메뉴 건너뛰기




Volumn 180, Issue 2, 1998, Pages 350-358

YopD of Yersinia pestis plays a role in negative regulation of the low- calcium response in addition to its role in translocation of Yops

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; OUTER MEMBRANE PROTEIN;

EID: 0031936516     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.2.350-358.1998     Document Type: Article
Times cited : (127)

References (62)
  • 4
    • 0026022459 scopus 로고
    • Analysis of the V antigen lcrGVH-yopBD operon of Yersinia pseudotuberculosis: Evidence for a regulatory role of LcrH and LcrV
    • Bergman, T., S. Håkansson, Å. Forsberg, L. Norlander, A. Macellaro, A. Bäckman, I. Bölin, and H. Wolf-Watz. 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    Håkansson, S.2    Forsberg, Å.3    Norlander, L.4    Macellaro, A.5    Bäckman, A.6    Bölin, I.7    Wolf-Watz, H.8
  • 5
    • 0028217290 scopus 로고
    • The lcrB (yscN/U) gene cluster of Yersinia pseudotuberculosis is involved in Yop secretion and shows high homology to the spa gene clusters of Shigella flexneri and Salmonella typhimurium
    • Bergman, T., K. Erickson, E. Golyov, C. Persson, and H. Wolf-Watz. 1994. The lcrB (yscN/U) gene cluster of Yersinia pseudotuberculosis is involved in Yop secretion and shows high homology to the spa gene clusters of Shigella flexneri and Salmonella typhimurium. J. Bacteriol. 176:2619-2626.
    • (1994) J. Bacteriol. , vol.176 , pp. 2619-2626
    • Bergman, T.1    Erickson, K.2    Golyov, E.3    Persson, C.4    Wolf-Watz, H.5
  • 7
    • 0024546348 scopus 로고
    • Homology between VirF, the transcriptional activator of the Yersinia virulence region, and the Escherichia coli arabinose operon regulator
    • Cornelis, G. R., C. Sluiters, C. Lambert de Rouvroit, and T. Michiels. 1989. Homology between VirF, the transcriptional activator of the Yersinia virulence region, and the Escherichia coli arabinose operon regulator. J. Bacteriol. 171:254-262.
    • (1989) J. Bacteriol. , vol.171 , pp. 254-262
    • Cornelis, G.R.1    Sluiters, C.2    Lambert De Rouvroit, C.3    Michiels, T.4
  • 8
    • 0031026828 scopus 로고    scopus 로고
    • The Yersinia Yop virulon: A bacterial system for subverting eukaryotic cells
    • Cornelis, G. R., and H. Wolf-Watz. 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
  • 9
    • 0019435820 scopus 로고
    • Plasmids in Yersinia pestis
    • Ferber, D. M., and R. R. Brubaker. 1981. Plasmids in Yersinia pestis. Infect. Immun. 31:839-841.
    • (1981) Infect. Immun. , vol.31 , pp. 839-841
    • Ferber, D.M.1    Brubaker, R.R.2
  • 10
    • 0028178610 scopus 로고
    • 2+ response (LCR) secretion (ysc) locus lies within the lcrB region of the LCR plasmid in Yersinia pestis
    • 2+ response (LCR) secretion (ysc) locus lies within the lcrB region of the LCR plasmid in Yersinia pestis. J. Bacteriol. 176:569-579.
    • (1994) J. Bacteriol. , vol.176 , pp. 569-579
    • Fields, K.A.1    Plano, G.V.2    Straley, S.C.3
  • 12
    • 0030954706 scopus 로고    scopus 로고
    • Failure to detect binding of LcrH to the V antigen of Yersinia pestis
    • Fields, K. A., A. W. Williams, and S. C. Straley. 1997. Failure to detect binding of LcrH to the V antigen of Yersinia pestis. Infect. Immun. 65:3954-3957.
    • (1997) Infect. Immun. , vol.65 , pp. 3954-3957
    • Fields, K.A.1    Williams, A.W.2    Straley, S.C.3
  • 13
    • 0025762461 scopus 로고
    • The surface-located YopN protein is involved in calcium signal transduction in Yersinia pseudotuberculosis
    • Forsberg, Å, A.-M. Viitanen, M. Skurnik, and H. Wolf-Watz. 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, Å.1    Viitanen, A.-M.2    Skurnik, M.3    Wolf-Watz, H.4
  • 15
    • 0021710132 scopus 로고
    • Genetic analysis of the low calcium response in Yersinia pestis Mud1 (Ap lac) insertion mutants
    • Goguen, J. D., J. Yother, and S. C. Straley. 1984. Genetic analysis of the low calcium response in Yersinia pestis Mud1 (Ap lac) insertion mutants. J. Bacteriol. 160:842-848.
    • (1984) J. Bacteriol. , vol.160 , pp. 842-848
    • Goguen, J.D.1    Yother, J.2    Straley, S.C.3
  • 18
    • 0029930059 scopus 로고    scopus 로고
    • The Yersinia YpkA Ser/Thr kinase is translocated and subsequently targeted to the inner surface of the HeLa cell plasma membrane
    • Håkansson, S., E. E. Galyov, R. Rosqvist, and H. Wolf-Watz. 1996. The Yersinia YpkA Ser/Thr kinase is translocated and subsequently targeted to the inner surface of the HeLa cell plasma membrane. Mol. Microbiol. 20: 593-603.
    • (1996) Mol. Microbiol. , vol.20 , pp. 593-603
    • Håkansson, S.1    Galyov, E.E.2    Rosqvist, R.3    Wolf-Watz, H.4
  • 19
    • 0029908022 scopus 로고    scopus 로고
    • The YopB protein of Yersinia pseudotuberculosis is essential for translocation of Yop effector proteins across the target cell plasma membrane and displays contact-dependent membrane-disrupting activity
    • Håkansson, S., C. Persson, K. Schesser, E. E. Galyov, R. Rosqvist, and H. Wolf-Watz. 1996. The YopB protein of Yersinia pseudotuberculosis is essential for translocation of Yop effector proteins across the target cell plasma membrane and displays contact-dependent membrane-disrupting activity. EMBO J. 15:5812-5823.
    • (1996) EMBO J. , vol.15 , pp. 5812-5823
    • Håkansson, S.1    Persson, C.2    Schesser, K.3    Galyov, E.E.4    Rosqvist, R.5    Wolf-Watz, H.6
  • 20
    • 0020959710 scopus 로고
    • Studies on transformation of E. coli with plasmids
    • Hanahan, D. 1983. Studies on transformation of E. coli with plasmids. J. Mol. Biol. 166:557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 21
    • 0027930194 scopus 로고
    • Essential role of YopD in inhibition of the respiratory burst of macrophages by Yersinia enterocolitica
    • Hartland, E. L., S. P. Green, W. A. Philips, and R. M. Robins-Browne. 1994. Essential role of YopD in inhibition of the respiratory burst of macrophages by Yersinia enterocolitica. Infect. Immun. 62:4445-4453.
    • (1994) Infect. Immun. , vol.62 , pp. 4445-4453
    • Hartland, E.L.1    Green, S.P.2    Philips, W.A.3    Robins-Browne, R.M.4
  • 22
    • 0029967338 scopus 로고    scopus 로고
    • Contributions of YopB to virulence of Yersinia enterocolitica
    • Hartland, E. L., A.-M. Bordun, and R. M. Robins-Browne. 1996. Contributions of YopB to virulence of Yersinia enterocolitica. Infect. Immun. 64:2308-2314.
    • (1996) Infect. Immun. , vol.64 , pp. 2308-2314
    • Hartland, E.L.1    Bordun, A.-M.2    Robins-Browne, R.M.3
  • 23
    • 0001823786 scopus 로고
    • Recombinant PCR
    • M. A. Innis, D. H. Gelfand, J. J. Sninsky, and T. J. White (ed.), Academic Press, San Diego, Calif
    • Higuchi, R. 1990. Recombinant PCR, p. 177-183. In M. A. Innis, D. H. Gelfand, J. J. Sninsky, and T. J. White (ed.), PCR protocols: a guide to methods and applications. Academic Press, San Diego, Calif.
    • (1990) PCR Protocols: A Guide to Methods and Applications , pp. 177-183
    • Higuchi, R.1
  • 24
    • 0027141070 scopus 로고
    • Temperature sensing in Yersinia pestis: Translation of the LcrF activator protein is thermally regulated
    • Hoe, N. P., and J. D. Goguen. 1993. Temperature sensing in Yersinia pestis: translation of the LcrF activator protein is thermally regulated. J. Bacteriol. 175:7901-7909.
    • (1993) J. Bacteriol. , vol.175 , pp. 7901-7909
    • Hoe, N.P.1    Goguen, J.D.2
  • 26
    • 0027724892 scopus 로고
    • Sensing structural intermediates in bacterial flagellar assembly by export of a negative regulator
    • Hughes, K. T., K. L. Gillen, M. J. Semon, and J. E. Karlinsey. 1993. Sensing structural intermediates in bacterial flagellar assembly by export of a negative regulator. Science 262:1277-1280.
    • (1993) Science , vol.262 , pp. 1277-1280
    • Hughes, K.T.1    Gillen, K.L.2    Semon, M.J.3    Karlinsey, J.E.4
  • 27
    • 0028284750 scopus 로고
    • Excretion of the anti-sigma factor through a flagellar structure couples flagellar gene expression with flagellar assembly in Salmonella typhimurium
    • Kutsukake, K. 1994. Excretion of the anti-sigma factor through a flagellar structure couples flagellar gene expression with flagellar assembly in Salmonella typhimurium. Mol. Gen. Genet. 243:605-612.
    • (1994) Mol. Gen. Genet. , vol.243 , pp. 605-612
    • Kutsukake, K.1
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 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
  • 29
    • 0026542646 scopus 로고
    • Role of the transcriptional activator VirF in the expression of the pYV plasmid genes of Yersinia enterocolitica
    • Lambert de Rouvroit, C., C. Sluiters, and G. R. Cornelis. 1992. Role of the transcriptional activator VirF 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
  • 30
    • 0030998981 scopus 로고    scopus 로고
    • Type III secretion systems: Machines to deliver bacterial proteins into eukaryotic cells?
    • Lee, C. A. 1997. Type III secretion systems: machines to deliver bacterial proteins into eukaryotic cells? Trends Microbiol. 5:148-156.
    • (1997) Trends Microbiol. , vol.5 , pp. 148-156
    • Lee, C.A.1
  • 31
    • 0028837276 scopus 로고
    • PCR mapping of integrons reveals several novel combinations of resistance genes
    • Levesque, C., L. Piche, L. Chantal, and P. H. Roy. 1995. PCR mapping of integrons reveals several novel combinations of resistance genes. Antimicrob. Agents Chemother. 39:185-191.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 185-191
    • Levesque, C.1    Piche, L.2    Chantal, L.3    Roy, P.H.4
  • 32
    • 0025358996 scopus 로고
    • Yersinia pestis pH 6 antigen: Genetic, biochemical, and virulence characterization of a protein involved in the pathogenesis of bubonic plague
    • Lindler, L. E., M. S. Klempner, and S. C. Straley. 1990. Yersinia pestis pH 6 antigen: genetic, biochemical, and virulence characterization of a protein involved in the pathogenesis of bubonic plague. Infect. Immun. 58:2569-2577.
    • (1990) Infect. Immun. , vol.58 , pp. 2569-2577
    • Lindler, L.E.1    Klempner, M.S.2    Straley, S.C.3
  • 33
    • 0000887786 scopus 로고    scopus 로고
    • Flagella and motility
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), ASM Press, Washington, D.C
    • Macnab, R. M. 1996. Flagella and motility, p. 123-145. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. ASM Press, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. , pp. 123-145
    • Macnab, R.M.1
  • 34
    • 0023892552 scopus 로고
    • A novel suicide vector and its use in construction of insertion mutations: Osmoregulation of outer membrane proteins and virulence determinants in Vibrio cholerae requires toxR
    • Miller, V. L., and J. J. Mekalanos. 1988: A novel suicide vector and its use in construction of insertion mutations: osmoregulation of outer membrane proteins and virulence determinants in Vibrio cholerae requires toxR. J Bacteriol. 170:2575-2583.
    • (1988) J Bacteriol. , vol.170 , pp. 2575-2583
    • Miller, V.L.1    Mekalanos, J.J.2
  • 35
    • 0027584038 scopus 로고
    • Overcoming inclusion body formation in a high-level expression system
    • Moore, J. T., A. Uppal, F. Maley, and G. F. Maley. 1993. Overcoming inclusion body formation in a high-level expression system. Protein Expr. Purif. 4:160-163.
    • (1993) Protein Expr. Purif. , vol.4 , pp. 160-163
    • Moore, J.T.1    Uppal, A.2    Maley, F.3    Maley, G.F.4
  • 36
    • 0031019824 scopus 로고    scopus 로고
    • Effect of Yersinia pestis YopM on experimental plague
    • Nemeth, J., and S. C. Straley. 1997. Effect of Yersinia pestis YopM on experimental plague. Infect. Immun. 65:924-930.
    • (1997) Infect. Immun. , vol.65 , pp. 924-930
    • Nemeth, J.1    Straley, S.C.2
  • 39
    • 0024992438 scopus 로고
    • Identification and cloning of a hemin storage locus involved in the pigmentation phenotype of Yersinia pestis
    • Perry, R. D., M. Pendrak, and P. Schuetze. 1990. Identification and cloning of a hemin storage locus involved in the pigmentation phenotype of Yersinia pestis. J. Bacteriol. 172:5929-5937.
    • (1990) J. Bacteriol. , vol.172 , pp. 5929-5937
    • Perry, R.D.1    Pendrak, M.2    Schuetze, P.3
  • 40
    • 0031029062 scopus 로고    scopus 로고
    • Yersinia pestis - Etiologic agent of plague
    • Perry, R. D., and J. D. Fetherston. 1997. Yersinia pestis - etiologic agent of plague. Clin. Microbiol. Rev. 10:35-66.
    • (1997) Clin. Microbiol. Rev. , vol.10 , pp. 35-66
    • Perry, R.D.1    Fetherston, J.D.2
  • 41
    • 0028802323 scopus 로고
    • Cell-surface-bound Yersinia translocate the protein tyrosine phosphatase YopH by a polarized mechanism into the target cell
    • Persson, C., R. Nordfelth, N. Holmström, S. Håkansson, R. Rosqvist, and H. Wolf-Watz. 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, N.3    Håkansson, S.4    Rosqvist, R.5    Wolf-Watz, H.6
  • 43
    • 0025840282 scopus 로고
    • LcrD, a membrane-bound regulator of the Yersinia pestis low-calcium response
    • Plano, G. V., S. S. Barve, and S. C. Straley. 1991. LcrD, a membrane-bound regulator of the Yersinia pestis low-calcium response. J. Bacteriol. 173:7293-7303.
    • (1991) J. Bacteriol. , vol.173 , pp. 7293-7303
    • Plano, G.V.1    Barve, S.S.2    Straley, S.C.3
  • 44
    • 0027297680 scopus 로고
    • Multiple effects of lcrD mutations in Yersinia pestis
    • Plano, G. V., and S. C. Straley. 1993. Multiple effects of lcrD mutations in Yersinia pestis. J. Bacteriol. 175:3536-3545.
    • (1993) J. Bacteriol. , vol.175 , pp. 3536-3545
    • Plano, G.V.1    Straley, S.C.2
  • 45
    • 0029039020 scopus 로고
    • Mutations in yscC, yscD, and yscG prevent high-level expression and secretion of V antigen and Yops in Yersinia pestis
    • Plano, G. V., and S. C. Straley. 1995. Mutations in yscC, yscD, and yscG prevent high-level expression and secretion of V antigen and Yops in Yersinia pestis. J. Bacteriol. 177:3843-3854.
    • (1995) J. Bacteriol. , vol.177 , pp. 3843-3854
    • Plano, G.V.1    Straley, S.C.2
  • 47
    • 0024437782 scopus 로고
    • Molecular analysis of lcrGVH, the V antigen operon of Yersinia pestis
    • 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. 171:5646-5653.
    • (1989) J. Bacteriol. , vol.171 , pp. 5646-5653
    • Price, S.B.1    Leung, K.Y.2    Barve, S.S.3    Straley, S.C.4
  • 48
    • 0024604790 scopus 로고
    • lcrH, a gene necessary for virulence of Yersinia pestis and for the normal response of Y. pestis to ATP and calcium
    • Price, S. B., and S. C. Straley. 1989. lcrH, a gene necessary for virulence of Yersinia pestis and for the normal response of Y. pestis to ATP and calcium. Infect. Immun. 57:1491-1498.
    • (1989) Infect. Immun. , vol.57 , pp. 1491-1498
    • Price, S.B.1    Straley, S.C.2
  • 49
    • 17744415944 scopus 로고
    • Detection and characterization of Yersinia pestis plasmids determining pesticin I, fraction I antigen and mouse toxin synthesis
    • Protsenko, O. A., P. I. Anisimov, O. T. Mozharov, N. P. Konnov, Y. A. Popov, and A. M. Kokookshkin. 1983. Detection and characterization of Yersinia pestis plasmids determining pesticin I, fraction I antigen and mouse toxin synthesis. Genetika 19:1081-1090.
    • (1983) Genetika , vol.19 , pp. 1081-1090
    • Protsenko, O.A.1    Anisimov, P.I.2    Mozharov, O.T.3    Konnov, N.P.4    Popov, Y.A.5    Kokookshkin, A.M.6
  • 50
    • 0026772670 scopus 로고
    • A novel protein, LcrQ, involved in the low-calcium response of Yersinia pseudotuberculosis, shows extensive homology to YopH
    • Rimpiläinen, M., Å. Forsberg, and H. Wolf-Watz. 1992. A novel protein, LcrQ, involved in the low-calcium response of Yersinia pseudotuberculosis, shows extensive homology to YopH. J. Bacteriol. 174:3355-3363.
    • (1992) J. Bacteriol. , vol.174 , pp. 3355-3363
    • Rimpiläinen, M.1    Forsberg, Å.2    Wolf-Watz, H.3
  • 51
    • 0027982852 scopus 로고
    • Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells
    • Rosqvist, R., K.-E. Magnusson, and H. Wolf-Watz. 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
  • 52
    • 0027434697 scopus 로고
    • Membrane traffic wardens and protein secretion in Gram-negative bacteria
    • Salmond, G. P. C., and P. J. Reeves. 1993. Membrane traffic wardens and protein secretion in Gram-negative bacteria. Trends Biochem. Sci. 18:7-12.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 7-12
    • Salmond, G.P.C.1    Reeves, P.J.2
  • 54
    • 0027420061 scopus 로고
    • New suicide vector for gene replacement in yersiniae and other gram-negative bacteria
    • Skrzypek, E., P. L. Haddix, G. V. Plano, and S. C. Straley. 1993. New suicide vector for gene replacement in yersiniae and other gram-negative bacteria. Plasmid 29:160-163.
    • (1993) Plasmid , vol.29 , pp. 160-163
    • Skrzypek, E.1    Haddix, P.L.2    Plano, G.V.3    Straley, S.C.4
  • 55
    • 0027229148 scopus 로고
    • LcrG, a secreted protein involved in negative regulation of the low-calcium response in Yersinia pestis
    • Skrzypek, E., and S. C. Straley. 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
    • Skrzypek, E.1    Straley, S.C.2
  • 56
    • 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
  • 57
    • 0023715723 scopus 로고
    • Genetic analysis of the 9.5-kilobase virulence plasmid of Yersinia pestis
    • Sodeinde, O. A., and J. D. Goguen. 1988. Genetic analysis of the 9.5-kilobase virulence plasmid of Yersinia pestis. Infect. Immun. 56:2743-2748.
    • (1988) Infect. Immun. , vol.56 , pp. 2743-2748
    • Sodeinde, O.A.1    Goguen, J.D.2
  • 58
    • 0028105015 scopus 로고
    • Translocation of a hybrid YopE-adenylate cyclase from Yersinia enterocolitica into HeLa cells
    • Sory, M.-P., and G. R. Cornells. 1994. Translocation of a hybrid YopE-adenylate cyclase from Yersinia enterocolitica into HeLa cells. Mol. Microbiol. 14:583-594.
    • (1994) Mol. Microbiol. , vol.14 , pp. 583-594
    • Sory, M.-P.1    Cornells, G.R.2
  • 59
    • 0022629859 scopus 로고
    • 2+ in Yersinia pestis include structural genes for outer membrane proteins
    • 2+ in Yersinia pestis include structural genes for outer membrane proteins. Infect. Immun. 51:445-454.
    • (1986) Infect. Immun. , vol.51 , pp. 445-454
    • Straley, S.C.1    Bowmen, W.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.