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Chapter 24 : Yops of the Pathogenic Yersinia spp.

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Abstract:

During their interaction with host cells, the pathogenic spp. export a set of proteins known as the outer membrane proteins, or Yops. This chapter reviews the work that led to the discovery of the Yops and discusses recent progress made in understanding the expression and function of these proteins. Bacterial infection of the lungs results in pneumonic plague, a form of the disease that is transmissible by aerosolization and that is often fatal. is responsible for a variety of human illnesses ranging in severity from mild gastroenteritis to acute terminal ileitis. Various rodents, farm animals, and birds are the normal reservoirs for . The product of shares significant homology with PulD, a protein required for the export of pullulanase by . A number of additional polypeptides (later to be identified as the Yops) were detected in sucrose gradient-purified outer membranes from pYV-containing and grown under LCR conditions. The ability of strains to induce rounding and detachment of cultured mammalian cells has been referred to as "cytotoxicity". A partial cytotoxic activity is reconstituted if these protein preparations are introduced into HeLa cells by the use of glass carrier beads. This indicates that YopE must enter the cytoplasm of the host cell to be active. Signal transduction is critically involved in a number of cellular host responses to microbial infection.

Citation: Bliska J. 1994. Yops of the Pathogenic Yersinia spp., p 365-381. In Miller V, Kaper J, Portnoy D, Isberg R (ed), Molecular Genetics of Bacterial Pathogenesis. ASM Press, Washington, DC. doi: 10.1128/9781555818340.ch24

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Outer Membrane Proteins
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Peyer's Patches
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Sodium Dodecyl Sulfate
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Scanning Electron Microscopy
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Cell-Mediated Immune Response
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Scanning Electron Microscopy
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Figures

Image of Figure 1
Figure 1

SDS-PAGE analysis of outer membrane polypeptides. Lane A, strain 9576 grown at 25°C; lane B, strain 9576-c grown at 25°C; lane C, strain 9576 grown at 37°C; lane D, strain 9576-c grown at 37°C. From Portnoy et al. ( ).

Citation: Bliska J. 1994. Yops of the Pathogenic Yersinia spp., p 365-381. In Miller V, Kaper J, Portnoy D, Isberg R (ed), Molecular Genetics of Bacterial Pathogenesis. ASM Press, Washington, DC. doi: 10.1128/9781555818340.ch24
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Image of Figure 2
Figure 2

strains harboring the virulence plasmid and pregrown at 28°C are localized intracellular in HEp-2 cells. Bacterial strains were grown at 28°C in L broth overnight and were added to monolayers of HEp-2 cells at 37°C. After 2 h for binding and entry, unbound bacteria were washed away and the monolayers were fixed, embedded, and sectioned for electron microscopy. (A and B) Virulence plasmid-cured (C and D) Virulence plasmid-containing From Isberg ( ).

Citation: Bliska J. 1994. Yops of the Pathogenic Yersinia spp., p 365-381. In Miller V, Kaper J, Portnoy D, Isberg R (ed), Molecular Genetics of Bacterial Pathogenesis. ASM Press, Washington, DC. doi: 10.1128/9781555818340.ch24
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Image of Figure 3
Figure 3

strains harboring the virulence plasmid and pregrown at 37°C do not enter HEp-2 cells. was grown overnight in L broth at 28°C. Freshly saturated cultures were diluted in the same medium and were aerated at 37°C for 3 h at this temperature before addition to monolayers of HEp-2 cells. After 2 h for binding and intracellular entry of the bacteria, the monolayers were washed and processed for thin-section electron microscopy. Displayed are two micrographs of infected in this fashion. From Isberg ( ).

Citation: Bliska J. 1994. Yops of the Pathogenic Yersinia spp., p 365-381. In Miller V, Kaper J, Portnoy D, Isberg R (ed), Molecular Genetics of Bacterial Pathogenesis. ASM Press, Washington, DC. doi: 10.1128/9781555818340.ch24
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Figure 4

SDS-PAGE analysis of proteins released by mutants. strains were grown at 37°C in a defined low-Ca medium ( ). Proteins were isolated from the growth medium by precipitation with trichloroacetic acid and were analyzed by electrophoresis on an SDS-polyacrylamide gel (12%). The strains used are described in Bliska et al. ( ). Lane 1, plasmid-cured lane 2, wild-type lane 3, catalytic YopH mutant lane 4, YopH deletion mutant Δ The positions of the molecular size markers (in kilodaltons) and YopH are indicated on the right.

Citation: Bliska J. 1994. Yops of the Pathogenic Yersinia spp., p 365-381. In Miller V, Kaper J, Portnoy D, Isberg R (ed), Molecular Genetics of Bacterial Pathogenesis. ASM Press, Washington, DC. doi: 10.1128/9781555818340.ch24
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Figure 5

Structure of YopH. At the top is shown a restriction map of and a corresponding scale in kilobases. At the bottom is shown a functional map of YopH with a scale corresponding to length in amino acids. The domains involved in various functions of the protein are indicated. Sec, N-terminal 48 residues sufficient for export ( ); YscM, region of YopH that is homologous to YscM (LcrQ) and that corresponds to the first 128 amino acids and overlaps the export domain ( ): SRD; substrate recognition domain (residues 129 to 261), a region of the protein involved in phosphoprotein-binding activity ( ); PTPase, domain of YopH that is homologous to eukaryotic protein tyrosine phosphatase catalytic domains ( ).

Citation: Bliska J. 1994. Yops of the Pathogenic Yersinia spp., p 365-381. In Miller V, Kaper J, Portnoy D, Isberg R (ed), Molecular Genetics of Bacterial Pathogenesis. ASM Press, Washington, DC. doi: 10.1128/9781555818340.ch24
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References

/content/book/10.1128/9781555818340.chap24
1. Ben Gurion, R.,, and A. Shafferman. 1981. Essential virulence determinants of different Yersinia species are carried on a common plasmid. Plasmid 5:183187.
2. Bliska, J. B. Unpublished data.
3. Bliska, J. B.,, M. C. Copass,, and S. Falkow. 1993. The Yersinia pseudotuberculosis adhesin YadA mediates intimate bacterial attachment to and entry into HEp-2 cells. Infect. Immun. 61:39143921.
4. Bliska, J. B.,, J. C. Clemens,, J. E. Dixon,, and S. Falkow. 1992. The Yersinia tyrosine phosphatase: specificity of a bacterial virulence determinant for phosphoproteins in the J774A. 1 macrophage. J. Exp. Med. 176:16251630.
5. Bliska, J. B.,, J. E. Galan,, and S. Falkow. 1993. Signal transduction in the mammalian cell during bacterial attachment and entry. Cell 73:903920.
6. Bliska, J. B.,, K. Guan,, J. E. Dixon,, and S. Falkow. 1991. Tyrosine phosphate hydrolysis of host proteins by an essential Yersinia virulence determinant. Proc. Natl. Acad. Sci. USA 88:11871191.
7. Bolin, I.,, A. Forsberg,, L. Norlander,, M. Skurnik,, and H. Wolf-Watz. 1988. Identification and mapping of the temperature-inducible, plasmid-encoded proteins of Yersinia spp. Infect. Immun. 56:343348.
8. Bolin, I.,, D. A. Portnoy,, and H. Wolf-Watz. 1985. Expression of the temperature-inducible outer membrane proteins of yersiniae. Infect. Immun. 48:234240.
9. Bolin, I.,, and H. Wolf-Watz. 1988. The plasmid-encoded Yop2b protein of Yersinia pseudotuberculosis is a virulence determinant regulated by calcium and temperature at the level of transcription. Mol. Microbiol. 2:237245.
10. Brubaker, R. R. 1991. Factors promoting acute and chronic diseases caused by yersiniae. Clin. Microbiol. Rev. 4:309324.
11. Burrows, T. W.,, and G. A. Bacon. 1956. The basis of virulence in Pasteurella pestis: an antigen determining virulence. Br. J. Exp. Pathol. 37:481493.
12. Cornells, G.,, Y. Laroche,, G. Balligand,, M. P. Sory,, and G. Wauters. 1987. Yersinia enterocolitica, a primary model for bacterial invasiveness. Rev. Infect. Dis. 9:6487.
13. Cornells, G. R.,, T. Blot,, C. Lambert de Rouvroit,, T. Michlels,, B. Mulder,, C. Sluiters,, M.-P. Sory,, M. Van Bouchaute,, and J.-C. Vanooteghem. 1989. The Yersinia yop regulon. Mol. Microbiol. 3: 14551459.
14. Delor, I.,, and G. R. Cornells. 1992. Role of Yersinia enterocolitica Yst toxin in experimental infection of young rabbits. Infect. Immun. 60:42694277.
15. Eichelberg, K.,, C. C. Ginochio,, and J. E. Galan. Molecular and functional characterization of the Salmonella typhimurium invasion genes invB and invC: homology of InvC to the F0F1 ATPase family of proteins. J. Bacteriol., in press.
16. Fischer, E. H.,, H. Charbonneau,, and N. Tonks. 1991. Protein tyrosine phosphatases: a diverse family of intracellular and transmembrane enzymes. Science 253:401406.
17. Forsberg, A.,, I. Bolin,, L. Norlander,, and H. Wolf-Watz. 1987. Molecular cloning and expression of calcium-regulated, plasmid-encoded proteins of Yersinia pseudotuberculosis. Microb. Pathog. 2:123137.
18. Forsberg, A.,, and H. Wolf-Watz. 1988. The virulence protein Yop5 of Yersinia pseudotuberculosis is regulated at transcriptional level by plasmid-p1B1-encoded trans-acting elements controlled by temperature and calcium. Mol. Microbiol. 2:121133.
19. 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 (London) 364:639642.
20. Fujimura, Y.,, T. Kihara,, and H. Mine. 1992. Membranous cells as a portal of Yersinia pseudotuberculosis entry into rabbit ileum. J. Clin. Electron Microsc. 25:3545.
21. Galan, J. E.,, and C. C. Ginocchio. The molecular genetic basis of Salmonella entry into mammalian cells. Biochem. Trans., in press.
22. Galyov, E. E.,, S. Hakansson,, A. Forsberg,, and H. Wolf-Watz. 1993. A secreted protein kinase of Yersinia pseudotuberculosis is an indispensable virulence determinant. Nature (London) 361: 730732.
23. Gemski, P.,, J. R. Lazere,, T. Casey,, and J. A. Wohlhieter. 1980. Presence of a virulence-associated plasmid in Yersinia pseudotuberculosis. Infect. Immun. 28:10441047.
24. Ginocchio, C. C.,, S. B. Olmsted,, C. L. Wells,, and J. E. Galan. 1994. Contact with epithelial cells induces the formation of surface appendages on Salmonella typhimurium. Cell 76:717724.
25. Goguen, J. D.,, W. S. Walker,, T. P. Hatch,, and J. Yother. 1986. Plasmid-determined cytotoxicity in Yersinia pestis and Yersinia pseudotuberculosis. Infect. Immun. 51:788794.
26. Guan, K.,, and J. E. Dixon. 1990. Protein tyrosine phosphatase activity of an essential virulence determinant in Yersinia. Science 249:553556.
27. Hakansson, S.,, T. Bergman,, J. Vanooteghem,, G. Cornells,, and H. Wolf-Watz. 1993. YopB and YopD constitute a novel class of Yersinia Yop proteins. Infect. Immun. 61:7180.
28. Hanski, C.,, U. Kutschka,, H. P. Schmoranzer,, M. Naumann,, A. Stallmach,, H. Hahn,, and H. Menge. 1989. Immunohistochemical and electron microscopic study of interaction of Yersinia enterocolitica serotype 08 with intestinal mucosa during experimental enteritis. Infect. Immun. 57:673678.
29. Heesemann, J.,, B. Algermissen,, and R. Laufs. 1986. Immunochemical analysis of plasmid-encoded proteins released by enteropathogenic Yersinia sp. grown in calcium-deficient media. Infect. Immun. 54:561567.
30. Heesemann, J.,, B. Algermissen,, and R. Laufs. 1984. Genetically manipulated virulence of Yersinia enterocolitica. Infect. Immun. 46:105110.
31. Heesemann, J.,, and R. Laufs. 1985. Double immunofluorescence microscopic technique for accurate differentiation of extracellularly and intracellularly located bacteria in cell culture. J. Clin. Microbiol. 22:168175.
32. Hunter, T. 1989. Protein modification: phosphorylation on tyrosine residues. Curr. Opin. Cell Biol. 1:11681181.
33. Isberg, R. R. 1989. Determinants for thermoinducible cell binding and plasmid-encoded cellular entry detected in the absence of the Yersinia pseudotuberculosis invasin protein. Infect. Immun. 57:19982005.
34. Isberg, R. R. 1991. Discrimination between intracellular uptake and surface adhesion of bacterial pathogens. Science 252:934938.
35. Juliano, R. J.,, and S. Haskill. 1993. Signal transduction from the extracellular matrix. J. Cell Biol. 120:577585.
36. Lambert de Rouvroit, C.,, C. Sluiters,, and G. R. Cornells. 1992. Role of the transcriptional activator, VirF, and temperature in the expression of the pYV plasmid genes of Yersinia enterocolitica. Mol. Microbiol. 6:395409.
37. Leung, K. Y.,, B. S. Reisner,, and S. C. Straley. 1990. YopM inhibits platelet aggregation and is necessary for virulence of Yersinia pestis in mice. Infect. Immun. 58:32623271.
38. Leung, K. Y.,, and S. C. Straley. 1989. The yopM gene of Yersinia pestis encodes a released protein having homology with the human platelet surface protein GPIba. J. Bacteriol. 171:46234632.
39. McDonough, K. A.,, A. M. Barnes,, T. J. Quan,, J. Montenieri,, and S. Falkow. 1993. Mutation in the pla gene of Yersinia pestis alters the course of the plague bacillus-flea (Siphonaptera: Cerato-phyllidae) interaction. J. Med. Entomol. 30:772780.
40. Michiels, T.,, and G. Cornells. 1988. Nucleotide sequence and transcription analysis of yop51 from Yersinia enterocolitica W22703. Microb. Pathog. 5:449459.
41. Michiels, T.,, and G. R. Cornells. 1991. Secretion of hybrid proteins by the Yersinia Yop export system. J. Bacteriol. 173:16771685.
42. Michiels, T.,, J.-C. Vanooteghem,, C. Lambert de Rouvoit,, B. China,, A. Gustin,, P. Boudry,, and G. R. Cornells. 1991. Analysis of virC, an operon involved in the secretion of Yop proteins by Yersinia enterocolitica. J. Bacteriol. 173:49945009.
43. Michiels, T.,, P. Wattiau,, R. Brasseur,, J.-C. Ruysschaert,, and G. Cornells. 1990. Secretion of Yop proteins by yersiniae. Infect. Immun. 58:28402849.
44. Pace, J.,, M. J. Hayman,, and J. E. Galan. 1993. Signal transduction and invasion of epithelial cells by Salmonella typhimurium. Cell 72:505514.
45. Portnoy, D.,, S. L. Moseley,, and S. Falkow. 1981. Characterization of plasmids and plasmid-associated determinants of Yersinia enterocolitica pathogenesis. Infect. Immun. 31:775782.
46. Portnoy, D. A.,, and S. Falkow. 1981. Virulence-associated plasmids from Yersinia enterocolitica and Yersinia pestis. J. Bacteriol. 148:877883.
47. Portnoy, D. A.,, and R. J. Martinez. 1985. Role of a plasmid in the pathogenicity of Yersinia species. Curr. Top. Microbiol. Immunol. 118:2951.
48. Portnoy, D. A.,, H. Wolf-Watz,, I. Bolin,, A. B. Beeder,, and S. Falkow. 1984. Characterization of common virulence plasmids in Yersinia species and their role in the expression of outer membrane proteins. Infect. Immun. 43:108114.
49. Price, S. B.,, K. Y. Leung,, S. S. Barve,, and S. C. Straley. 1989. Molecular analysis of lcrGVH, the V antigen operon of Yersinia pestis. J. Bacteriol. 171:56465653.
50. Protsenko, O. A.,, P. I. Anisimov,, O. T. Mosarov,, N. P. Donnov,, Y. A. Popov,, and A. M. Kokushkin. 1983. Detection and characterization of Yersinia pestis plasmids determining pesticin 1, fraction 1 antigen and mouse toxin synthesis. Genetika 19:10811090.
51. Reisner, B. S.,, and S. C. Straley. 1992. Yersinia pestis YopM: thrombin binding and overexpression. Infect. Immun. 60:52425252.
52. Rimpilainen, M.,, A. Forsberg,, and W. H. Wolf. 1992. A novel protein, LcrQ, involved in the low-calcium response of Yersinia pseudotuberculosis shows extensive homology to YopH. Infect. Immun. 174:33553363.
53. Rosqvist, R.,, I. Bolin,, and H. Wolf-Watz. 1988. Inhibition of phagocytosis in Yersinia pseudotuberculosis: a virulence plasmid-encoded ability involving the Yop2b protein. Infect. Immun. 56: 21392143.
54. Rosqvist, R.,, A. Forsberg,, M. Rimpilainen,, T. Bergman,, and H. Wolf-Watz. 1990. The cytotoxic protein YopE of Yersinia obstructs the primary host defence. Mol. Microbiol. 4:657667.
55. Rosqvist, R.,, A. Forsberg,, and W. H. Wolf. 1992. Intracellular targeting of the Yersinia YopE cytotoxin in mammalian cells induces actin microfilament disruption. Infect. Immun. 59: 45624569.
56. Rosqvist, R.,, M. Skurnik,, and H. Wolf-Watz. 1988. Increased virulence of Yersinia pseudotuberculosis by two independent mutations. Nature (London) 334:522524.
57. Sample, A. K.,, J. M. Fowler,, and R. R. Brubaker. 1987. Modulation of the low calcium response in Yersinia pestis via plasmid-plasmid interaction. Microb. Pathog. 2:443453.
58. Skurnik, M.,, and H. Wolf-Watz. 1989. Analysis of the yopA gene encoding the Yopl virulence determinants of Yersinia spp. Mol. Microbiol. 3:517529.
59. Sodeinde, O. A.,, A. Sample,, R. R. Brubaker,, and J. D. Goguen. 1988. Plasminogen activator/ coagulase gene in Yersinia pestis is responsible for degradation of plasmid-encoded outer membrane proteins. Infect. Immun. 56:27492752.
60. Sodeinde, O. A.,, Y. V. Subrahmanyam,, K. Stark,, T. Quan,, Y. Bao,, and J. D. Goguen. 1993. A surface protease and the invasive character of plague. Science 258:10041007.
61. Straley, S. C.,, and W. S. Bowmer. 1986. Virulence genes regulated at the transcriptional level by Ca2+ in Yersinia pestis include structural genes for outer-membrane proteins. Infect. Immun. 51: 445454.
62. Straley, S. C.,, and R. R. Brubaker. 1981. Cytoplasmic and membrane proteins of yersiniae cultivated under conditions simulating mammalian intracellular environment. Proc. Natl. Acad. Sci. USA 78:12241228.
63. Straley, S. C.,, G. V. Piano,, E. Skrzypek,, and J. B. Bliska. 1993. Yops of Yersinia spp. pathogenic for humans. Infect. Immun. 61:31053110.
64. Straley, S. C.,, G. V. Piano,, E. Skrzypek,, P. L. Haddix,, and K. A. Fields. 1993. Regulation by Ca2+ in the Yersinia low-Ca2+ response. Mol. Microbiol. 8:10051010.
65. Viitanen, A.-M.,, P. Toivanen, and M. Skurnik. 1990. The lcrE gene is part of an operon in the lcr region of Yersinia enterocolitica O:3. J. Bacteriol. 172:31523162.
66. Wattiau, P.,, and G. R. Cornells. 1993. SycE, a chaperone-like protein of yersinia enterocolitica involved in the secretion of YopE. Mol. Microbiol. 8:123131.
67. Wolf-Watz, H.,, D. A. Portnoy,, I. Bolin,, and S. Falkow. 1985. Transfer of the virulence plasmid of Yersinia pestis to Yersinia pseudotuberculosis. Infect. Immun. 48:241243.
68. Yang, Y.,, and R. Isberg. 1993. Cellular internalization in the absence of invasin expression is promoted by the Yersinia pseudotuberculosis yadA product. Infect. Immun. 61:39073913.
69. Zhang, Z. Y.,, J. C. Clemens,, H. L. Schubert,, J. A. Stuckey,, M. W. F. Fischer,, D. M. Hume,, M. A. Saper,, and J. E. Dixon. 1992. Expression, purification and physiochemical characterization of a recombinant Yersinia tyrosine phosphatase. J. Biol. Chem. 267:2375923766.
70. Zink, D. L.,, J. C. Feeley,, J. G. Wells,, C. Vanderzant,, J. C. Vickery,, W. D. Roof,, and G. A. O'Donovan. 1980. Plasmid-mediated tissue invasiveness in Yersinia enterocolitica. Nature (London) 283:224226.

Tables

Generic image for table
Table 1

Yops and other pYV-encoded proteins released by yersiniae

The names and apparent molecular masses of the proteins released from spp. are given. Molecular masses are from Michiels et al. ( ).

Number of amino acids in each protein as predicted from the gene sequence. Values are for proteins encoded by Y. unless indicated otherwise by the abbreviations in parentheses: Ype, Ye,

ND, not determined.

Citation: Bliska J. 1994. Yops of the Pathogenic Yersinia spp., p 365-381. In Miller V, Kaper J, Portnoy D, Isberg R (ed), Molecular Genetics of Bacterial Pathogenesis. ASM Press, Washington, DC. doi: 10.1128/9781555818340.ch24

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