User menu

Accès à distance ? S'identifier sur le proxy UCLouvain

Customized secretion chaperones in pathogenic bacteria.

Primary tabs

Wattiau, Pierre [UCL] WOESTYN, SOPHIE [UCL] Cornelis, Guy R. [UCL]

Pathogenic yersiniae secrete about a dozen anti-host proteins, the Yops, by a pathway which does not involve cleavage of a classical signal peptide. The Yop secretory apparatus, called Ysc, for Yop secretion, is the archetype of type III secretion systems (which serve for the secretion of virulence proteins by several animal and plant pathogens) and is related to the flagellar assembly apparatus. The Yop secretion signal is N-terminal but has not been defined to date. Apart from the Ysc machinery, secretion of at least four Yops requires cytoplasmic proteins called Syc (for specific Yop chaperone). Each Syc protein binds to its cognate Yop. Unlike most cytoplasmic chaperones, these proteins do not have an ATP-binding domain, and are presumably devoid of ATPase activity. They share a few common properties: an acidic pl, a size in the range of 15-20 kDa, and a putative amphipathic alpha-helix in the C-terminal portion. They were recently shown to have counterparts in other pathogenic bacteria, where they appear to have a similar function.

Document type Article de périodique (Journal article) – Journal Article, Research Support, Non-U.S. Gov't, Review
Publication date 1996
Journal information "Molecular microbiology" - Vol. 20, no. 2, p. 255-62 (1996)
Peer reviewed yes
issn 0950-382X
Publication status Publié
Affiliation UCL - MD/MIGE - Département de microbiologie, d'immunologie et de génétique
MESH Subject Amino Acid Sequence ; Animals ; Bacterial Outer Membrane Proteins - metabolism ; Bacterial Proteins - metabolism ; Molecular Chaperones - chemistry - metabolism ; Molecular Sequence Data ; Trans-Activators - metabolism ; Yersinia - metabolism - pathogenicity
Links
  1. Albertini A.M., J Bacteriol, 173, 3573 (1991)
  2. Allaoui A., Mol Microbiol, 7, 59 (1993)
  3. Allaoui A., J Bacteriol, 176, 4534 (1994)
  4. Allaoui A., J Bacteriol, 177, 4230 (1995)
  5. Allaoui Abdelmounaaïm, Schulte Ralf, Cornelis Guy R., Mutational analysis of theYersinia enterocolitica virCoperon: characterization ofyscE, F, G, I, J, Krequired for Yop secretion andyscHencoding YopR, 10.1111/j.1365-2958.1995.mmi_18020343.x
  6. Andrews G.P., Infect Immun, 59, 1997 (1991)
  7. Arlat M., EMBO J, 13, 543 (1994)
  8. Bawe S.S., J Bacteriol, 712, 4661 (1990)
  9. Bergman T., J Bacteriol, 173, 1607 (1991)
  10. Bergman T., J Bacteriol, 176, 2619 (1994)
  11. Carpenter Phillip B., Zuberi Aamir R., Ordal George W., Bacillus subtilis flagellar proteins FliP, FliQ, FliR and FlhB are related to Shigella flexneri virulence factors, 10.1016/0378-1119(93)90014-t
  12. Cock H., Mol Microbiol, 6, 599 (1992)
  13. Dayhoff Margaret O., Barker Winona C., Hunt Lois T., [47] Establishing homologies in protein sequences, Enzyme Structure Part I (1983) ISBN:9780121819910 p.524-545, 10.1016/s0076-6879(83)91049-2
  14. Fath M.J., Microbiol Rev, 57, 995 (1993)
  15. Fields K.A., J Bacteriol, 176, 569 (1994)
  16. Forsberg A., J Bacteriol, 172, 1547 (1990)
  17. Frank D.W., J Bacteriol, 173, 6460 (1991)
  18. Frithz-Lindsten E., Mol Microbiol, 16, 635 (1995)
  19. Galyov Edouard E., Håkansson Sebastian, Forsberg Åke, Wolf-Watz Hans, A secreted protein kinase of Yersinia pseudotuberculosis is an indispensable virulence determinant, 10.1038/361730a0
  20. Ginocchio C., Infect Immun, 63, 729 (1995)
  21. Gomez-Duarte O.G., Infect Immun, 63, 1767 (1995)
  22. Guan K., Science, 249, 553 (1990)
  23. Hakansson S., Infect Immun, 61, 71 (1993)
  24. Hartl Franz-Ulrich, Lecker Stewart, Schiebel Elmar, Hendrick Joseph P., Wickner William, The binding cascade of SecB to SecA to SecYE mediates preprotein targeting to the E. coli plasma membrane, 10.1016/0092-8674(90)90160-g
  25. He Sheng Yang, Huang Hsiou-Chen, Collmer Alan, Pseudomonas syringae pv. syringae harpinPss: A protein that is secreted via the hrp pathway and elicits the hypersensitive response in plants, 10.1016/0092-8674(93)90354-s
  26. Hermant Daniel, Menard Robert, Arricau Nathalie, Parsot Claude, Popoff Michel Y., Functional conservation of the Salmonella and Shigella effectors of entry into epithelial cells, 10.1111/j.1365-2958.1995.mmi_17040781.x
  27. Hobson A. H., Buckley C. M., Aamand J. L., Jorgensen S. T., Diderichsen B., McConnell D. J., Activation of a bacterial lipase by its chaperone., 10.1073/pnas.90.12.5682
  28. Hultgren S., Chaperone-Assisted Assembly And Molecular Architecture Of Adhesive Pili, 10.1146/annurev.micro.45.1.383
  29. Jarvis K. G., Giron J. A., Jerse A. E., McDaniel T. K., Donnenberg M. S., Kaper J. B., Enteropathogenic Escherichia coli contains a putative type III secretion system necessary for the export of proteins involved in attaching and effacing lesion formation., 10.1073/pnas.92.17.7996
  30. Jerse A. E., Yu J., Tall B. D., Kaper J. B., A genetic locus of enteropathogenic Escherichia coli necessary for the production of attaching and effacing lesions on tissue culture cells., 10.1073/pnas.87.20.7839
  31. Kaniga K., J Bacteriol, 177, 3965 (1995)
  32. Kok R.G., J Bacteriol, 177, 3295 (1995)
  33. Kuehn M. J., Normark S., Hultgren S. J., Immunoglobulin-like PapD chaperone caps and uncaps interactive surfaces of nascently translocated pilus subunits., 10.1073/pnas.88.23.10586
  34. Kulich S.M., J Biol Chem, 269, 10431 (1994)
  35. Kumamoto C.A., Mol Microbiol, 5, 19 (1991)
  36. Lupas A., Science, 252, 1162 (1991)
  37. Ménard Robert, Sansonetti Philippe, Parsot Claude, Vasselon Thierry, Extracellular association and cytoplasmic partitioning of the IpaB and IpaC invasins of S. flexneri, 10.1016/0092-8674(94)90260-7
  38. Michiels T., J Bacteriol, 173, 1677 (1991)
  39. Michiels T., Infect Immun, 58, 2840 (1990)
  40. Michiels T., J Bacteriol, 173, 4994 (1991)
  41. Plano G.V., J Bacteriol, 175, 3536 (1993)
  42. Price S.B., Infect Immun, 57, 1491 (1989)
  43. Price S.B., J Bacteriol, 171, 5646 (1989)
  44. Pugsley A.P., Microbiol Rev, 57, 50 (1993)
  45. Rimpilainen M., J Bacteriol, 174, 3355 (1992)
  46. Rosqvist R., Infect Immun, 59, 4562 (1991)
  47. Rosqvist R., EMBO J, 13, 964 (1994)
  48. Rosqvist R., EMBO J, 14, 4187 (1995)
  49. Russel M., Science, 265, 612 (1994)
  50. Salmond George P.C., Reeves Philip J., Membrance traffic wardens and protein secretion in Gram-negative bacteria, 10.1016/0968-0004(93)90080-7
  51. Sasakawa C., Mol Microbiol, 3, 1191 (1989)
  52. Sory M.-P., Mol Microbiol, 14, 583 (1994)
  53. Sory M. P., Boland A., Lambermont I., Cornelis G. R., Identification of the YopE and YopH domains required for secretion and internalization into the cytosol of macrophages, using the cyaA gene fusion approach., 10.1073/pnas.92.26.11998
  54. Gijsegem F., Mol Microbiol, 15, 1095 (1995)
  55. Wattiau P., Mol Microbiol, 8, 123 (1993)
  56. Wattiau P., Bernier B., Deslee P., Michiels T., Cornelis G. R., Individual chaperones required for Yop secretion by Yersinia., 10.1073/pnas.91.22.10493
  57. Woestyn S., J Bacteriol, 176, 1561 (1994)
  58. Yahr T.L., J Bacteriol, 176, 3832 (1994)
  59. Yahr T.L., J Bacteriol, 177, 1169 (1995)
Bibliographic reference Wattiau, Pierre ; WOESTYN, SOPHIE ; Cornelis, Guy R.. Customized secretion chaperones in pathogenic bacteria.. In: Molecular microbiology, Vol. 20, no. 2, p. 255-62 (1996)
Permanent URL http://hdl.handle.net/2078.1/29369