A common structural motif in the binding of virulence factors to bacterial secretion chaperones

Molecular Cell

Volumn 21, Issue 5, 2006, Pages 653-664

  Lilic, Mirjana ^a   Vujanac, Milos ^a   Stebbins, C Erec ^a  

^a ROCKEFELLER UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; GLOBULAR PROTEIN; POLYPEPTIDE; PROTEIN A; VIRULENCE FACTOR;

ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; CRYSTAL STRUCTURE; HOST CELL; NONHUMAN; PROTEIN DOMAIN; PROTEIN SECRETION; PROTEIN STRUCTURE; SALMONELLA; SPECIES IDENTIFICATION;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; GENE TARGETING; MICROFILAMENT PROTEINS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SALMONELLA TYPHIMURIUM; VIRULENCE FACTORS;

BACTERIA (MICROORGANISMS); SALMONELLA;

EID: 33344459126     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2006.01.026     Document Type: Article

References (42)

1. Y. Akeda, and J.E. Galan Chaperone release and unfolding of substrates in type III secretion Nature 437 2005 911 915
2. J.T. Barbieri, M.J. Riese, and K. Aktories Bacterial toxins that modify the actin cytoskeleton Annu. Rev. Cell Dev. Biol. 18 2002 315 344
3. S.C. Birtalan, R.M. Phillips, and P. Ghosh Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens Mol. Cell 9 2002 971 980
4. P.A. Bronstein, E.A. Miao, and S.I. Miller InvB is a type III secretion chaperone specific for SspA J. Bacteriol. 182 2000 6638 6644
5. G.R. Cornelis Type III secretion: a bacterial device for close combat with cells of their eukaryotic host Philos. Trans. R. Soc. Lond. B Biol. Sci. 355 2000 681 693
6. S. Doublie Preparation of selenomethionyl proteins for phase determination Methods Enzymol. 276 1997 523 530
7. K. Ehrbar, A. Friebel, S.I. Miller, and W.D. Hardt Role of the Salmonella pathogenicity island 1 (SPI-1) protein InvB in type III secretion of SopE and SopE2, two Salmonella effector proteins encoded outside of SPI-1 J. Bacteriol. 185 2003 6950 6967
8. K. Ehrbar, S. Hapfelmeier, B. Stecher, and W.D. Hardt InvB is required for type III-dependent secretion of SopA in Salmonella enterica serovar Typhimurium J. Bacteriol. 186 2004 1215 1219
9. J.E. Galan Salmonella interactions with host cells: type III secretion at work Annu. Rev. Cell Dev. Biol. 17 2001 53 86
10. J.E. Galan, and A. Collmer Type III secretion machines: bacterial devices for protein delivery into host cells Science 284 1999 1322 1328
11. A. Gauthier, and B.B. Finlay Translocated intimin receptor and its chaperone interact with ATPase of the type III secretion apparatus of enteropathogenic Escherichia coli J. Bacteriol. 185 2003 6747 6755
12. P. Ghosh Process of protein transport by the type III secretion system Microbiol. Mol. Biol. Rev. 68 2004 771 795
13. C.J. Hueck Type III protein secretion systems in bacterial pathogens of animals and plants Microbiol. Mol. Biol. Rev. 62 1998 379 433
14. K. Kaniga, D. Trollinger, and J.E. Galan Identification of two targets of the type III protein secretion system encoded by the inv and spa loci of Salmonella typhimurium that have homology to the Shigella IpaD and IpaA proteins J. Bacteriol. 177 1995 7078 7085
15. S.H. Lee, and J.E. Galan InvB is a type III secretion-associated chaperone for the Salmonella enterica effector protein SopE J. Bacteriol. 185 2003 7279 7284
16. S.H. Lee, and J.E. Galan Salmonella type III secretion-associated chaperones confer secretion-pathway specificity Mol. Microbiol. 51 2004 483 495
17. M. Lerm, G. Schmidt, and K. Aktories Bacterial protein toxins targeting rho GTPases FEMS Microbiol. Lett. 188 2000 1 6
18. M. Lilic, V.E. Galkin, A. Orlova, M.S. VanLoock, E.H. Egelman, and C.E. Stebbins Salmonella SipA polymerizes actin by stapling filaments with nonglobular protein arms Science 301 2003 1918 1921
19. H.A. Lockman, and R. Curtiss III Salmonella typhimurium mutants lacking flagella or motility remain virulent in BALB/c mice Infect. Immun. 58 1990 137 143
20. Y. Luo, M.G. Bertero, E.A. Frey, R.A. Pfuetzner, M.R. Wenk, L. Creagh, S.L. Marcus, D. Lim, F. Sicheri, and C. Kay Structural and biochemical characterization of the type III secretion chaperones CesT and SigE Nat. Struct. Biol. 8 2001 1006 1008
21. E.J. McGhie, R.D. Hayward, and V. Koronakis Cooperation between actin-binding proteins of invasive Salmonella: SipA potentiates SipC nucleation and bundling of actin EMBO J. 20 2001 2131 2139
22. G.N. Murshudov, A.A. Vagin, and E.J. Dodson Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallogr. D Biol. Crystallogr. 53 1997 240 255
23. Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
24. C. Parsot, C. Hamiaux, and A.L. Page The various and varying roles of specific chaperones in type III secretion systems Curr. Opin. Microbiol. 6 2003 7 14
25. A. Perrakis, R. Morris, and V.S. Lamzin Automated protein model building combined with iterative structure refinement Nat. Struct. Biol. 6 1999 458 463
26. J. Phan, J.E. Tropea, and D.S. Waugh Structure of the Yersinia pestis type III secretion chaperone SycH in complex with a stable fragment of YscM2 Acta Crystallogr. D Biol. Crystallogr. 60 2004 1591 1599
27. K.S. Ramamurthi, and O. Schneewind Substrate recognition by the Yersinia type III protein secretion machinery Mol. Microbiol. 50 2003 1095 1102
28. W.R. Rypniewski, H.M. Holden, and I. Rayment Structural consequences of reductive methylation of lysine residues in hen egg white lysozyme: an X-ray analysis at 1.8 Å resolution Biochemistry 32 1993 9851 9858
29. G. Schiavo, and F.G. van der Goot The bacterial toxin toolkit Nat. Rev. Mol. Cell Biol. 2 2001 530 537
30. T.R. Schneider, and G.M. Sheldrick Substructure solution with SHELXD Acta Crystallogr. D Biol. Crystallogr. 58 2002 1772 1779
31. F.D. Schubot, M.W. Jackson, K.J. Penrose, S. Cherry, J.E. Tropea, G.V. Plano, and D.S. Waugh Three-dimensional structure of a macromolecular assembly that regulates type III secretion in Yersinia pestis J. Mol. Biol. 346 2005 1147 1161
32. A.U. Singer, D. Desveaux, L. Betts, J.H. Chang, Z. Nimchuk, S.R. Grant, J.L. Dangl, and J. Sondek Crystal structures of the type III effector protein AvrPphF and its chaperone reveal residues required for plant pathogenesis Structure (Camb.) 12 2004 1669 1681
33. C.E. Stebbins, and J.E. Galan Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion Nature 414 2001 77 81
34. C.E. Stebbins, and J.E. Galan Structural mimicry in bacterial virulence Nature 412 2001 701 705
35. C.E. Stebbins, and J.E. Galan Priming virulence factors for delivery into the host Nat. Rev. Mol. Cell Biol. 4 2003 738 743
36. A. van Eerde, C. Hamiaux, J. Perez, C. Parsot, and B.W. Dijkstra Structure of Spa15, a type III secretion chaperone from Shigella flexneri with broad specificity EMBO Rep. 5 2004 477 483
37. R.F. Wang, and S.R. Kushner Construction of versatile low-copy-number vectors for cloning, sequencing and gene expression in Escherichia coli Gene 100 1991 195 199
38. P. Wattiau, S. Woestyn, and G.R. Cornelis Customized secretion chaperones in pathogenic bacteria Mol. Microbiol. 20 1996 255 262
39. M.D. Winn, M.N. Isupov, and G.N. Murshudov Use of TLS parameters to model anisotropic displacements in macromolecular refinement Acta Crystallogr. D Biol. Crystallogr. 57 2001 122 133
40. M.D. Winn, G.N. Murshudov, and M.Z. Papiz Macromolecular TLS refinement in REFMAC at moderate resolutions Methods Enzymol. 374 2003 300 321
41. M.L. Zaharik, S. Gruenheid, A.J. Perrin, and B.B. Finlay Delivery of dangerous goods: type III secretion in enteric pathogens Int. J. Med. Microbiol. 291 2002 593 603
42. D. Zhou, M.S. Mooseker, and J.E. Galan Role of the S. typhimurium actin-binding protein SipA in bacterial internalization Science 283 1999 2092 2095