Молекулярные аспекты вирулентности иерсиний | КМАХ

Молекулярные аспекты вирулентности иерсиний

Клиническая Микробиология и Антимикробная Химиотерапия. 2002; 4(3):248-266

​ Ценева Г.Я., Солодовникова Н.Ю., Воскресенская Е.А.
иерсинии патогенность биологические функции генетический контроль
Раздел
Болезни и возбудители
Тип
Журнальная статья
Публикация
Клиническая Микробиология и Антимикробная Химиотерапия. 2002; 4(3):248-266

Аннотация

Проанализирована и обобщена информация отечественных и зарубежных исследователей о патогенных свойствах иерсиний, особенностях молекулярно.генетических механизмов, регулирующих экспрессию факторов патогенности. Представлены данные о роли различных внешних факторов в регуляции генов вирулентности. Определены дальнейшие перспективы изучения механизмов взаимодействия иерсиний в системе «паразит – хозяин» и генетического контроля их патогенности.

  • 1. Определитель бактерий Берджи. Пер с англ. Г.А. Заварзина. Под ред. Дж. Хоулта, H. Крига, П. Снита, Дж. Стейли, С. Уилльямса. В 2 т. Mосква: Мир; 1997.
  • 2. Skurnik M., Peippo A., Ervela E. Characterization of the O-antigen gene clusters of Yersinia pseudotuberculosis and the cryptic O-antigen gene claster of Yersinia pestis shows that the plague bacillus is most closely related to and has evolved from Y. pseudotuberculosis serotype O:1b. Mol Microbiol 2000; 37:316-30.
  • 3. Kapatral V., Olson J.W., Pepe J.C., Miller V.L., Minnich S.A. Temperature-dependent regulation of Yersinia enterocolitica Class III flagellar genes. Mol Microbiol 1996;19:1061-71.
  • 4. Bottone E.J. Yersinia enterocolitica: overview and epidemiologic correlates. Microb Infect 1999; 1:323-33.
  • 5. Andersson К., Magnusson K.-E., Majeed M., Stenghal 0., Fallman M. Yersinia pseudotuberculosis-induced calcium signaling in neutrophils is blocked by the virulence effector YopH. Infect Immun 1999; 67:2567-74.
  • 6. A new pathway for the secretion of virulence factors by bacteria: the flagellar export apparatus functions as a protein-secretion system. Proc Natl Acad Sci USA 1999; 96:6456-61.
  • 7. Heesemann J., Keller С., Morawa R., Schmidt N., Seimens H.J., Laufs R. Plasmid of human strains of Yersinia enterocolitica: molecular relatedness and possible importance. J Infect Dis 1983; 147:107-15.
  • 8. Lian C.J., Hwang W.S., Kelly J.K., Pai C.H. Invasiveness of Yersinia enterocolitica lacking the virulence plasmid: an in vivo study. J Med Microbiol 1987; 24:219-26.
  • 9. Lian C.J., Pai C.H. Inhibition of human neutrophil hemoluminescence by plasmid-mediated outer membrane proteins of Yersinia enterocolitica. Infect Immun 1985; 49:145-51.
  • 10. Forsberg A., Rosqvist R. In vivo expression of virulence genes of Yersinia pseudotuberculosis. Infect Agents Dis 1993; 2:275-78.
  • 11. Ценева Г.Я. Варианты проявления основных патогенных свойств иерсиний в эксперименте и их сопоставление с изменениями у больных. Материалы международной конференции «Инфекции, обусловленные иерсиниями (иерсиниоз, псевдотуберкулез), и другие актуальные инфекции». Санкт-Петербургский НИИЭМ им. Пастера; 2000. с. 66.
  • 12. Kapperud G., Namork E., Skarpeid H.-J. Temperatureinducible surface-fibrillae associated with the virulence plasmid of Yersinia enterocolitica and Yersinia pseudotuberculosis. Infect Immun 1985; 47:561-6.
  • 13. Isberg R.R., Falkow S. A single genetic locus encoded by Yersinia pseudotuberculosis permit invasion of cultured animal cells by Escherihia coli K-12. Nature 1985; 317:262-4.
  • 14. Kapperud G., Namork E., Skurnik M., Nesbakken T. Plasmid-mediate surface fibrillae of Yersinia pseudotuberculosis and Yersinia enterocolitica: relationship to the outer mebrane protein YOP1 and possible importance for pathogenesis. Infect Immun 1987; 55:2247-2254.
  • 15. Yang Y., Isberg R.R. Transcriptional regulation of the Yersinia pseudotuberculosis pH6 antigen adhesin by two envelope-assotiated components. Mol Microbiol 1997; 24:499-510.
  • 16. Isberg R.R., Voorhis D., Falkow S. Identification of invasin: a protein that allows enteric bacteria to penetrate cultured mammalian cells. Cel 1987; 50:769-78.
  • 17. Straley S.C., Skrzypek E., Piano G.V., Bliska J.B. Yops of Yersinia spp. pathogenic for humans. Infect Immun 1993; 61:3105-10.
  • 18. Arencibia I., Suatez N.C., Wolf-Watz H., Sundqvist K.G. Yersinia invasin, a bacterial beta-1-integrin ligand, is potent inducer of lymphocyte motility and migration tio collagen type IV and fibronectin. J Immunol 1997; 159:1853-9.
  • 19. Young V.B., Miller V.L., Falkow S., Schoolnik G.K. Sequence, localization and function of the invasin protein of Yersinia enterocolitica. Mol Microbiol 1990; 4:1119-28.
  • 20. Miller V.L., Falkow S. Evidens for two genetic loci from Yersinia enterocolitica that can promote invasion of epithelian cells. Infect Immun 1988; 56:1242-8.
  • 21. Fortineau N., Beretti J.L., Berche P., Simonet M. Lack of antibody response to invasin in humans with yersiniosis. Clin Diagnostic Lab Immunol 1994; 1:235-7.
  • 22. Тимченко Н.Ф., Венедиктов B.C., Павлова Т.Н. Моделирование инициации псевдотуберкулезной инфекции. Журн микробиол 1988; 7:16-20.
  • 23. Pederson K.J., Carlson S., Pierson D.E. The ClpP protein, a subunit of the Clp protease, modulating ail gene expression in Yersinia enterocolitica. Mol Microbiol 1997; 26:99-107.
  • 24. Pierson D.E., Falkow S. The ail gene of Yersinia enterocolitica has a role in the ability of the organism to survive serum killing. Infect Immun 1993; 61:1846-52.
  • 25. Pierson D.E. Mutations affecting lipopolysaccharide enhance ail-mediated entry of Yersinia enterocolitica into mammalian cells. J Bacteriol 1994; 176:4043-51.
  • 26. Goverde R.L., Jansen W.H., Brunings H.A., Huis-in-'tVeld J.H., Mooi F.R. Digoxigenen-labeled invand ailprobes for the detection and identification of pathogenic Yersinia enterocolitica in clinical specimens and naturally contaminated pig samples. J Appl Bacteriol 1993; 74:301-13.
  • 27. Yang Y., Merriam J.J., Mueller J.P., Isberg R.R. The psa locus is responsible for thermoinducible binding of Yersinia pseudotuberculosis to cultured cells. Infect Immun 1996; 64:2483-9.
  • 28. Cornelis G.R, Boland A., Boyd A.P., et al. The virulence plasmid of Yersinia, an antihost genom. Microbiol Mol Biol Rev 1998; 62:1315-52.
  • 29. Iriarte M., Stainier I., Cornelis G.R. The rpoS gene from Yersinia enterocolitica and its influence on expression of virulence factors. Infect Immun 1995; 63:1840-7.
  • 30. Iriarte M., Vanooteghem J.C., Delor I., Diaz R., Knutton S., Cornellis G.R. The Myf fibrillae of Yersinia enterocolitica. Mol Microbiol 1993; 9:507-20.
  • 31. Sansonetti P.J., Phalipon A. M cells as ports of entry for enteroinvasive pathogens: mechanisms of interaction, consequences for the disease process. Semin Immunol 1999; 11:193-203.
  • 32. Clark M.A., Hirst B.H., Jepson M.A. M-cell surface beta 1 intergrin expression and invasin-mediated targeting of Yersinia pseudotuberculosis to mouse Peyer's patch cells. Infect Imumun 1998; 66:1237-43.
  • 33. Kwaga J., Iversen J.O. Plasmid and outer membrane proteins of Yersinia enterocolitica and related species of swin origin. Vet Microbiol 1993; 36:205-14.
  • 34. China В., Michiels T., Cornelis G.R. The pYV plasmid of Yersinia encodes a lipoprotein YlpA, related to TraT. Mol Microbiol 1990; 4:1585-93.
  • 35. Heesemann J. Enteropathogenic yersinias: pathogenicity factors and new diagnostic methods [Germany]. Immun Infect 1990; 18:186-91.
  • 36. Pettersson J., Holmstrom A., Hill J., et al. The V-antigen of Yersinia is surface exposed before target сеll contact and involved in virulence protein translocation. Mol Microbiol 1999; 32:961-76.
  • 37. Bergman Т., Hakansson S., Forsberg A., et al. Analysis of the V-antigen IcrGVH-yopBD operon of Yersinia psendotuberculosis: evidence for a regulatory role of LcrH and LcrV. J Bacteriol 1991; 173:1607-16.
  • 38. Mulder В., Michiels Т., Simonet M., Sory M.-P., Cornelis G. Identification of additional virulence determinants on the plasmid of Yersinia enterocolitica W227. Infect Immun 1989; 57:2534-41.
  • 39. Forsberg A., Viitanen A.-M., Skurnik M., Wolf-Watz H. The surface-located YopN protein is involved in calcium signal transduction in Yersinia pseudotuberculosis. Mol Microbiol 1991; 5:977-86.
  • 40. Michiels Т., Vanooteghem J.-C., Lambert de Rouvroit C., et al. Analysis of virC, an operon involved in the secretion of Yop proteins by Yersinia enterocolitica. J Bacteriol 1991; 173:4994-5009.
  • 41. Cornelis G.R. Role of the transcription activator virF and the histone-like protein YmoA in the thermoregulation of virulence functions in Yersiniae. Int J Med Microbiol Virol Parasitol Infect Dis 1993; 278:149-64.
  • 42. Skurnik M., Toivanen P. LcrF iz the temperature-regulated activator of the yadA gene of Yersinia enterocolitica and Yersinia pseudotuberculosis. J Bacteriol 1992; 174:2047-51.
  • 43. Gripenberg-Lerche C., Skurnik M., Toivanen P. Role of YadA-mediated collagen binding in arthritogenicity of Yersinia enterocolitica serotype O:8: experimental studies with rats. Infect Immun 1995; 63:3222-6.
  • 44. Flugel A., Schulze-Koops H., Heesemann J., et al. Interaction of enteropathogenic Yersinia enterocolitica with complex basement membranes and the extracellular matrix proteins collagen type IV, laminin-1 and -2, and nidogen/entacin. J Biol Chem 1994; 269:29732-8.
  • 45. Schulz-Koops H., Burkhardt H., Heesemann J., et al. Outer membrane protein YadA of enteropathogenic yersiniae mediates specific binding to cellular but not plasma fibronecti. Infect Immun 1993; 61:2513-9.
  • 46. Paerregaard A., Espersen F., Jensen O.M., Skurnik M. Interactions between Yersinia enterocolitica and rabbit iteal mucus: growth, adhesion, penetration and subsequent changes in surface hydrophobicity and ability to adhere to iteal brush border membrane vesicles. Infect Immun 1991; 59:253-260.
  • 47. Paerregaard A., Espersen F., Skurnik M. Role of the Yersinia outer membrane protein YadA in adhesion to rabbit intestinal tissue and rabbit intestinal brush border membrane vesicles. APMIS 1991; 99:226-32.
  • 48. Bliska J.B., Copass M.C., Falkow S. The Yersinia pseudotuberculosis adhesin YadA mediates intimate bacterial attachment to and entry into Hep-2 cells. Inf Immun 1993; 61:3914-21.
  • 49. Heesemann J., Gruter L. Genetic evidence that the outer membrane protein Yop1 of Yersinia enteroclitica mediates adherence and phagocytosis resistance to human epithelial cells. FEMS Microbiol Let 1987; 40:37-41.
  • 50. Yang Y., Isberg R.R. Cellular internalization in the absence of invasin expression is promoted by the Yersinia pseudotuberculosis yadA product. Infect Immun 1993; 61:3907-13.
  • 51. Visser L.G., Annema A., van Furth R. Role of Yops in inhibition of phagocytosis and killing of opsonized Yersinia enterocolitica by human granulocytes. Infect Immun 1995; 63:2570-5.
  • 52. Roggenkamp A., Ruchdeschel K., Leitritz L., Schmitt R., Heesemann J. Deletion of aminoacids 29 to 81 in adhesion protein YadA of Yersinia enterocolitica serotype O:8 resuts in selective abrogation of adherence to neutrophils. Infect Immun 1996; 64:2506-14.
  • 53. Han Y.W., Miller V.L. Reevaluation of the virulence phenotype of the inv yadA double mutants of Yersinia pseudotuberculosis. Infect Immun. 1997; 65:327-30.
  • 54. Rosqvist R., Forsberg A., Wolf-Watz H. Intracellular targeting of the Yersinia YopE cytotoxin in mammalian cells induces actin microfilament disruption. Infect Innnun 1991; 59:4562-9.
  • 55. Forsberg A., Rosqvist R. In vivo expression of virulence genes of Yersinia pseudotuberculosis. Infect Agents Dis 1993; 2:275-8.
  • 56. Guan K., Dixon J.E. Protein tyrosine phosphatase activity of an essential virulence determinant in Yersinia. Science 1990; 249:553-6.
  • 57. Andersson К., Carballeira N., Magnosson K.E., et al. YopH of Yersinia pseudotuberculosis interrupts early phosphotyrosine signalling associated with phagocytosis. Mol Microbiol 1996; 20:1057-69.
  • 58. Persson С., Carballeira N., Wolf-Watz H., Fallman M. The PTPase YopH inhibits uptake of Yersinia, tyrosine phosphorylation of p130 Cas and FAK, and the associated accumulation of these proteins in peripheral focal adhesion. EMBO J 1997; 16:2307-18.
  • 59. Follman M., Andersson К., Hakansson S., Magnass K.-E., Stendahl O., Wotf-Watz H. Yersinia pseudotuberculosis inhibits Fc receptor-mediated phagocytosis in J774 cells. Infect Immun 1995; 63:3117-24.
  • 60. Galyov E.E., Hakansson S., Forsberg A., Wolf-Watz H. A secreted protein kinase of Yersinia pseudotuberculosis showing homology with eukariotic Ser/Thr protein kinases is an indispensable virulence determinant. Nature 1993; 361:730-2.
  • 61. Mills S.D., Boland A., Sory M.P., et al. Yersinia enterocolitica induces apoptosis in macrophages by a process requiring functional type III secretion and translocation mechanisms and involving YopP, presumably acting as an effector protein. Proc Nat Acad Sci USA 1997; 94:12638-43.
  • 62. Palmer L.E.S., Hobbie S., Galan J.E., Bliska J.B. YopJ оf Yersinia pseudotuberculosis is required for the inhibition of macrophages TNF-α production and downregulation of the MAP kinase p38 and JNK. Mol Microbiol 1998; 27:953-5.
  • 63. Monack D.M., Mecsas J., Ghori N., Falkow S. Yersinia signals macrophages to undergo apoptosis and YopJ iz necessary for this cell death. Proc Natl Acad Sci USA 1997; 94:10385-90.
  • 64. Boland A, Cornelis G.R. Role of YopP in supression of tumor necrosis factor alpha release by macrophages during Yersinia infection. Infect Immun 1998; 66:1878-1884.
  • 65. Leung K.Y., Reisner B.S., Straley S.C. YopM inhibits platelet aggregation and is necessary for virulence of Yersinia pestis in mice. Infect Immun 1990; 58:3262-71.
  • 66. Iriarte M., Cornelis G.R. YopT, a new Yersinia Yop effector protein, affects the cytoskeleton of host cells. Mol Microbiol 1998; 29:915-29.
  • 67. Kerr J. Type III (contact-dependent) secretion in Gramnegative bacteria. Rev Med Microbiol 1999; 10:155-64.
  • 68. Hakansson S., Bergman Т., Vanooteghem J.-C., Cornelis G., Wolf-Watz H. YopB and YopD constitute a novel class of Yersinia Yop proteins. Infect Immun 1993; 61:71-80.
  • 69. Neyt C., Cornelis G. Insertion of a Yop translocation pore into the macrophage plasma membrane by Yersinia enterocolitica: requirement for translocators YopB and YopD, but not LcrG. Mol Microbiol 1999; 33:971-81.
  • 70. Neyt C., Cornelis G. Role of SycD, the shaperone of the Yersinia Yop translocators YopB and YopD. Mol Microbiol 1999; 31:143-56.
  • 71. Hakansson S., Schesser K., Persson С., et al. The YopB protein of Yersinia pseudotuberculosis is essential for the translocation of Yop effector proteins across the target cell plasma membrane and displays a contact-depended membrane disrupting activity. EMBO J 1996; 15:581223.
  • 72. Hartland E.L., Robins-Browne R.M. In vitro association between the virulence proteins, YopD and YopE, of Yersinia enterocolitica. FEMS Microbiol Let 1998; 162:207-13.
  • 73. Sarker M.R., Neyt С., Stainier I., Cornelis G. The Yersinia Yop virulon: LcrV is required for extrusion of the translocators YopB and YopD. J Bacteriol 1998; 180:1207-14.
  • 74. Beuscher H.U., Burdack S., Rollinghoff M. Bacterial cytokine antagonists encoded by pathogenic yersiniae. Behring Institute Mitteilungen 1997; 98:240-8.
  • 75. Roggenkamp A., Geiger A.M., Leitritz L., Kessler A., Heesemann J. Passive immunity to infection with Yersinia spp. mediated by anti-recombinant V antigen is dependent on polymorphism of V antigen. Infection Immun 1997; 65:446-51.
  • 76. Boyd АР., Sory M P., Iriarte M., Cornelis G.R. Heparin interferes with translocation of Yop proteins into HeLa cells and binds to LcrG, a regulatory component of the Yersinia Yop apparatus. Mol Microbiol 1998; 27: 425-36.
  • 77. Nilles M.L., Fields K.A, Straley S.C. The V antigen of Yersinia pestis regulates Yop vectorial targeting as well as Yop secretion through effects on YopB and LcrG. J Bacteriol 1998; 180:3410-20.
  • 78. Koster M., Bitter W., de Cock H., Allaoui A., Cornelis G.R., Tommassen J. The outer membrane component, YscC, of the Yop secretion machinery of Yersinia enterocolitica forms a ring-shaped multimeric complex. Mol Microbiol 1997; 26:789-98.
  • 79. Iriarte M., Sory M.P., Boland A., et al. TyeA, a protein involved in control of Yop release and in translocation of Yersinia Yop effectors. EMBO J 1998; 17:1907-18.
  • 80. Sarker M.R, Sory M.-P., Boyd A.P., Iriarte M., Cornelis G.R. LcrG is required for efficient translocation of Yersinia Yop effector proteins into eukariotic cells. Infect Immun 1998; 66:2976-9.
  • 81. Nilles M.L., Williams W., Skrzypek E., Straley S.C. Yersinia pestis LcrV forms a stable complex with LcrG and may have a secretion-related regulatory role in the low-Ca2+ response. J Bacteriol 1997; 179:1307-16.
  • 82. Holmstrom A., Rosqvist R., Wolf-Watz H., Forsberg A. Virulence plasmid-encoded YopK is essential for Yersinia pseudotuberculosis to cause systemic infection in mice. Infect Immun 1995; 63:2269-76.
  • 83. Holmstrom A., Pettrson J., Rosqvist R., et al. A YopK of Yersinia pseudotuberculosis controls translocation of Yop effectors across the eukaryotic cell membrane. Mol Microbiol 1997; 24:73-91.
  • 84. Lambert de Rouvroit С., Sluiters С., Cornelis G. Role of the transcriptional activator, VirF, and temperature in the expression of the pYV plazmid genes of Yersinia enterocolitica. Mol Microbiol 1992; 6:395-409.
  • 85. Hanski C., Kutschuka U., Schmoranzer H.P., et al. Immunohistichemical and electron microscopic study of interaction of Yersinia enterocolitica serotype O:8 with intestinal mucosa during experimental enteritis. Infect Immun 1989; 57:673-8.
  • 86. Carniel E. The Yersinia high-pathogenicity island. Intern Micribiol 1999; 2:161-7.
  • 87. Hacker J., Blum-Oehler G., Muhldorier I. Pathogenicity islands of virulent bacteria: structure, function and imppact on microbial evolution. Mol Microbiol 1997; 23:1089-97.
  • 88. Carniel E., Guilvout I., Prentice M. Characterization of a large chromosomal «high-pathogenicity island» in biotype 1b Yersinia enterocolitica. J Bacteriol 1996; 178:6743-51.
  • 89. Gehring A.M., Demoll E., Fetherston J.D., et al. Iron acquisition in plague: modular logic in enzymatic biogenesis of yersiniabactine in Yersinia pestis. Chem Biol 1998; 5:573-86.
  • 90. Buchrieser C., Brosh R., Bach S., Guiyole A., Carniel E. The high-pathogenicity island of Y. pseudotuberculosis can be inserted into any of the three chromosomal asn tRNA genes. Mol Microbiol 1998; 30:965-78.
  • 91. Carniel E., Guiyole A., Guilvout I., Mercereau Puijalon O. Molecular cloning, iron-regulation and mutagenesis of the irp2 gene encoding HMWP2, a protein specific for the hihgly pathogenic Yersinia. Mol Microbiol 1992; 6:379-88.
  • 92. Rakin A., Saken E., Harmsen D., Heesemann J. The pesticin receptor of Yersinia enterocolitica: a novel virulence factor with dual function. Mol Microbiol 1994; 13: 253-63.
  • 93. Straley S.C., Perry R.D. Environmental modulation of gene expretion and pathogenesis in Yersinia. Trends in Mocrobiology 1995; 3:310-7.
  • 94. Бондаренко В.М. Факторы патогенности бактерий и их роль в развитии инфекционного процесса. Журн микробиол 1999; 5:34-9.
  • 95. Donnelly G.A.E., Lu J., Takeda Т., МсКеу D.M. Colonic epithelial physiology is altered in response to the bacterial superantigen Yersinia pseudotuberculosis mitogen. J Infec Dis 1999; 180:1590-6.
  • 96. Куляшова Л.Б., Ценева Г.Я., Буйневич Ю.Б. Роль антигенов наружной мембраны Yersinia pseudotuberculosis в патогенезе и диагностике псевдотуберкулеза. Журн микробиол 1997; 1:14-8.
  • 97. Saikia G.K, Thapliyal D.C. Enterotoxigenicity as an attribute of virulence in Yersinia enterocolitica. Indian J Experiment Biol 1997; 35:1108-10.
  • 98. Miyoshi-Akiyama Т., Imanischi K., Uchiyama T. Purification and partial characterization of a product from Yersinia pseudotuberculosis with the ability to activate human T-cells. Infect Immun 1993; 61:3922-7.
  • 99. Саrnоу С., Muller-Alouf H., Desreumaux P., Mullet С., Grangette С., Simonet M. The superantigenic toxin of Yersinia pseudotuberculosis. a novel virulence factor? Int J Med Microbiol 2000; 290:477-82.
  • 100. Carnoy C., Mullet С., Muller-Alouf H., Leteurtre E., Simonet M. Superantigen YPMa exacerbates the virulence of Yersinia pseudotuberculosis in mice. Infect Immun 2000; 68:2553-9.
  • 101. Бондаренко В.М., Голкочева Е.Н., Найденский X. Обнаружение островков высокой патогенности и синтеза SIgA протеазы у редко встречающихся видов иерсиний. Материалы конференции «Инфекции, обусловленные иерсиниями (иерсиниоз, псевдотуберкулез), и другие актуальные инфекции. Санкт-Петербургский НИИЭМ им. Пастера; 2000. с. 8.
  • 102. Бурцева Т.И., Бузолева Л.С., Сомов Г.П. Секретируемая трипсиноподобная протеиназа Yersinia pseudotuberculosis. Биохимия 1995; 60:1589-95.
  • 103. Gemski P., Lazere J.R., Casey T. Plasmid associated with pathogenicity and calcium dependence of Yersinia enterocolitica. Infect Immun 1980; 27:682-5.
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