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Volumn 188, Issue 3, 1999, Pages 151-159

Anti-recombinant V antigen serum promotes uptake of Yersinia enterocolitica serotype O8 by macrophages

Author keywords

Passive immunization; Phagocytosis resistance; V antigen; Yersinia enterocolitica

Indexed keywords

BACTERIAL ANTIGEN; CYTOCHALASIN D; GENTAMICIN; OUTER MEMBRANE PROTEIN; RECOMBINANT PROTEIN;

EID: 0033390753     PISSN: 03008584     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004300050118     Document Type: Article
Times cited : (7)

References (50)
  • 1
    • 0026554246 scopus 로고
    • T lymphocytes mediate protection against Yersinia enterocolitica in mice: Characterization of murine T-cell clones specific for Y. enterocolitica
    • 1. Autenrieth IB, Tingle A, Reske Kunz A, Heesemann J (1992) T lymphocytes mediate protection against Yersinia enterocolitica in mice: characterization of murine T-cell clones specific for Y. enterocolitica. Infect Immun 60:1140-1149
    • (1992) Infect Immun , vol.60 , pp. 1140-1149
    • Autenrieth, I.B.1    Tingle, A.2    Reske Kunz, A.3    Heesemann, J.4
  • 2
    • 0026022459 scopus 로고
    • Analysis of the V antigen lcrGVH-yopBD operon of Yersinia pseudotuberculosis: Evidence for a regulatory role of LcrH and LcrV
    • 2. Bergman T, Hakansson S, Forsberg A, Norlander L, Macellaro A, Backman A, Bolin I, Wolf-Watz H (1991) Analysis of the V antigen lcrGVH-yopBD operon of Yersinia pseudotuberculosis: evidence for a regulatory role of LcrH and LcrV. J Bacteriol 173:1607-1616
    • (1991) J Bacteriol , vol.173 , pp. 1607-1616
    • Bergman, T.1    Hakansson, S.2    Forsberg, A.3    Norlander, L.4    Macellaro, A.5    Backman, A.6    Bolin, I.7    Wolf-Watz, H.8
  • 3
    • 0028900810 scopus 로고
    • Inhibition of the Fc receptor-mediated oxidative burst in macrophages by the Yersinia pseudotuberculosis tyrosine phosphatase
    • 3. Bliska JB, Black DS (1995) Inhibition of the Fc receptor-mediated oxidative burst in macrophages by the Yersinia pseudotuberculosis tyrosine phosphatase. Infect Immun 63:681-685
    • (1995) Infect Immun , vol.63 , pp. 681-685
    • Bliska, J.B.1    Black, D.S.2
  • 4
    • 0029814613 scopus 로고    scopus 로고
    • Status of YopM and YopN in the Yersinia Yop virulon: YopM of Y. enterocolitica is internalized inside the cytosol of PU5-1.8 macrophages by the YopB, D, N delivery apparatus
    • 4. Boland A, Sory MP, Iriarte M, Kerbourch C, Wattiau P, Cornelis GR (1996) Status of YopM and YopN in the Yersinia Yop virulon: YopM of Y. enterocolitica is internalized inside the cytosol of PU5-1.8 macrophages by the YopB, D, N delivery apparatus. EMBO J 15:5191-5201
    • (1996) EMBO J , vol.15 , pp. 5191-5201
    • Boland, A.1    Sory, M.P.2    Iriarte, M.3    Kerbourch, C.4    Wattiau, P.5    Cornelis, G.R.6
  • 5
    • 0031026828 scopus 로고    scopus 로고
    • The Yersinia Yop virulon: A bacterial system for subverting eukaryotic cells
    • 5. Cornelis GR, Wolf-Watz H (1997) The Yersinia Yop virulon: a bacterial system for subverting eukaryotic cells. Mol Microbiol 23:861-867
    • (1997) Mol Microbiol , vol.23 , pp. 861-867
    • Cornelis, G.R.1    Wolf-Watz, H.2
  • 7
    • 0028276409 scopus 로고
    • Interaction of polymorphonuclear leukocytes with Yersinia enterocolitica: Role of the Yersinia virulence plasmid and modulation by the iron-chelator desferrioxamine B
    • 7. Ewald JH, Heesemann J, Rüdiger H, Autenrieth IB (1994) Interaction of polymorphonuclear leukocytes with Yersinia enterocolitica: role of the Yersinia virulence plasmid and modulation by the iron-chelator desferrioxamine B. J Infect Dis 170:140-150
    • (1994) J Infect Dis , vol.170 , pp. 140-150
    • Ewald, J.H.1    Heesemann, J.2    Rüdiger, H.3    Autenrieth, I.B.4
  • 9
    • 0242504622 scopus 로고    scopus 로고
    • Yersinia proteins that target host cell signaling pathways
    • 9. Fallman M, Persson C, Wolf-Watz H (1997) Yersinia proteins that target host cell signaling pathways. J Clin Invest 99:1153-1157
    • (1997) J Clin Invest , vol.99 , pp. 1153-1157
    • Fallman, M.1    Persson, C.2    Wolf-Watz, H.3
  • 10
    • 0025762461 scopus 로고
    • The surface-located YopN protein is involved in calcium signal transduction in Yersinia pseudotuberculosis
    • 10. Forsberg A, Viitanen AM, Skurnik M, Wolf-Watz H (1991) The surface-located YopN protein is involved in calcium signal transduction in Yersinia pseudotuberculosis. Mol Microbiol 5:977-986
    • (1991) Mol Microbiol , vol.5 , pp. 977-986
    • Forsberg, A.1    Viitanen, A.M.2    Skurnik, M.3    Wolf-Watz, H.4
  • 11
    • 0029908022 scopus 로고    scopus 로고
    • 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-dependent membrane disrupting activity
    • 11. Hakansson S, Schesser K, Persson C, Galyov EE, Rosqvist R, Homble F, Wolf-Watz H (1996) 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-dependent membrane disrupting activity. EMBO J 155812-5823
    • (1996) EMBO J , pp. 155812-155823
    • Hakansson, S.1    Schesser, K.2    Persson, C.3    Galyov, E.E.4    Rosqvist, R.5    Homble, F.6    Wolf-Watz, H.7
  • 12
    • 0021868498 scopus 로고
    • Double immunofluorescence microscopic technique for accurate differentiation of extracellularly and intracellularly located bacteria in cell culture
    • 12. Heesemann J, Laufs R(1985) Double immunofluorescence microscopic technique for accurate differentiation of extracellularly and intracellularly located bacteria in cell culture. J Clin Microbiol 22:168-175
    • (1985) J Clin Microbiol , vol.22 , pp. 168-175
    • Heesemann, J.1    Laufs, R.2
  • 13
    • 0020692529 scopus 로고
    • Plasmids of human strains of Yersinia enterocolitica: Molecular relatedness and possible importance for pathogenesis
    • 13. Heesemann J, Keller C, Morawa R, Schmidt N, Siemens HJ, Laufs R (1983) Plasmids of human strains of Yersinia enterocolitica: molecular relatedness and possible importance for pathogenesis. J Infect Dis 147:107-115
    • (1983) J Infect Dis , vol.147 , pp. 107-115
    • Heesemann, J.1    Keller, C.2    Morawa, R.3    Schmidt, N.4    Siemens, H.J.5    Laufs, R.6
  • 14
    • 0030777667 scopus 로고    scopus 로고
    • Regions of Yersinia pestis V antigen that contribute to protection against plague identified by passive and active immunization
    • 14. Hill J, Leary SE, Griffin KF, Williamson ED, Titball RW (1997) Regions of Yersinia pestis V antigen that contribute to protection against plague identified by passive and active immunization. Infect Immun 65:4476-4482
    • (1997) Infect Immun , vol.65 , pp. 4476-4482
    • Hill, J.1    Leary, S.E.2    Griffin, K.F.3    Williamson, E.D.4    Titball, R.W.5
  • 15
    • 0031864184 scopus 로고    scopus 로고
    • Type III protein secretion systems in bacterial pathogens of animals and plants
    • 15. Hueck CJ (1998) Type III protein secretion systems in bacterial pathogens of animals and plants. Microbiol Mol Biol Rev 62:379-433
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 379-433
    • Hueck, C.J.1
  • 16
    • 0031880899 scopus 로고    scopus 로고
    • YopT, a new Yersinia effector protein, affects the cytoskeleton of host cells
    • 16. Iriarte M, Cornelis GR (1998) YopT, a new Yersinia effector protein, affects the cytoskeleton of host cells. Mol Microbiol 29:915-929
    • (1998) Mol Microbiol , vol.29 , pp. 915-929
    • Iriarte, M.1    Cornelis, G.R.2
  • 17
    • 0032055051 scopus 로고    scopus 로고
    • TyeA, a protein involved in control of Yop release and in translocation of Yersinia Yop effectors
    • 17. Iriarte M, Sory MP, Boland A, Boyd AP, Mills SD, Lambermont I Cornells GR (1998) TyeA, a protein involved in control of Yop release and in translocation of Yersinia Yop effectors. EMBO J 17:1907-1918
    • (1998) EMBO J , vol.17 , pp. 1907-1918
    • Iriarte, M.1    Sory, M.P.2    Boland, A.3    Boyd, A.P.4    Mills, S.D.5    Lambermont I Cornells, G.R.6
  • 18
    • 0022406060 scopus 로고
    • A single genetic locus encoded by Yersinia pseudotuberculosis permits invasion of cultured animal cells by Escherichia coli K-12
    • 18. Isberg RR, Falkow S (1985) A single genetic locus encoded by Yersinia pseudotuberculosis permits invasion of cultured animal cells by Escherichia coli K-12. Nature 317:262-264
    • (1985) Nature , vol.317 , pp. 262-264
    • Isberg, R.R.1    Falkow, S.2
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 19. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0026542646 scopus 로고
    • Role of the transcriptional activator, VirF, and temperature in the expression of the pYV plasmid genes of Yersinia enterocolitica
    • 20. Lambert de Rouvroit C, Sluiters C, Cornelis GR (1992) Role of the transcriptional activator, VirF, and temperature in the expression of the pYV plasmid genes of Yersinia enterocolitica. Mol Microbiol 6:395-409
    • (1992) Mol Microbiol , vol.6 , pp. 395-409
    • Lambert De Rouvroit, C.1    Sluiters, C.2    Cornelis, G.R.3
  • 21
    • 0000735659 scopus 로고
    • Biosynthesis and purification of V and W antigen in Yersinia pestis
    • 21. Lawton WD, Erdman RL, Surgalla ML (1963) Biosynthesis and purification of V and W antigen in Yersinia pestis. J Immunol 91:179-185
    • (1963) J Immunol , vol.91 , pp. 179-185
    • Lawton, W.D.1    Erdman, R.L.2    Surgalla, M.L.3
  • 22
    • 0029134827 scopus 로고
    • Active immunization with recombinant V antigen from Yersinia pestis protects mice against plague
    • 22. Leary SE, Williamson ED, Griffin KF, Russell P, Eley SM, Titball RW (1995) Active immunization with recombinant V antigen from Yersinia pestis protects mice against plague. Infect Immun 63:2854-2858
    • (1995) Infect Immun , vol.63 , pp. 2854-2858
    • Leary, S.E.1    Williamson, E.D.2    Griffin, K.F.3    Russell, P.4    Eley, S.M.5    Titball, R.W.6
  • 23
    • 0030998981 scopus 로고    scopus 로고
    • Type III secretion systems: Machines to deliver bacterial proteins into eukaryotic cells?
    • 23. Lee CA (1997) Type III secretion systems: machines to deliver bacterial proteins into eukaryotic cells? Trends Microbiol 5148-5156
    • (1997) Trends Microbiol , pp. 5148-5156
    • Lee, C.A.1
  • 24
    • 0028058806 scopus 로고
    • Passive immunity to yersiniae mediated by anti-recombinant V antigen and protein A-V antigen fusion peptide
    • 24. Motin VL, Nakajima R, Smirnov GB, Brubaker RR (1994) Passive immunity to yersiniae mediated by anti-recombinant V antigen and protein A-V antigen fusion peptide. Infect Immun 62:4192-4201
    • (1994) Infect Immun , vol.62 , pp. 4192-4201
    • Motin, V.L.1    Nakajima, R.2    Smirnov, G.B.3    Brubaker, R.R.4
  • 25
    • 0027534069 scopus 로고
    • Association between virulence of Yersinia pestis and suppression of gamma interferon and tumor necrosis factor alpha
    • 25. Nakajima R, Brubaker RR(1993) Association between virulence of Yersinia pestis and suppression of gamma Interferon and tumor necrosis factor alpha. Infect Immun 61:23-31
    • (1993) Infect Immun , vol.61 , pp. 23-31
    • Nakajima, R.1    Brubaker, R.R.2
  • 26
    • 0029021978 scopus 로고
    • Suppression of cytokines in mice by protein A-V antigen fusion peptide and restoration of synthesis by active immunization
    • 26. Nakajima R, Motin VL, Brubaker RR (1995) Suppression of cytokines in mice by protein A-V antigen fusion peptide and restoration of synthesis by active immunization. Infect Immun 63:3021-3029
    • (1995) Infect Immun , vol.63 , pp. 3021-3029
    • Nakajima, R.1    Motin, V.L.2    Brubaker, R.R.3
  • 27
    • 0030946572 scopus 로고    scopus 로고
    • Resistance to lipopolysaccharide mediated by yersiniae V antigen-polyhistidine fusion peptide: Amplification of interleukin-10
    • 27. Nedialkov YA, Motin VL, Brubaker RR (1997) Resistance to lipopolysaccharide mediated by yersiniae V antigen-polyhistidine fusion peptide: amplification of interleukin-10. Infect Immun 65:1196-1203
    • (1997) Infect Immun , vol.65 , pp. 1196-1203
    • Nedialkov, Y.A.1    Motin, V.L.2    Brubaker, R.R.3
  • 29
    • 0031802098 scopus 로고    scopus 로고
    • The V antigen of Yersinia pestis regulates Yop vectorial targeting as well as Yop secretion through effects on YopB and LcrG
    • 29. Nilles ML, Fields KA, Straley SC (1998) The V antigen of Yersinia pestis regulates Yop vectorial targeting as well as Yop secretion through effects on YopB and LcrG. J Bacteriol 180:3410-3420
    • (1998) J Bacteriol , vol.180 , pp. 3410-3420
    • Nilles, M.L.1    Fields, K.A.2    Straley, S.C.3
  • 30
    • 0028802323 scopus 로고
    • Cell-surface-bound Yersinia translocate the protein tyrosine phosphatase YopH by a polarized mechanism into the target cell
    • 30. Persson C, Nordfelth R, Holmström A, Hakansson S, Rosqvist R, Wolf-Watz H (1995) Cell-surface-bound Yersinia translocate the protein tyrosine phosphatase YopH by a polarized mechanism into the target cell. Mol Microbiol 18:135-150
    • (1995) Mol Microbiol , vol.18 , pp. 135-150
    • Persson, C.1    Nordfelth, R.2    Holmström, A.3    Hakansson, S.4    Rosqvist, R.5    Wolf-Watz, H.6
  • 34
    • 0031907148 scopus 로고    scopus 로고
    • Analysis of the Yersinia pestis V protein for the presence of linear antibody epitopes
    • 34. Pullen JK, Anderson GW Jr, Welkos SL, Friedlander AM (1998) Analysis of the Yersinia pestis V protein for the presence of linear antibody epitopes. Infect Immun 66:521-527
    • (1998) Infect Immun , vol.66 , pp. 521-527
    • Pullen, J.K.1    Anderson G.W., Jr.2    Welkos, S.L.3    Friedlander, A.M.4
  • 35
    • 0029088644 scopus 로고
    • Substitution of two histidine residues in YadA protein of Yersinia enterocolitica abrogates collagen binding, cell adherence and mouse virulence
    • 35. Roggenkamp A, Neuberger H-R, Flügel A, Schmoll T, Heesemann J (1995) Substitution of two histidine residues in YadA protein of Yersinia enterocolitica abrogates collagen binding, cell adherence and mouse virulence. Mol Microbiol 16:1207-1219
    • (1995) Mol Microbiol , vol.16 , pp. 1207-1219
    • Roggenkamp, A.1    Neuberger, H.-R.2    Flügel, A.3    Schmoll, T.4    Heesemann, J.5
  • 36
    • 0031018415 scopus 로고    scopus 로고
    • Passive immunity to infection with Yersinia spp. mediated by anti-recombinant V antigen is dependent on polymorphism of V antigen
    • 36. Roggenkamp A, Geiger AM, Leitritz L, Kessler A, Heesemann J (1997) Passive immunity to infection with Yersinia spp. mediated by anti-recombinant V antigen is dependent on polymorphism of V antigen. Infect Immun 65:446-451
    • (1997) Infect Immun , vol.65 , pp. 446-451
    • Roggenkamp, A.1    Geiger, A.M.2    Leitritz, L.3    Kessler, A.4    Heesemann, J.5
  • 38
    • 0027982852 scopus 로고
    • Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells
    • 38. Rosqvist R, Magnusson KE, Wolf-Watz H (1994) Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells. EMBO J 13:964-972
    • (1994) EMBO J , vol.13 , pp. 964-972
    • Rosqvist, R.1    Magnusson, K.E.2    Wolf-Watz, H.3
  • 39
    • 0030041090 scopus 로고    scopus 로고
    • Differential contribution of Yersinia enterocolitica virulence factors to evasion of microbicidal action of neutrophils
    • 39. Ruckdeschel K, Roggenkamp A, Schubert S, Heesemann J (1996) Differential contribution of Yersinia enterocolitica virulence factors to evasion of microbicidal action of neutrophils. Infect Immun 64:724-733
    • (1996) Infect Immun , vol.64 , pp. 724-733
    • Ruckdeschel, K.1    Roggenkamp, A.2    Schubert, S.3    Heesemann, J.4
  • 40
    • 0031885218 scopus 로고    scopus 로고
    • The Yersinia Yop virulon: LcrV is required for extrusion of the translocators YopB and YopD
    • 40. Sarker MR, Neyt C, Stainier I, Cornelis GR (1998) The Yersinia Yop virulon: LcrV is required for extrusion of the translocators YopB and YopD. J Bacteriol 180:1207-1214
    • (1998) J Bacteriol , vol.180 , pp. 1207-1214
    • Sarker, M.R.1    Neyt, C.2    Stainier, I.3    Cornelis, G.R.4
  • 41
    • 0031811818 scopus 로고    scopus 로고
    • LcrG is required for efficient translocation of Yersinia Yop effector proteins into eukaryotic cells
    • 41. Sarker MR, Sory MP, Boyd AP, Iriarte M, Cornelis GR (1998) LcrG is required for efficient translocation of Yersinia Yop effector proteins into eukaryotic cells. Infect Immun 66:2976-2979
    • (1998) Infect Immun , vol.66 , pp. 2976-2979
    • Sarker, M.R.1    Sory, M.P.2    Boyd, A.P.3    Iriarte, M.4    Cornelis, G.R.5
  • 42
    • 0032907634 scopus 로고    scopus 로고
    • Active and passive immunization with the Pseudomonas V antigen protects against type III intoxication and lung injury
    • 42. Sawa T, Yahr TL, Ohara M, Kurahashi K, Gropper MA, Wiener-Kronish JP, Frank DW (1999) Active and passive immunization with the Pseudomonas V antigen protects against type III intoxication and lung injury. Nat Med 5:392-398
    • (1999) Nat Med , vol.5 , pp. 392-398
    • Sawa, T.1    Yahr, T.L.2    Ohara, M.3    Kurahashi, K.4    Gropper, M.A.5    Wiener-Kronish, J.P.6    Frank, D.W.7
  • 43
    • 0031775572 scopus 로고    scopus 로고
    • The yopJ locus is required for Yersinia-mediated inhibition of NF-kB activation and cytokine expression: YopJ contains a eukaryotic SH2-like domain that is essential for its repressive activity
    • 43. Schesser K, Spiik A-K, Dukuzumuremyi J-M, Neurath MF, Pettersson S, Wolf-Watz H (1998) The yopJ locus is required for Yersinia-mediated inhibition of NF-kB activation and cytokine expression: YopJ contains a eukaryotic SH2-like domain that is essential for its repressive activity. Mol Microbiol 28:1067-1079
    • (1998) Mol Microbiol , vol.28 , pp. 1067-1079
    • Schesser, K.1    Spiik, A.-K.2    Dukuzumuremyi, J.-M.3    Neurath, M.F.4    Pettersson, S.5    Wolf-Watz, H.6
  • 45
    • 0027229148 scopus 로고
    • LcrG, a secreted protein involved in negative regulation of the low-calcium response in Yersinia pestis
    • 45. Skryzpek E, Straley SC (1993) LcrG, a secreted protein involved in negative regulation of the low-calcium response in Yersinia pestis. J Bacteriol 175:3520-3528
    • (1993) J Bacteriol , vol.175 , pp. 3520-3528
    • Skryzpek, E.1    Straley, S.C.2
  • 46
    • 0029031698 scopus 로고
    • 2+ response, and virulence of Yersinia pestis
    • 2+ response, and virulence of Yersinia pestis. J Bacteriol 177:2530-2542
    • (1995) J Bacteriol , vol.177 , pp. 2530-2542
    • Skrzypek, E.1    Straley, S.C.2
  • 47
    • 0030698085 scopus 로고    scopus 로고
    • YscM1 and YscM2, two Yersinia enterocolitica proteins causing downregulation of yop transcription
    • 47. Stainier I, Iriarte M, Cornelis GR (1997) YscM1 and YscM2, two Yersinia enterocolitica proteins causing downregulation of yop transcription. Mol Microbiol 26:833-843
    • (1997) Mol Microbiol , vol.26 , pp. 833-843
    • Stainier, I.1    Iriarte, M.2    Cornelis, G.R.3
  • 48
    • 0021150264 scopus 로고
    • Roles of V antigen in promoting virulence and immunity in yersiniae
    • 48. Une T, Brubaker RR (1984) Roles of V antigen in promoting virulence and immunity in yersiniae. J Immunol 133:2226-2230
    • (1984) J Immunol , vol.133 , pp. 2226-2230
    • Une, T.1    Brubaker, R.R.2
  • 49
    • 0027180060 scopus 로고
    • Role of plasmid-encoded antigens of Yersinia enterocolitica in humoral immunity against secondary Y. enterocolitica infection in mice
    • 49. Vogel U, Autenrieth IB, Berner R, Heesemann J (1993) Role of plasmid-encoded antigens of Yersinia enterocolitica in humoral immunity against secondary Y. enterocolitica infection in mice. Microb Pathog 15:23-36
    • (1993) Microb Pathog , vol.15 , pp. 23-36
    • Vogel, U.1    Autenrieth, I.B.2    Berner, R.3    Heesemann, J.4
  • 50
    • 0031936516 scopus 로고    scopus 로고
    • YopD of Yersinia pestis plays a role in negative regulation of the low-calcium response in addition to its role in translocation of Yops
    • 50. Williams AW, Straley SC (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
    • (1998) J Bacteriol , vol.180 , pp. 350-358
    • Williams, A.W.1    Straley, S.C.2


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