I. Lencer,, and J. J. Mekalanos. 2001. Vibrio cholerae-induced cellular responses of polarized T84 intestinal epithelial cells are dependent on production of cholera toxin and the RTX toxin. Infect. Immun. 69: 6310– 6317.
58. Fullner, K. J.,, and J. J. Mekalanos. 2000. In vivo covalent cross-linking of cellular actin by the Vibrio cholerae RTX toxin. EMBO J. 19: 5315– 5323.
59. Furuse, M.,, K. Fujita,, T. Hiiragi,, K. Fujimoto,, and S. Tsukita. 1998. Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin. J. Cell Biol. 141: 1539– 1550.
60. Furuse, M.,, T. Hirase,, M. Itoh,, A. Nagafuchi,, S. Yonemura,, and S. Tsukita. 1993. Occludin: a novel integral membrane protein localizing at tight junctions. J. Cell Biol. 123: 1777– 1788.
61. Furuse, M.,, H. Sasaki,, and S. Tsukita. 1999. Manner of interaction of heterogeneous claudin species within and between tight junction strands. J. Cell Biol. 147: 891– 903.
62. Galan, J. E.,, and D. Zhou. 2000. Striking a balance: modulation of the actin cytoskeleton by Salmonella. Proc. Natl. Acad. Sci. USA 97: 8754– 8761.
63. Galyov, E. E.,, M. W. Wood,, R. Rosqvist,, P. B. Mullan,, P. R. Watson,, S. Hedges,, and T. S. Wallis. 1997. A secreted effector protein of Salmonella dublin is translocated into eukaryotic cells and mediates inflammation and fluid secretion in infected ileal mucosa. Mol. Microbiol. 25: 903– 912.
64. Gamblin, S. J.,, and S. J. Smerdon. 1998. GTPase-activating proteins and their complexes. Curr. Opin. Struct. Biol. 8: 195– 201.
65. Geiger, B.,, A. Bershadsky,, R. Pankov,, and K. M. Yamada. 2001. Transmembrane crosstalk between the extracellular matrix—cytoskeleton crosstalk. Nat. Rev. Mol. Cell Biol. 2: 793– 805.
66. Gerhard, R.,, G. Schmidt,, F. Hofmann,, and K. Aktories. 1998. Activation of Rho GTPases by Escherichia coli cytotoxic necrotizing factor 1 increases intestinal permeability in Caco-2 cells. Infect. Immun. 66: 5125– 5131.
67. Gilbert, T.,, A. Le Bivic,, A. Quaroni,, and E. Rodriguez-Boulan. 1991. Microtubular organization and its involvement in the biogenetic pathways of plasma membrane proteins in Caco-2 intestinal epithelial cells. J. Cell Biol. 113: 275– 288.
68. Glenney, J. R., Jr., P. Glenney, and K. Weber. 1983. The spectrin-related molecule, TW-260/240, cross-links the actin bundles of the microvillus rootlets in the brush borders of intestinal epithelial cells. J. Cell Biol. 96: 1491– 1496.
69. Goosney, D. L.,, R. DeVinney,, and B. B. Finlay. 2001. Recruitment of cytoskeletal and signaling proteins to enteropathogenic and enterohemorrhagic Escherichia coli pedestals. Infect. Immun. 69: 3315– 3322.
70. Gottardi, C. J.,, M. Arpin,, A. S. Fanning,, and D. Louvard. 1996. The junction-associated protein, zonula occludens-1, localizes to the nucleus before the maturation and during the remodeling of cell-cell contacts. Proc. Natl. Acad. Sci. USA 93: 10779– 10784.
71. Gottardi, C. J.,, and B. M. Gumbiner. 2001. Adhesion signaling: how beta-catenin interacts with its partners. Curr. Biol. 11: R792– R794.
72. Gruenheid, S.,, R. DeVinney,, F. Bladt,, D. Goosney,, S. Gelkop,, G. D. Gish,, T. Pawson,, and B. B. Finlay. 2001. Enteropathogenic E. coli Tir binds Nck to initiate actin pedestal formation in host cells. Nat. Cell Biol. 3: 856– 859.
73. Gumbiner, B.,, T. Lowenkopf,, and D. Apatira. 1991. Identification of a 160-kDa polypeptide that binds to the tight junction protein ZO-1. Proc. Natl. Acad. Sci. USA 88: 3460– 3464.
74. Gumbiner, B. M. 1996. Cell adhesion: the molecular basis of tissue architecture and morphogenesis. Cell 84: 345– 357.
75. Gumbiner, B. M. 1993. Proteins associated with the cytoplasmic surface of adhesion molecules. Neuron 11: 551– 564.
76. Gumbiner, B. M. 2000. Regulation of cadherin adhesive activity. J. Cell Biol. 148: 399– 404.
77. Gumbiner, B. M. 1995. Signal transduction of beta-catenin. Curr. Opin. Cell Biol. 7: 634– 640.
78. Gumbiner, B. M.,, and P. D. McCrea. 1993. Catenins as mediators of the cytoplasmic functions of cadherins. J. Cell Sci. Suppl. 17: 155– 158.
79. Gumbiner, B. M.,, and K. M. Yamada. 1995. Cell-to-cell contact and extracellular matrix. Curr. Opin. Cell Biol. 7: 615– 618.
80. Hardt, W. D.,, L. M. Chen,, K. E. Schuebel,, X. R. Bustelo,, and J. E. Galan. 1998. S. typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells. Cell 93: 815– 826.
81. Haskins, J.,, L. Gu,, E. S. Wittchen,, J. Hibbard,, and B. R. Stevenson. 1998. ZO-3, a novel member of the MAGUK protein family found at the tight junction, interacts with ZO-1 and occludin. J. Cell Biol. 141: 199– 208.
82. Hayward, R. D.,, and V. Koronakis. 1999. Direct nucleation and bundling of actin by the SipC protein of invasive Salmonella. EMBO J. 18: 4926– 4934.
83. Hayward, R. D.,, E. J. McGhie,, and V. Koronakis. 2000. Membrane fusion activity of purified SipB, a Salmonella surface protein essential for mammalian cell invasion. Mol. Microbiol. 37: 727– 739.
84. He, D.,, S. J. Hagen,, C. Pothoulakis,, M. Chen,, N. D. Medina,, M. Warny,, and J. T. LaMont. 2000. Clostridium difficile toxin A causes early damage to mitochondria in cultured cells. Gastroenterology 119: 139– 150.
85. Henderson, I. R.,, S. Hicks,, F. Navarro-Garcia,, W. P. Elias,, A. D. Philips,, and J. P. Nataro. 1999. Involvement of the enteroaggregative Escherichia coli plasmid-encoded toxin in causing human intestinal damage. Infect. Immun. 67: 5338– 5344.
86. Henderson, I. R.,, and J. P. Nataro. 2001. Virulence functions of autotransporter proteins. Infect. Immun. 69: 1231– 1243.
87.[Reference deleted.]
88. Henderson, I. R.,, F. Navarro-Garcia,, and J. P. Nataro. 1998. The great escape: structure and function of the autotransporter proteins. Trends Microbiol. 6: 370– 378.
89. Hersh, D.,, D. M. Monack,, M. R. Smith,, N. Ghori,, S. Falkow,, and A. Zychlinsky. 1999. The Salmonella invasin SipB induces macrophage apoptosis by binding to caspase-1. Proc. Natl. Acad. Sci. USA 96: 2396– 2401.
90. Higgs, H. N.,, and T. D. Pollard. 2001. Regulation of actin filament network formation through ARP2/3 complex: activation by a diverse array of proteins. Annu. Rev. Biochem. 70: 649– 676.
91. Hildebrand, J. D.,, M. D. Schaller,, and J. T. Parsons. 1995. Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase. Mol. Biol. Cell 6: 637– 647.
92. Hirst, R.,, A. Horwitz,, C. Buck,, and L. Rohrschneider. 1986. Phosphorylation of the fibronectin receptor complex in cells transformed by oncogenes that encode tyrosine kinases. Proc. Natl. Acad. Sci. USA 83: 6470– 6474.
93. Horwitz, A.,, K. Duggan,, C. Buck,, M. C. Beckerle,, and K. Burridge. 1986. Interaction of plasma membrane fibronectin receptor with talin—a transmembrane linkage. Nature 320: 531– 533.
94. Hueck, C. J. 1998. Type III protein secretion systems in bacterial pathogens of animals and plants. Microbiol. Mol. Biol. Rev. 62: 379– 433.
95. Hueck, C. J.,, M. J. Hantman,, V. Bajaj,, C. Johnston,, C. A. Lee,, and S. I. Miller. 1995. Salmonella typhimurium secreted invasion determinants are homologous to Shigella Ipa proteins. Mol. Microbiol. 18: 479– 490.
96. Ishii, K.,, and K. J. Green. 2001. Cadherin function: breaking the barrier. Curr. Biol. 11: R569– R572.
97. Jepson, M.,, B. Kenny,, and A. Leard. 2001. Role of sipA in the early stages of Salmonella typhimurium entry into epithelial cells. Cell. Microbiol. 3: 417– 426.
98. Johnson, R. P.,, and S. W. Craig. 1995. Factin binding site masked by the intramolecular association of vinculin head and tail domains. Nature 373: 261– 264.
99. Johnson, R. P.,, and S. W. Craig. 1994. An intramolecular association between the head and tail domains of vinculin modulates talin binding. J. Biol. Chem. 269: 12611– 12619.
100. Just, I.,, F. Hofmann,, and K. Aktories. 2000. Molecular mode of action of the large clostridial cytotoxins. Curr. Top. Microbiol. Immunol. 250: 55– 83.
101. Just, I.,, F. Hofmann,, H. Genth,, and R. Gerhard. 2001. Bacterial protein toxins inhibiting low-molecular-mass GTP-binding proteins. Int. J. Med. Microbiol. 291: 243– 250.
102. Kalman, D.,, O. D. Weiner,, D. L. Goosney,, J. W. Sedat,, B. B. Finlay,, A. Abo,, and J. M. Bishop. 1999. Enteropathogenic E. coli acts through WASP and Arp2/3 complex to form actin pedestals. Nat. Cell Biol. 1: 389– 391.
103. Kamm, K. E.,, and J. T. Stull. 2001. Dedicated myosin light chain kinases with diverse cellular functions. J. Biol. Chem. 276: 4527– 4530.
104. Kang, F.,, D. L. Purich,, and F. S. Southwick. 1999. Profilin promotes barbed-end actin filament assembly without lowering the critical concentration. J. Biol. Chem. 274: 36963– 36972.
105. Kaper, J. B.,, T. K. McDaniel,, K. G. Jarvis,, and O. Gomez-Duarte. 1997. Genetics of virulence of enteropathogenic E. coli. Adv. Exp. Med. Biol. 412: 279– 287.
106. Keller, T. C., 3rd, K. A. Conzelman, R. Chasan, and M. S. Mooseker. 1985. Role of myosin in terminal web contraction in isolated intestinal epithelial brush borders. J. Cell. Biol. 100: 1647– 1655.
107. Kenny, B.,, R. DeVinney,, M. Stein,, D. J. Reinscheid,, E. A. Frey,, and B. B. Finlay. 1997. Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells. Cell 91: 511– 520.
108. Kenny, B.,, S. Ellis,, A. D. Leard,, J. Warawa,, H. Mellor,, and M. A. Jepson. 2002. Co-ordinate regulation of distinct host cell signalling pathways by multifunctional enteropathogenic Escherichia coli effector molecules. Mol. Microbiol. 44: 1095– 1107.
109. Kenny, B.,, and M. Jepson. 2000. Targeting of an enteropathogenic Escherichia coli (EPEC) effector protein to host mitochondria. Cell Microbiol. 2: 579– 590.
110. Keon, B. H.,, S. Schafer,, C. Kuhn,, C. Grund,, and W. W. Franke. 1996. Symplekin, a novel type of tight junction plaque protein. J. Cell Biol. 134: 1003– 1018.
111. Knutton, S.,, I. Rosenshine,, M. J. Pallen,, I. Nisan,, B. C. Neves,, C. Bain,, C. Wolff,, G. Dougan,, and G. Frankel. 1998. A novel EspA-associated surface organelle of enteropathogenic Escherichia coli involved in protein translocation into epithelial cells. EMBO J 17: 2166– 2176.
112. Koshy, S. S.,, M. H. Montrose,, and C. L. Sears. 1996. Human intestinal epithelial cells swell and demonstrate actin rearrangement in response to the metalloprotease toxin of Bacteroides fragilis. Infect. Immun. 64: 5022– 5028.
113. Lerm, M.,, G. Schmidt,, and K. Aktories. 2000. Bacterial protein toxins targeting rho GTPases. FEMS Microbiol. Lett. 188: 1– 6.
114. Lesser, C. F.,, C. A. Scherer,, and S. I. Miller. 2000. Rac, ruffle and rho: orchestration of Salmonella invasion. Trends Microbiol. 8: 151– 152.
115. Lin, W.,, K. J. Fullner,, R. Clayton,, J. A. Sexton,, M. B. Rogers,, K. E. Calia,, S. B. Calderwood,, C. Fraser,, and J. J. Mekalanos. 1999. Identification of a Vibrio cholerae RTX toxin gene cluster that is tightly linked to the cholera toxin prophage. Proc. Natl. Acad. Sci. USA 96: 1071– 1076.
116. Lloyd, S. A.,, A. Forsberg,, H. Wolf-Watz,, and M. S. Francis. 2001. Targeting exported substrates to the Yersinia TTSS: different functions for different signals? Trends Microbiol. 9: 367– 371.
117. Lombardo, C. R.,, S. A. Weed,, S. P. Kennedy,, B. G. Forget,, and J. S. Morrow. 1994. Beta II-spectrin (fodrin) and beta I epsilon 2-spectrin (muscle) contain NH2-and COOHterminal membrane association domains (MAD1 and MAD2). J. Biol. Chem. 269: 29212– 29219.
118. Louvet-Vallee, S. 2000. ERM proteins: from cellular architecture to cell signaling. Biol. Cell 92: 305– 316.
119. Luo, Y.,, E. A. Frey,, R. A. Pfuetzner,, A. L. Creagh,, D. G. Knoechel,, C. A. Haynes,, B. B. Finlay,, and N. C. Strynadka. 2000. Crystal structure of enteropathogenic Escherichia coli intimin-receptor complex. Nature 405: 1073– 1077.
120. Madara, J. L.,, and K. Dharmsathaphorn. 1985. Occluding junction structure-function relationships in a cultured epithelial monolayer. J. Cell Biol. 101: 2124– 2133.
121. Marcial, M. A.,, S. L. Carlson,, and J. L. Madara. 1984. Partitioning of paracellular conductance along the ileal crypt-villus axis: a hypothesis based on structural analysis with detailed consideration of tight junction structurefunction relationships. J. Membr. Biol. 80: 59– 70.
122. Martin-Padura, I.,, S. Lostaglio,, M. Schneemann,, L. Williams,, M. Romano,, P. Fruscella,, C. Panzeri,, A. Stoppacciaro,, L. Ruco,, A. Villa,, D. Simmons,, and E. Dejana. 1998. Junctional adhesion molecule, a novel member of the immunoglobulin superfamily that distributes at intercellular junctions and modulates monocyte transmigration. J. Cell Biol. 142: 117– 127.
123. McClane, B. A. 2000. Clostridium perfringens enterotoxin and intestinal tight junctions. Trends Microbiol. 8: 145– 146.
124. McClane, B. A. 2001. The complex interactions between Clostridium perfringens enterotoxin and epithelial tight junctions. Toxicon 39: 1781– 1791.
125. McDaniel, T. K.,, and J. B. Kaper. 1997. A cloned pathogenicity island from enteropathogenic Escherichia coli confers the attaching and effacing phenotype on E. coli K-12. Mol. Microbiol. 23: 399– 407.
126. McGhie, E. J.,, R. D. Hayward,, and V. Koronakis. 2001. Cooperation between actinbinding proteins of invasive Salmonella: SipA potentiates SipC nucleation and bundling of actin. EMBO J. 20: 2131– 2139.
127. McGrath, J. L.,, E. A. Osborn,, Y. S. Tardy,, C. F. Dewey, Jr., and J. H. Hartwig. 2000. Regulation of the actin cycle in vivo by actin filament severing. Proc. Natl. Acad. Sci. USA 97: 6532– 6537.
128. McNamara, B.,, A. Koutsouris,, C. O’Connell,, J.-P. Nougayrede,, M. Donnenberg,, and G. Hecht. 2001. Translocated EspF protein from enteropathogenic Escherichia coli disrupts host intestinal barrier function. J. Clin. Invest. 107: 621– 629.
129. Menard, R.,, M. C. Prevost,, P. Gounon,, P. Sansonetti,, and C. Dehio. 1996. The secreted Ipa complex of Shigella flexneri promotes entry into mammalian cells. Proc. Natl. Acad. Sci. USA 93: 1254– 1258.
130. Meyer, R. K.,, and U. Aebi. 1990. Bundling of actin filaments by alpha-actinin depends on its molecular length. J. Cell Biol. 110: 2013– 2024.
131. Miao, E. A.,, C. A. Scherer,, R. M. Tsolis,, R. A. Kingsley,, L. G. Adams,, A. J. Baumler,, and S. I. Miller. 1999. Salmonella typhimurium leucine-rich repeat proteins are targeted to the SPI1 and SPI2 type III secretion systems. Mol. Microbiol. 34: 850– 864.
132. Miner, J. H. 1999. Renal basement membrane components. Kidney Int. 56: 2016– 2024.
133. Mitra, K.,, D. Zhou,, and J. E. Galan. 2000. Biophysical characterization of SipA, an actinbinding protein from Salmonella enterica. FEBS Lett. 482: 81– 84.
134. Moncrief, J. S.,, R. Obiso, Jr., L. A. Barroso, J. J. Kling, R. L. Wright, R. L. Van Tassell, D. M. Lyerly, and T. D. Wilkins. 1995. The enterotoxin of Bacteroides fragilis is a metalloprotease. Infect. Immun. 63: 175– 181.
135. Mooseker, M. S.,, K. A. Conzelman,, T. R. Coleman,, J. E. Heuser,, and M. P. Sheetz. 1989. Characterization of intestinal microvillar membrane disks: detergent-resistant membrane sheets enriched in associated brush border myosin I (110K-calmodulin). J. Cell Biol. 109: 1153– 1161.
136. Morita, K.,, M. Furuse,, K. Fujimoto,, and S. Tsukita. 1999. Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands. Proc. Natl. Acad. Sci. USA 96: 511– 516.
137. Morrow, J. S.,, C. D. Cianci,, T. Ardito,, A. S. Mann,, and M. Kashgarian. 1989. Ankyrin links fodrin to the alpha subunit of Na,KATPase in Madin-Darby canine kidney cells and in intact renal tubule cells. J. Cell Biol. 108: 455– 465.
138. Mounier, J.,, V. Laurent,, A. Hall,, P. Fort,, M. F. Carlier,, P. J. Sansonetti,, and C. Egile. 1999. Rho family GTPases control entry of Shigella flexneri into epithelial cells but not intracellular motility. J. Cell Sci. 112: 2069– 2080.
139. Mullins, R. D.,, J. A. Heuser,, and T. D. Pollard. 1998. The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl. Acad. Sci. USA 95: 6181– 6186.
140. Mullins, R. D.,, J. F. Kelleher,, J. Xu,, and T. D. Pollard. 1998. Arp2/3 complex from Acanthamoeba binds profilin and cross-links actin filaments. Mol. Biol. Cell. 9: 841– 852.
141. Mullins, R. D.,, and T. D. Pollard. 1999. Structure and function of the Arp2/3 complex. Curr. Opin. Struct. Biol. 9: 244– 249.
142. Nakatani, Y.,, K. Masudo,, Y. Miyagi,, Y. Inayama,, N. Kawano,, Y. Tanaka,, K. Kato,, T. Ito,, H. Kitamura,, Y. Nagashima,, S. Yamanaka,, N. Nakamura,, J. Sano,, N. Ogawa,, N. Ishiwa,, K. Notohara,, M. Resl,, and E. J. Mark. 2002. Aberrant nuclear localization and gene mutation of beta-catenin in low-grade adenocarcinoma of fetal lung type: up-regulation of the Wnt signaling pathway may be a common denominator for the development of tumors that form morules. Mod. Pathol. 15: 617– 624.
143. Navarro-Garcia, F.,, A. Canizalez-Roman,, J. Luna,, C. Sears,, and J. P. Nataro. 2001. Plasmid-encoded toxin of enteroaggregative Escherichia coli is internalized by epithelial cells. Infect. Immun. 69: 1053– 1060.
144. Navarro-Garcia, F.,, C. Eslava,, J. M. Villaseca,, R. Lopez-Revilla,, J. R. Czeczulin,, S. Srinivas,, J. P. Nataro,, and A. Cravioto. 1998. In vitro effects of a high-molecularweight heat-labile enterotoxin from enteroaggregative Escherichia coli. Infect. Immun. 66: 3149– 3154.
145. Navarro-Garcia, F.,, C. Sears,, C. Eslava,, A. Cravioto,, and J. P. Nataro. 1999. Cytoskeletal effects induced by pet, the serine protease enterotoxin of enteroaggregative Escherichia coli. Infect. Immun. 67: 2184– 2192.
146. Nelson, W. J.,, and P. J. Veshnock. 1987. Ankyrin binding to (Na ++ K +)ATPase and implications for the organization of membrane domains in polarized cells. Nature 328: 533– 536.
147. Nguyen, L.,, I. T. Paulsen,, J. Tchieu,, C. J. Hueck,, and M. H. Saier, Jr. 2000. Phylogenetic analyses of the constituents of Type III protein secretion systems. J. Mol. Microbiol. Biotechnol. 2: 125– 144.
148. Nhieu, G. T.,, and P. J. Sansonetti. 1999. Mechanism of Shigella entry into epithelial cells. Curr. Opin. Microbiol. 2: 51– 55.
149. Nievers, M. G.,, I. Kuikman,, D. Geerts,, I. M. Leigh,, and A. Sonnenberg. 2000. Formation of hemidesmosome-like structures in the absence of ligand binding by the (alpha)6(beta)4 integrin requires binding of HD1/plectin to the cytoplasmic domain of the (beta)4 integrin subunit. J. Cell Sci. 113(Part 6): 963– 973.
150. Noren, N. K.,, C. M. Niessen,, B. M. Gumbiner,, and K. Burridge. 2001. Cadherin engagement regulates Rho family GTPases. J. Biol. Chem. 276: 33305– 33308.
151. Norris, F. A.,, M. P. Wilson,, T. S. Wallis,, E. E. Galyov,, and P. W. Majerus. 1998. SopB, a protein required for virulence of Salmonella dublin, is an inositol phosphate phosphatase. Proc. Natl. Acad. Sci. USA 95: 14057– 14059.
152. Nusrat, A.,, M. Giry,, J. R. Turner,, S. P. Colgan,, C. A. Parkos,, D. Carnes,, E. Lemichez,, P. Boquet,, and J. L. Madara. 1995. Rho protein regulates tight junctions and perijunctional actin organization in polarized epithelia. Proc. Natl. Acad. Sci. USA 92: 10629– 10633.
153. Obiso, R. J., Jr.,, A. O. Azghani,, and T. D. Wilkins. 1997. The Bacteroides fragilis toxin fragilysin disrupts the paracellular barrier of epithelial cells. Infect. Immun. 65: 1431– 1439.
154. Obiso, R. J., Jr.,, D. M. Lyerly,, R. L. Van Tassell,, and T. D. Wilkins. 1995. Proteolytic activity of the Bacteroides fragilis enterotoxin causes fluid secretion and intestinal damage in vivo. Infect. Immun. 63: 3820– 3826.
155. Osiecki, J. C.,, J. Barker,, W. L. Picking,, A. B. Serfis,, E. Berring,, S. Shah,, A. Harrington,, and W. D. Picking. 2001. IpaC from Shigella and SipC from Salmonella possess similar biochemical properties but are functionally distinct. Mol. Microbiol. 42: 469– 481.
156. Otey, C. A.,, F. M. Pavalko,, and K. Burridge. 1990. An interaction between alphaactinin and the beta 1 integrin subunit in vitro. J. Cell Biol. 111: 721– 729.
157. Phillips, A.,, J. Giron,, S. Hicks,, G. Dougan,, and G. Frankel. 2000. Intimin from enteropathogenic Escherichia coli mediates remodelling of the eukaryotic cell surface. Microbiology 146: 1333– 1344.
158. Pollard, T. D.,, L. Blanchoin,, and R. D. Mullins. 2001. Actin dynamics. J. Cell Sci. 114: 3– 4.
159. Pothoulakis, C. 2000. Effects of Clostridium difficile toxins on epithelial cell barrier. Ann. N.Y. Acad. Sci. 915: 347– 356.
160. Pothoulakis, C.,, and J. T. Lamont. 2001. Microbes and microbial toxins: paradigms for microbial-mucosal interactions. II. The integrated response of the intestine to Clostridium difficile toxins. Am. J. Physiol. Gastrointest. Liver Physiol. 280: G178– G183.
161. Ressad, F.,, D. Didry,, C. Egile,, D. Pantaloni,, and M. F. Carlier. 1999. Control of actin filament length and turnover by actin depolymerizing factor (ADF/cofilin) in the presence of capping proteins and ARP2/3 complex. J. Biol. Chem. 274: 20970– 20976.
162. Richard, J. F.,, L. Petit,, M. Gibert,, J. C. Marvaud,, C. Bouchaud,, and M. R. Popoff. 1999. Bacterial toxins modifying the actin cytoskeleton. Int. Microbiol. 2: 185– 194.
163. Ridley, A. J. 2001. Rho family proteins: coordinating cell responses. Trends Cell Biol. 11: 471– 477.
164. Ridley, A. J. 2001. Rho GTPases and cell migration. J. Cell Sci. 114: 2713– 2722.
165. Riegler, M.,, M. Lotz,, C. Sears,, C. Pothoulakis,, I. Castagliuolo,, C. C. Wang,, R. Sedivy,, T. Sogukoglu,, E. Cosentini,, G. Bischof,, W. Feil,, B. Teleky,, G. Hamilton,, J. T. LaMont,, and E. Wenzl. 1999. Bacteroides fragilis toxin 2 damages human colonic mucosa in vitro. Gut 44: 504– 510.
166. Rippere-Lampe, K. E.,, A. D. O’Brien,, R. Conran,, and H. A. Lockman. 2001. Mutation of the gene encoding cytotoxic necrotizing factor type 1 (cnf[1]) attenuates the virulence of uropathogenic Escherichia coli. Infect. Immun. 69: 3954– 3964.
167. Rosenshine, I.,, S. Ruschkowski,, M. Stein,, D. J. Reinscheid,, S. D. Mills,, and B. B. Finlay. 1996. A pathogenic bacterium triggers epithelial signals to form a functional bacterial receptor that mediates actin pseudopod formation. EMBO J. 15: 2613– 2624.
168. Rudolph, M. G.,, C. Weise,, S. Mirold,, B. Hillenbrand,, B. Bader,, A. Wittinghofer,, and W. D. Hardt. 1999. Biochemical analysis of SopE from Salmonella typhimurium, a highly efficient guanosine nucleotide exchange factor for Rho GTPases. J. Biol. Chem. 274: 30501– 30509.
169. Saidi, R. F.,, K. Jaeger,, M. H. Montrose,, S. Wu,, and C. L. Sears. 1997. Bacteroides fragilis toxin rearranges the actin cytoskeleton of HT29/C1 cells without direct proteolysis of actin or decrease in F-actin content. Cell Motil. Cytoskel. 37: 159– 165.
170. Saidi, R. F.,, and C. L. Sears. 1996. Bacteroides fragilis toxin rapidly intoxicates human intestinal epithelial cells (HT29/C1) in vitro. Infect. Immun. 64: 5029– 5034.
171. Saitou, M.,, Y. Ando-Akatsuka,, M. Itoh,, M. Furuse,, J. Inazawa,, K. Fujimoto,, and S. Tsukita. 1997. Mammalian occludin in epithelial cells: its expression and subcellular distribution. Eur. J. Cell Biol. 73: 222– 231.
172. Sarker, M. R.,, U. Singh,, and B. A. Mc-Clane. 2000. An update on Clostridium perfringens enterotoxin. J. Nat. Toxins 9: 251– 266.
173. Sasaki, T.,, and Y. Takai. 1998. The Rho small G protein family-Rho GDI system as a temporal and spatial determinant for cytoskeletal control. Biochem. Biophys. Res. Commun. 245: 641– 645.
174. Sastry, S. K.,, M. Lakonishok,, S. Wu,, T. Q. Truong,, A. Huttenlocher,, C. E. Turner,, and A. F. Horwitz. 1999. Quantitative changes in integrin and focal adhesion signaling regulate myoblast cell cycle withdrawal. J. Cell Biol. 144: 1295– 1309.
175. Schaller, M. D.,, C. A. Borgman,, B. S. Cobb,, R. R. Vines,, A. B. Reynolds,, and J. T. Parsons. 1992. pp125FAK, a structurally distinctive protein-tyrosine kinase associated with focal adhesions. Proc. Natl. Acad. Sci. USA 89: 5192– 5196.
176. Schaller, M. D.,, C. A. Otey,, J. D. Hildebrand,, and J. T. Parsons. 1995. Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains. J. Cell Biol. 130: 1181– 1187.
177. Schmidt, G.,, and K. Aktories. 1998. Bacterial cytotoxins target Rho GTPases. Naturwissenschaften 85: 253– 261.
178. Schmidt, G.,, and K. Aktories. 2000. Rho GTPase-activating toxins: cytotoxic necrotizing factors and dermonecrotic toxin. Methods Enzymol. 325: 125– 136.
179. Schnittler, H. J.,, S. W. Schneider,, H. Raifer,, F. Luo,, P. Dieterich,, I. Just,, and K. Aktories. 2001. Role of actin filaments in endothelial cell-cell adhesion and membrane stability under fluid shear stress. Pflugers Arch. 442: 675– 687.
180. Sears, C. L. 2000. Molecular physiology and pathophysiology of tight junctions V. Assault of the tight junction by enteric pathogens. Am. J. Physiol. Gastrointest. Liver Physiol. 279: G1129– G1134.
181. Sears, C. L. 2001. The toxins of Bacteroides fragilis. Toxicon 39: 1737– 1746.
182. Sears, C. L.,, L. L. Myers,, A. Lazenby,, and R. L. Van Tassell. 1995. Enterotoxigenic Bacteroides fragilis. Clin. Infect. Dis. 20(Suppl. 2): S142– S148.
183. Sinclair, J. F.,, and A. D. O’Brien. 2002. Cell-surface localized nucleolin is a eucaryotic receptor for the adhesin intimin-γ of enterohemorrhagic Escherichia coli O157:H7. J. Biol. Chem. 277: 2876– 2885.
184. Skoudy, A.,, J. Mounier,, A. Aruffo,, H. Ohayon,, P. Gounon,, P. Sansonetti,, and G. Tran Van Nhieu. 2000. CD44 binds to the Shigella IpaB protein and participates in bacterial invasion of epithelial cells. Cell Microbiol. 2: 19– 33.
185. Sonoda, N.,, M. Furuse,, H. Sasaki,, S. Yonemura,, J. Katahira,, Y. Horiguchi,, and S. Tsukita. 1999. Clostridium perfringens enterotoxin fragment removes specific claudins from tight junction strands: evidence for direct involvement of claudins in tight junction barrier. J. Cell Biol. 147: 195– 204.
186. Southwick, F. S. 2000. Gelsolin and ADF/cofilin enhance the actin dynamics of motile cells. Proc. Natl. Acad. Sci. USA 97: 6936– 6938.
187. Spinardi, L.,, S. Einheber,, T. Cullen,, T. A. Milner,, and F. G. Giancotti. 1995. A recombinant tail-less integrin beta 4 subunit disrupts hemidesmosomes, but does not suppress alpha 6 beta 4-mediated cell adhesion to laminins. J. Cell Biol. 129: 473– 487.
188. Steele-Mortimer, O.,, L. A. Knodler,, S. L. Marcus,, M. P. Scheid,, B. Goh,, C. G. Pfeifer,, V. Duronio,, and B. B. Finlay. 2000. Activation of Akt/protein kinase B in epithelial cells by the Salmonella typhimurium effector sigD. J. Biol. Chem. 275: 37718– 37724.
189. Steinbock, F. A.,, and G. Wiche. 1999. Plectin: a cytolinker by design. Biol. Chem. 380: 151– 158.
190. Stevenson, B. R.,, J. D. Siliciano,, M. S. Mooseker,, and D. A. Goodenough. 1986. Identification of ZO-1: a high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia. J. Cell Biol. 103: 755– 766.
191. Stossel, T. P.,, J. Condeelis,, L. Cooley,, J. H. Hartwig,, A. Noegel,, M. Schleicher,, and S. S. Shapiro. 2001. Filamins as integrators of cell mechanics and signalling. Nat. Rev. Mol. Cell. Biol. 2: 138– 145.
192. Stutzmann, J.,, A. Bellissent-Waydelich,, L. Fontao,, J. F. Launay,, and P. Simon-Assmann. 2000. Adhesion complexes implicated in intestinal epithelial cell-matrix interactions. Microsc. Res. Tech. 51: 179– 190.
193. Sukhan, A.,, T. Kubori,, J. Wilson,, and J. E. Galan. 2001. Genetic analysis of assembly of the Salmonella enterica serovar Typhimurium type III secretion-associated needle complex. J. Bacteriol. 183: 1159– 1167.
194. Sun, H. Q.,, M. Yamamoto,, M. Mejillano,, and H. L. Yin. 1999. Gelsolin, a multifunctional actin regulatory protein. J. Biol. Chem. 274: 33179– 33182.
195. Taylor, K. A.,, P. W. Luther,, and M. S. Donnenberg. 1999. Expression of the EspB protein of enteropathogenic Escherichia coli within HeLa cells affects stress fibers and cellular morphology. Infect. Immun. 67: 120– 125.
196. Temm-Grove, C. J.,, B. M. Jockusch,, R. P. Weinberger,, G. Schevzov,, and D. M. Helfman. 1998. Distinct localizations of tropomyosin isoforms in LLC-PK1 epithelial cells suggests specialized function at cell-cell adhesions. Cell Motil. Cytoskeleton 40: 393– 407.
197. Toyotome, T.,, T. Suzuki,, A. Kuwae,, T. Nonaka,, H. Fukuda,, S. Imajoh-Ohmi,, T. Toyofuku,, M. Hori,, and C. Sasakawa. 2001. Shigella protein IpaH(9.8) is secreted from bacteria within mammalian cells and transported to the nucleus. J. Biol. Chem. 276: 32071– 32079.
198. Tran Van Nhieu, G.,, A. Ben-Ze’ev,, and P. J. Sansonetti. 1997. Modulation of bacterial entry into epithelial cells by association between vinculin and the Shigella IpaA invasin. EMBO J. 16: 2717– 2729.
199. Tran Van Nhieu, G.,, E. Caron,, A. Hall,, and P. J. Sansonetti. 1999. IpaC induces actin polymerization and filopodia formation during Shigella entry into epithelial cells. EMBO J. 18: 3249– 3262.
200. Tsukamoto, T.,, and S. K. Nigam. 1997. Tight junction proteins form large complexes and associate with the cytoskeleton in an ATP depletion model for reversible junction assembly. J. Biol. Chem. 272: 16133– 16139.
201. Tsukita, S.,, K. Oishi,, N. Sato,, J. Sagara,, and A. Kawai. 1994. ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons. J. Cell Biol. 126: 391– 401.
202. Turner, C. E.,, J. R. Glenney, Jr.,, and K. Burridge. 1990. Paxillin: a new vinculinbinding protein present in focal adhesions. J. Cell Biol. 111: 1059– 1068.
203. Ursitti, J.,, and R. Bloch,. 2001. Spectrin, p. 2965– 2971. In T. Creighton (ed.), Encyclopedia of Molecular Medicine, vol. 5. John Wiley & Sons, New York. N.Y.
204. Uzzau, S.,, P. Cappuccinelli,, and A. Fasano. 1999. Expression of Vibrio cholerae zonula occludens toxin and analysis of its subcellular localization. Microb. Pathog. 27: 377– 385.
205. Uzzau, S.,, R. Lu,, W. Wang,, C. Fiore,, and A. Fasano. 2001. Purification and preliminary characterization of the zonula occludens toxin receptor from human (CaCo2) and murine (IEC6) intestinal cell lines. FEMS Microbiol. Lett. 194: 1– 5.
206. Villaseca, J. M.,, F. Navarro-Garcia,, G. Mendoza-Hernandez,, J. P. Nataro,, A. Cravioto,, and C. Eslava. 2000. Pet toxin from enteroaggregative Escherichia coli produces cellular damage associated with fodrin disruption. Infect. Immun. 68: 5920– 5927.
207. Wahl, S.,, H. Barth,, T. Ciossek,, K. Aktories,, and B. K. Mueller. 2000. Ephrin-A5 induces collapse of growth cones by activating Rho and Rho kinase. J. Cell Biol. 149: 263– 270.
208. Waldor, M. K.,, and J. J. Mekalanos. 1996. Lysogenic conversion by a filamentous phage encoding cholera toxin. Science 272: 1910– 1914.
209. Wang, W.,, S. Uzzau,, S. E. Goldblum,, and A. Fasano. 2000. Human zonulin, a potential modulator of intestinal tight junctions. J. Cell Sci. 113(Part 24): 4435– 4440.
210. Watarai, M.,, S. Funato,, and C. Sasakawa. 1996. Interaction of Ipa proteins of Shigella flexneri with alpha5beta1 integrin promotes entry of the bacteria into mammalian cells. J. Exp. Med. 183: 991– 999.
211. Werb, Z.,, P. M. Tremble,, O. Behrendtsen,, E. Crowley,, and C. H. Damsky. 1989. Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression. J. Cell Biol. 109: 877– 889.
212. Wieler, L. H.,, T. K. McDaniel,, T. S. Whittam,, and J. B. Kaper. 1997. Insertion site of the locus of enterocyte effacement in enteropathogenic and enterohemorrhagic Escherichia coli differs in relation to the clonal phylogeny of the strains. FEMS Microbiol. Lett. 156: 49– 53.
213. Wilde, C.,, and K. Aktories. 2001. The Rho-ADP-ribosylating C3 exoenzyme from Clostridium botulinum and related C3-like transferases. Toxicon 39: 1647– 1660.
214. Williams, A. W.,, and S. C. Straley. 1998. YopD of Yersinia pestis plays a role in negative regulation of the low-calcium response in addition to its role in translocation of Yops. J. Bacteriol. 180: 350– 358.
215. Windoffer, R.,, M. Borchert-Stuhltrager,, and R. E. Leube. 2002. Desmosomes: interconnected calcium-dependent structures of remarkable stability with significant integral membrane protein turnover. J. Cell Sci. 115: 1717– 1732.
216. Wood, M. W.,, M. A. Jones,, P. R. Watson,, A. M. Siber,, B. A. McCormick,, S. Hedges,, R. Rosqvist,, T. S. Wallis,, and E. E. Galyov. 2000. The secreted effector protein of Salmonella dublin, SopA, is translocated into eukaryotic cells and influences the induction of enteritis. Cell Microbiol. 2: 293– 303.
217. Wu, S.,, L. A. Dreyfus,, A. O. Tzianabos,, C. Hayashi,, and C. L. Sears. 2002. Diversity of the metalloprotease toxin produced by enterotoxigenic Bacteroides fragilis. Infect. Immun. 70: 2463– 2471.
218. Wu, S.,, K. C. Lim,, J. Huang,, R. F. Saidi,, and C. L. Sears. 1998. Bacteroides fragilis enterotoxin cleaves the zonula adherens protein, E-cadherin. Proc. Natl. Acad. Sci. USA 95: 14979– 14984.
219. Yap, A. S.,, W. M. Brieher,, and B. M. Gumbiner. 1997. Molecular and functional analysis of cadherin-based adherens junctions. Annu. Rev. Cell Dev. Biol. 13: 119– 146.
220. Yonemura, S.,, and S. Tsukita. 1999. Direct involvement of ezrin/radixin/moesin (ERM)-binding membrane proteins in the organization of microvilli in collaboration with activated ERM proteins. J. Cell Biol. 145: 1497– 1509.
221. Zhou, D. 2001. Collective efforts to modulate the host actin cytoskeleton by Salmonella type III-secreted effector proteins. Trends Microbiol. 9: 567– 569.
222. Zhou, D.,, L. M. Chen,, L. Hernandez,, S. B. Shears,, and J. E. Galan. 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– 259.
223. Zhou, D.,, M. S. Mooseker,, and J. E. Galan. 1999. An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin. Proc. Natl. Acad. Sci. USA 96: 10176– 10181.
224. Zhou, D.,, M. S. Mooseker,, and J. E. Galan. 1999. Role of the S. Typhimurium actin-binding protein SipA in bacterial internalization. Science 283: 2092– 2095.

Tables

Enteric Microbial Toxins and the Intestinal Epithelial Cytoskeleton
[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/10.1128/9781555817848.chap17-1,webId=/content/author/10.1128/9781555817848.chap17-1,properties={foaf_givenname=James P., foaf_name=James P. Nataro, foaf_surname=Nataro, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/10.1128/9781555817848.chap17-aff1]]}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/10.1128/9781555817848.chap17-2,webId=/content/author/10.1128/9781555817848.chap17-2,properties={foaf_givenname=Cynthia, foaf_name=Cynthia Sears, foaf_surname=Sears, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/10.1128/9781555817848.chap17-aff2]]}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/10.1128/9781555817848.chap17-3,webId=/content/author/10.1128/9781555817848.chap17-3,properties={foaf_givenname=Alessio, foaf_name=Alessio Fasano, foaf_surname=Fasano, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/10.1128/9781555817848.chap17-aff3]]}], com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/10.1128/9781555817848.chap17-4,webId=/content/author/10.1128/9781555817848.chap17-4,properties={foaf_givenname=Robert J., foaf_name=Robert J. Bloch, foaf_surname=Bloch, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/10.1128/9781555817848.chap17-aff4]]}]]
Citation: Nataro J, Sears C, Fasano A, Bloch R. 2003. Enteric Microbial Toxins and the Intestinal Epithelial Cytoskeleton, p 301-332. In Hecht G (ed), Microbial Pathogenesis and the Intestinal Epithelial Cell. ASM Press, Washington, DC. doi: 10.1128/9781555817848.ch17
/content/10.1128/9781555817848.chap17.tab17-1
TABLE 1

Major structural proteins of the cytoskeleton

Generic image for table
TABLE 1

Major structural proteins of the cytoskeleton

Citation: Nataro J, Sears C, Fasano A, Bloch R. 2003. Enteric Microbial Toxins and the Intestinal Epithelial Cytoskeleton, p 301-332. In Hecht G (ed), Microbial Pathogenesis and the Intestinal Epithelial Cell. ASM Press, Washington, DC. doi: 10.1128/9781555817848.ch17

Back to top
This is a required field
Please enter a valid email address
Please check the format of the address you have entered.
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error