메뉴 건너뛰기




Volumn 74, Issue 2, 2006, Pages 1381-1386

Calcium-regulated type III secretion of Yop proteins by an Escherichia coli hha mutant carrying a Yersinia pestis pCD1 virulence plasmid

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PROTEIN YOP; UNCLASSIFIED DRUG;

EID: 31844454263     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.74.2.1381-1386.2006     Document Type: Article
Times cited : (23)

References (37)
  • 1
    • 0029997802 scopus 로고    scopus 로고
    • Complementation of the hha mutation in Escherichia coli by the ymoA gene from Yersinia enterocolitica: Dependence on the gene dosage
    • Balsalobre, C., A. Juarez, C. Madrid, M. Mourino, A. Prenafeta, and F. J. Munoa. 1996. Complementation of the hha mutation in Escherichia coli by the ymoA gene from Yersinia enterocolitica: dependence on the gene dosage. Microbiology 142:1841-1846.
    • (1996) Microbiology , vol.142 , pp. 1841-1846
    • Balsalobre, C.1    Juarez, A.2    Madrid, C.3    Mourino, M.4    Prenafeta, A.5    Munoa, F.J.6
  • 2
    • 0019503719 scopus 로고
    • Essential virulence determinants of different Yersinia species are carried on a common plasmid
    • Ben-Gurion, R., and A. Shafferman. 1981. Essential virulence determinants of different Yersinia species are carried on a common plasmid. Plasmid 5:183-187.
    • (1981) Plasmid , vol.5 , pp. 183-187
    • Ben-Gurion, R.1    Shafferman, A.2
  • 4
    • 0033943054 scopus 로고    scopus 로고
    • LcrQ/YscM1, regulators of the Yersinia yop virulon, are injected into host cells by a chaperone-dependent mechanism
    • Cambronne, E. D., L. W. Cheng, and O. Schneewind. 2000. LcrQ/YscM1, regulators of the Yersinia yop virulon, are injected into host cells by a chaperone-dependent mechanism. Mol. Microbiol. 37:263-273.
    • (2000) Mol. Microbiol. , vol.37 , pp. 263-273
    • Cambronne, E.D.1    Cheng, L.W.2    Schneewind, O.3
  • 5
    • 0034536362 scopus 로고    scopus 로고
    • An investigation into the pathogenic properties of Escherichia coli strains BLR, BL21, DH5α and EQ1
    • Chart, H., H. R. Smith, R. M. La Ragione, and M. J. Woodward. 2000. An investigation into the pathogenic properties of Escherichia coli strains BLR, BL21, DH5α and EQ1. J. Appl. Microbiol. 89:1048-1058.
    • (2000) J. Appl. Microbiol. , vol.89 , pp. 1048-1058
    • Chart, H.1    Smith, H.R.2    La Ragione, R.M.3    Woodward, M.J.4
  • 6
    • 0034254928 scopus 로고    scopus 로고
    • Molecular and cell biology aspects of plague
    • Cornelis, G. R. 2000. Molecular and cell biology aspects of plague. Proc. Natl. Acad. Sci. USA 97:8778-8783.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8778-8783
    • Cornelis, G.R.1
  • 8
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 9
    • 0037241866 scopus 로고    scopus 로고
    • Translocation of YopE and YopN into eukaryotic cells by Yersinia pestis yopN, tyeA, sycN, yscB and lcrG deletion mutants measured using a phosphorylatable peptide tag and phosphospecific antibodies
    • Day, J. B., F. Ferracci, and G. V. Plano. 2003. Translocation of YopE and YopN into eukaryotic cells by Yersinia pestis yopN, tyeA, sycN, yscB and lcrG deletion mutants measured using a phosphorylatable peptide tag and phosphospecific antibodies. Mol. Microbiol. 47:807-823.
    • (2003) Mol. Microbiol. , vol.47 , pp. 807-823
    • Day, J.B.1    Ferracci, F.2    Plano, G.V.3
  • 10
    • 0038209026 scopus 로고    scopus 로고
    • The ttsA gene is required for low-calcium-induced type III secretion of Yop proteins and virulence of Yersinia enterocolitica W22703
    • DeBord, K. L., N. S. Galanopoulos, and O. Schneewind. 2003. The ttsA gene is required for low-calcium-induced type III secretion of Yop proteins and virulence of Yersinia enterocolitica W22703. J. Bacteriol. 185:3499-3507.
    • (2003) J. Bacteriol. , vol.185 , pp. 3499-3507
    • DeBord, K.L.1    Galanopoulos, N.S.2    Schneewind, O.3
  • 11
    • 0026462958 scopus 로고
    • The Hha protein from Escherichia coli is highly homologous to the YmoA protein from Yersinia enterocolitica
    • de la Cruz, F., M. Carmona, and A. Juarez. 1992. The Hha protein from Escherichia coli is highly homologous to the YmoA protein from Yersinia enterocolitica. Mol. Microbiol. 6:3451-3452.
    • (1992) Mol. Microbiol. , vol.6 , pp. 3451-3452
    • De La Cruz, F.1    Carmona, M.2    Juarez, A.3
  • 12
    • 0029148784 scopus 로고
    • SecYEG and SecA are the stoichiometric components of preprotein translocase
    • Douville, K., A. Price, J. Eichler, A. Economou, and W. Wickner. 1995. SecYEG and SecA are the stoichiometric components of preprotein translocase. J. Biol. Chem. 270:20106-20111.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20106-20111
    • Douville, K.1    Price, A.2    Eichler, J.3    Economou, A.4    Wickner, W.5
  • 13
    • 10344249890 scopus 로고    scopus 로고
    • Process of protein transport by the type III secretion system
    • Ghosh, P. 2004. Process of protein transport by the type III secretion system. Microbiol. Mol. Biol. Rev. 68:771-795.
    • (2004) Microbiol. Mol. Biol. Rev. , vol.68 , pp. 771-795
    • Ghosh, P.1
  • 14
    • 0024811752 scopus 로고
    • Genetics of proteolysis in Escherichia coli
    • Gottesman, S. 1989. Genetics of proteolysis in Escherichia coli. Annu. Rev. Genet. 23:163-198.
    • (1989) Annu. Rev. Genet. , vol.23 , pp. 163-198
    • Gottesman, S.1
  • 15
    • 0036078539 scopus 로고    scopus 로고
    • Role of Yops and adhesins in resistance of Yersinia enterocolitica to phagocytosis
    • Grosdent, N., I. Maridonneau-Parini, M. P. Sory, and G. R. Cornelis. 2002. Role of Yops and adhesins in resistance of Yersinia enterocolitica to phagocytosis. Infect. Immun. 70:4165-4176.
    • (2002) Infect. Immun. , vol.70 , pp. 4165-4176
    • Grosdent, N.1    Maridonneau-Parini, I.2    Sory, M.P.3    Cornelis, G.R.4
  • 16
    • 0000070148 scopus 로고    scopus 로고
    • A cloned Erwinia chrysanthemi Hrp (type III protein secretion) system functions in Escherichia coli to deliver Pseudomonas syringae Avr signals to plant cells and to secrete Avr proteins in culture
    • Ham, J. H., D. W. Bauer, D. E. Fouts, and A. Collmer. 1998. A cloned Erwinia chrysanthemi Hrp (type III protein secretion) system functions in Escherichia coli to deliver Pseudomonas syringae Avr signals to plant cells and to secrete Avr proteins in culture. Proc. Natl. Acad. Sci. USA 95:10206-10211.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10206-10211
    • Ham, J.H.1    Bauer, D.W.2    Fouts, D.E.3    Collmer, A.4
  • 17
    • 0023013754 scopus 로고
    • Immunochemical analysis of plasmid-encoded proteins released by enteropathogenic Yersinia sp. grown in calcium-deficient media
    • Heesemann, J., U. Gross, N. Schmidt, and R. Laufs. 1986. Immunochemical analysis of plasmid-encoded proteins released by enteropathogenic Yersinia sp. grown in calcium-deficient media. Infect. Immun. 54:561-567.
    • (1986) Infect. Immun. , vol.54 , pp. 561-567
    • Heesemann, J.1    Gross, U.2    Schmidt, N.3    Laufs, R.4
  • 19
    • 0032871341 scopus 로고    scopus 로고
    • DsbA is required for stable expression of outer membrane protein YscC and for efficient Yop secretion in Yersinia pestis
    • Jackson, M. W., and G. V. Plano. 1999. DsbA is required for stable expression of outer membrane protein YscC and for efficient Yop secretion in Yersinia pestis. J. Bacteriol. 181:5126-5130.
    • (1999) J. Bacteriol. , vol.181 , pp. 5126-5130
    • Jackson, M.W.1    Plano, G.V.2
  • 20
    • 9644301279 scopus 로고    scopus 로고
    • The ATP-dependent ClpXP and Lon proteases regulate expression of the Yersinia pestis type III secretion system via regulated proteolysis of YmoA, a small histone-like protein
    • Jackson, M. W., E. Silva-Herzog, and G. V. Plano. 2004. The ATP-dependent ClpXP and Lon proteases regulate expression of the Yersinia pestis type III secretion system via regulated proteolysis of YmoA, a small histone-like protein. Mol. Microbiol. 54:1364-1378.
    • (2004) Mol. Microbiol. , vol.54 , pp. 1364-1378
    • Jackson, M.W.1    Silva-Herzog, E.2    Plano, G.V.3
  • 21
    • 0019433725 scopus 로고
    • Rapid procedure for detection and isolation of large and small plasmids
    • Kado, C. I., and S. T. Liu. 1981. Rapid procedure for detection and isolation of large and small plasmids. J. Bacteriol. 145:1365-1373.
    • (1981) J. Bacteriol. , vol.145 , pp. 1365-1373
    • Kado, C.I.1    Liu, S.T.2
  • 22
    • 0036197713 scopus 로고    scopus 로고
    • Role of the Hha/YmoA family of proteins in the thermoregulation of the expression of virulence factors
    • Madrid, C., J. M. Nieto, and A. Juarez. 2002. Role of the Hha/YmoA family of proteins in the thermoregulation of the expression of virulence factors. Int. J. Med. Microbiol. 291:425-432.
    • (2002) Int. J. Med. Microbiol. , vol.291 , pp. 425-432
    • Madrid, C.1    Nieto, J.M.2    Juarez, A.3
  • 25
    • 0036174055 scopus 로고    scopus 로고
    • Evidence for direct protein-protein interaction between members of the enterobacterial Hha/YmoA and H-NS families of proteins
    • Nieto, J. M., C. Madrid, E. Miquelay, J. L. Parra, S. Rodrignez, and A. Juarez. 2002. Evidence for direct protein-protein interaction between members of the enterobacterial Hha/YmoA and H-NS families of proteins. J. Bacteriol. 184:629-635.
    • (2002) J. Bacteriol. , vol.184 , pp. 629-635
    • Nieto, J.M.1    Madrid, C.2    Miquelay, E.3    Parra, J.L.4    Rodrignez, S.5    Juarez, A.6
  • 26
    • 0033578923 scopus 로고    scopus 로고
    • Inhibition of the mitogen-activated protein kinase kinase superfamily by a Yersinia effector
    • Orth, K., L. E. Palmer, Z. Q. Bao, S. Stewart, A. E. Rudolph, J. B. Bliska, and J. E. Dixon. 1999. Inhibition of the mitogen-activated protein kinase kinase superfamily by a Yersinia effector. Science 285:1920-1923.
    • (1999) Science , vol.285 , pp. 1920-1923
    • Orth, K.1    Palmer, L.E.2    Bao, Z.Q.3    Stewart, S.4    Rudolph, A.E.5    Bliska, J.B.6    Dixon, J.E.7
  • 27
    • 0031780201 scopus 로고    scopus 로고
    • YopJ of Yersinia pseudotuberculosis is required for the inhibition of macrophage TNF-alpha production and downregulation of the MAP kinases p38 and JNK
    • Palmer, L. E., S. Hobbie, J. E. Galan, and J. B. Bliska. 1998. YopJ of Yersinia pseudotuberculosis is required for the inhibition of macrophage TNF-alpha production and downregulation of the MAP kinases p38 and JNK. Mol. Microbiol. 27:953-965.
    • (1998) Mol. Microbiol. , vol.27 , pp. 953-965
    • Palmer, L.E.1    Hobbie, S.2    Galan, J.E.3    Bliska, J.B.4
  • 29
    • 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, A. Holmstrom, S. Hakansson, 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    Holmstrom, A.3    Hakansson, S.4    Rosqvist, R.5    Wolf-Watz, H.6
  • 31
    • 0026772670 scopus 로고
    • A novel protein, LcrQ, involved in the low-calcium response of Yersinia pseudotuberculosis shows extensive homology to YopH
    • Rimpilainen, M., A. 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
    • Rimpilainen, M.1    Forsberg, A.2    Wolf-Watz, H.3
  • 32
    • 0025788249 scopus 로고
    • Intracellular targeting of the Yersinia YopE cytotoxin in mammalian cells induces actin microfilament disruption
    • Rosqvist, R., A. Forsberg, and H. Wolf-Watz. 1991. Intracellular targeting of the Yersinia YopE cytotoxin in mammalian cells induces actin microfilament disruption. Infect. Immun. 59:4562-4569.
    • (1991) Infect. Immun. , vol.59 , pp. 4562-4569
    • Rosqvist, R.1    Forsberg, A.2    Wolf-Watz, H.3
  • 33
    • 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
  • 34
    • 0031775572 scopus 로고    scopus 로고
    • The yopJ locus is required for Yersinia-mediated inhibition of NF-kappaB activation and cytokine expression: YopJ contains a eukaryotic SH2-like domain that is essential for its repressive activity
    • Schesser, K., A. K. Spiik, J. M. Dukuzumuremyi, M. F. Neurath, S. Pettersson, and H. Wolf-Watz. 1998. The yopJ locus is required for Yersinia-mediated inhibition of NF-kappaB 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
  • 36
    • 17144457298 scopus 로고    scopus 로고
    • Analysis of chaperone-dependent Yop secretion/translocation and effector function using a mini-virulence plasmid of Yersinia enterocolitica
    • Trulzsch, K., A. Roggenkamp, M. Aepfelbacher, G. Wilharm, K. Ruckdeschel, and J. Heesemann. 2003. Analysis of chaperone-dependent Yop secretion/translocation and effector function using a mini-virulence plasmid of Yersinia enterocolitica. Int. J. Med. Microbiol. 293:167-177.
    • (2003) Int. J. Med. Microbiol. , vol.293 , pp. 167-177
    • Trulzsch, K.1    Roggenkamp, A.2    Aepfelbacher, M.3    Wilharm, G.4    Ruckdeschel, K.5    Heesemann, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.