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Volumn 40, Issue 1, 2005, Pages 152-163

Yersinia pestis outer membrane type III secretion protein YscC: Expression, purification, characterization, and induction of specific antiserum

Author keywords

His tag; Intein; Type III secretion; Yersinia pestis; yscC

Indexed keywords

BACTERIA (MICROORGANISMS); EUKARYOTA; YERSINIA PESTIS;

EID: 13844296633     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2004.11.001     Document Type: Article
Times cited : (13)

References (31)
  • 1
    • 0036322385 scopus 로고    scopus 로고
    • Yersinia type III secretion: Send in the effectors
    • G.R. Cornelis Yersinia type III secretion: send in the effectors J. Cell Biol. 158 2002 401 408
    • (2002) J. Cell Biol. , vol.158 , pp. 401-408
    • Cornelis, G.R.1
  • 2
    • 0036192725 scopus 로고    scopus 로고
    • The Yersinia Ysc-Yop virulence apparatus
    • G.R. Cornelis The Yersinia Ysc-Yop virulence apparatus Int. J. Med. Microbiol. 291 2002 455 462
    • (2002) Int. J. Med. Microbiol. , vol.291 , pp. 455-462
    • Cornelis, G.R.1
  • 3
    • 0034254928 scopus 로고    scopus 로고
    • Molecular and cell biology aspects of plague
    • G.R. Cornelis Molecular and cell biology aspects of plague Proc. Natl. Acad. Sci. USA 97 2000 8778 8783
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8778-8783
    • Cornelis, G.R.1
  • 4
    • 0034194011 scopus 로고    scopus 로고
    • Type III machines of gram-negative bacteria: Delivering the goods
    • L.W. Cheng, and O. Schneewind Type III machines of gram-negative bacteria: delivering the goods Trends Microbiol. 8 2000 214 220
    • (2000) Trends Microbiol. , vol.8 , pp. 214-220
    • Cheng, L.W.1    Schneewind, O.2
  • 5
    • 3042812521 scopus 로고    scopus 로고
    • Structure and electrophysiological properties of the YscC secretin from the type III secretion system of Yersinia enterocolitica
    • P. Burghout, R. Van Boxtel, P. Van Gelder, P. Ringler, S.A. Muller, J. Tommassen, and M. Koster Structure and electrophysiological properties of the YscC secretin from the type III secretion system of Yersinia enterocolitica J. Bacteriol. 186 2004 4645 4654
    • (2004) J. Bacteriol. , vol.186 , pp. 4645-4654
    • Burghout, P.1    Van Boxtel, R.2    Van Gelder, P.3    Ringler, P.4    Muller, S.A.5    Tommassen, J.6    Koster, M.7
  • 6
    • 0029039020 scopus 로고
    • Mutations in yscC, yscD, and yscG prevent high-level expression and secretion of V antigen and Yops in Yersinia pestis
    • G.V. Plano, and S.C. Straley Mutations in yscC, yscD, and yscG prevent high-level expression and secretion of V antigen and Yops in Yersinia pestis J. Bacteriol. 177 1995 3843 3854
    • (1995) J. Bacteriol. , vol.177 , pp. 3843-3854
    • Plano, G.V.1    Straley, S.C.2
  • 8
    • 0030716279 scopus 로고    scopus 로고
    • The outer membrane component, YscC, of the Yop secretion machinery of Yersinia enterocolitica forms a ring-shaped multimeric complex
    • M. Koster, W. Bitter, H. de Cock, A. Allaoui, G.R. Cornelis, and J. Tommassen The outer membrane component, YscC, of the Yop secretion machinery of Yersinia enterocolitica forms a ring-shaped multimeric complex Mol. Microbiol. 26 1997 789 798
    • (1997) Mol. Microbiol. , vol.26 , pp. 789-798
    • Koster, M.1    Bitter, W.2    De Cock, H.3    Allaoui, A.4    Cornelis, G.R.5    Tommassen, J.6
  • 9
    • 20444384137 scopus 로고
    • Guide for the care and use of laboratory animals
    • Institute of Laboratory Animal Resources. U.S. Department of Health and Human Services, Bethesda
    • National Research Council, Institute of Laboratory Animal Resources. Guide for the care and use of laboratory animals. U.S. Department of Health and Human Services Publication No. (NIH) 86-23. U.S. Department of Health and Human Services, Bethesda, 1986
    • (1986) U.S. Department of Health and Human Services Publication No. (NIH) 86-23
  • 10
    • 0029422177 scopus 로고
    • Studies on the contribution of the F1 capsule-associated plasmid pFra to the virulence of Yersinia pestis
    • S.L. Welkos, K.M. Davis, L.M. Pitt, P.L. Worsham, and A.M. Freidlander Studies on the contribution of the F1 capsule-associated plasmid pFra to the virulence of Yersinia pestis Contrib. Microbiol. Immunol. 13 1995 299 305
    • (1995) Contrib. Microbiol. Immunol. , vol.13 , pp. 299-305
    • Welkos, S.L.1    Davis, K.M.2    Pitt, L.M.3    Worsham, P.L.4    Freidlander, A.M.5
  • 11
    • 0346997965 scopus 로고    scopus 로고
    • Mu dI1(Ap lac) mutagenesis of Yersinia pestis plasmid pFra and identification of temperature-regulated loci associated with virulence
    • S.L. Welkos, G.P. Andrews, L.E. Lindler, N.J. Snellings, and S.D. Strachan Mu dI1(Ap lac) mutagenesis of Yersinia pestis plasmid pFra and identification of temperature-regulated loci associated with virulence Plasmid 51 2004 1 11
    • (2004) Plasmid , vol.51 , pp. 1-11
    • Welkos, S.L.1    Andrews, G.P.2    Lindler, L.E.3    Snellings, N.J.4    Strachan, S.D.5
  • 13
    • 0026650189 scopus 로고
    • Structure and regulation of the Yersinia pestis yscBCDEF operon
    • P.L. Haddix, and S.C. Straley Structure and regulation of the Yersinia pestis yscBCDEF operon J. Bacteriol. 174 1992 4820 4828
    • (1992) J. Bacteriol. , vol.174 , pp. 4820-4828
    • Haddix, P.L.1    Straley, S.C.2
  • 14
    • 0033764483 scopus 로고    scopus 로고
    • Assembly and function of type III secretory systems
    • G.R. Cornelis, and F. Van Gijsegem Assembly and function of type III secretory systems Annu. Rev. Microbiol. 54 2000 735 774
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 735-774
    • Cornelis, G.R.1    Van Gijsegem, F.2
  • 15
    • 0029420939 scopus 로고
    • Construction of defined F1 negative mutants of virulent Yersinia pestis
    • P.L. Worsham, M.P. Stein, and S.L. Welkos Construction of defined F1 negative mutants of virulent Yersinia pestis Contrib. Microbiol. Immunol. 13 1995 325 328
    • (1995) Contrib. Microbiol. Immunol. , vol.13 , pp. 325-328
    • Worsham, P.L.1    Stein, M.P.2    Welkos, S.L.3
  • 17
    • 0031750789 scopus 로고    scopus 로고
    • Protection against experimental bubonic and pneumonic plague by a recombinant capsular F1-V antigen fusion protein vaccine
    • D.G. Heath, G.W. Anderson, J.M. Mauro, S.L. Welkos, G.P. Andrews, J. Adamovicz, and A.M. Friedlander Protection against experimental bubonic and pneumonic plague by a recombinant capsular F1-V antigen fusion protein vaccine Vaccine 16 1998 1131 1137
    • (1998) Vaccine , vol.16 , pp. 1131-1137
    • Heath, D.G.1    Anderson, G.W.2    Mauro, J.M.3    Welkos, S.L.4    Andrews, G.P.5    Adamovicz, J.6    Friedlander, A.M.7
  • 19
    • 0034888061 scopus 로고    scopus 로고
    • Overexpression and purification of Helicobacter pylori flavodoxin and induction of a specific antiserum in rabbits
    • R. Paul, F.U. Bosch, and K.P. Schafer Overexpression and purification of Helicobacter pylori flavodoxin and induction of a specific antiserum in rabbits Protein Expr. Purif. 22 2001 399 405
    • (2001) Protein Expr. Purif. , vol.22 , pp. 399-405
    • Paul, R.1    Bosch, F.U.2    Schafer, K.P.3
  • 20
    • 0037615187 scopus 로고    scopus 로고
    • Purification and characterization of the beta-trefoil fold protein barley alpha-amylase/subtilisin inhibitor overexpressed in Escherichia coli
    • B.C. Bonsager, M. Praetorius-Ibba, P.K. Nielsen, and B. Svensson Purification and characterization of the beta-trefoil fold protein barley alpha-amylase/subtilisin inhibitor overexpressed in Escherichia coli Protein Expr. Purif. 30 2003 185 193
    • (2003) Protein Expr. Purif. , vol.30 , pp. 185-193
    • Bonsager, B.C.1    Praetorius-Ibba, M.2    Nielsen, P.K.3    Svensson, B.4
  • 22
    • 3142551364 scopus 로고    scopus 로고
    • Expression cloned cDNA for 10-deacetylbaccatin III-10-O-acetyltransferase in Escherichia coli: A comparative study of three fusion systems
    • J. Fang, and D. Ewald Expression cloned cDNA for 10-deacetylbaccatin III-10-O-acetyltransferase in Escherichia coli: a comparative study of three fusion systems Protein Expr. Purif. 35 2004 17 24
    • (2004) Protein Expr. Purif. , vol.35 , pp. 17-24
    • Fang, J.1    Ewald, D.2
  • 24
    • 0036362061 scopus 로고    scopus 로고
    • Differential effects of supplementary affinity tags on the solubility of MBP fusion proteins
    • K.M. Routzahn, and D.S. Waugh Differential effects of supplementary affinity tags on the solubility of MBP fusion proteins J. Struct. Funct. Genomics 2 2002 83 92
    • (2002) J. Struct. Funct. Genomics , vol.2 , pp. 83-92
    • Routzahn, K.M.1    Waugh, D.S.2
  • 25
    • 3042784498 scopus 로고    scopus 로고
    • Modifying an immunogenic epitope on a therapeutic protein: A step towards an improved system for antibody-directed enzyme prodrug therapy (ADEPT)
    • A. Mayer, S.K. Sharma, B. Tolner, N.P. Minton, D. Purdy, P. Amlot, G. Tharakan, R.H. Begent, and K.A. Chester Modifying an immunogenic epitope on a therapeutic protein: a step towards an improved system for antibody-directed enzyme prodrug therapy (ADEPT) Br. J. Cancer 90 2004 2402 2410
    • (2004) Br. J. Cancer , vol.90 , pp. 2402-2410
    • Mayer, A.1    Sharma, S.K.2    Tolner, B.3    Minton, N.P.4    Purdy, D.5    Amlot, P.6    Tharakan, G.7    Begent, R.H.8    Chester, K.A.9
  • 26
    • 0034283337 scopus 로고    scopus 로고
    • Relative position of the hexahistidine tag effects binding properties of a tumor-associated single-chain Fv construct
    • A. Goel, D. Colcher, J.S. Koo, B.J. Booth, G. Pavlinkova, and S.K. Batra Relative position of the hexahistidine tag effects binding properties of a tumor-associated single-chain Fv construct Biochim. Biophys. Acta 1523 2000 13 20
    • (2000) Biochim. Biophys. Acta , vol.1523 , pp. 13-20
    • Goel, A.1    Colcher, D.2    Koo, J.S.3    Booth, B.J.4    Pavlinkova, G.5    Batra, S.K.6
  • 28
    • 0031874403 scopus 로고    scopus 로고
    • Determination of protein-protein interactions by matrix-assisted laser desorption/ionization mass spectrometry
    • T.B. Farmer, and R.M. Caprioli Determination of protein-protein interactions by matrix-assisted laser desorption/ionization mass spectrometry J. Mass. Spectrom. 33 1998 697 704
    • (1998) J. Mass. Spectrom. , vol.33 , pp. 697-704
    • Farmer, T.B.1    Caprioli, R.M.2
  • 29
    • 0036467351 scopus 로고    scopus 로고
    • Yersinia enterocolitica evasion of the host innate immune response by V antigen-induced IL-10 production of macrophages is abrogated in IL-10-deficient mice
    • A. Sing, A. Roggenkamp, A.M. Geiger, and J. Heesemann Yersinia enterocolitica evasion of the host innate immune response by V antigen-induced IL-10 production of macrophages is abrogated in IL-10-deficient mice J. Immunol. 168 2002 1315 1321
    • (2002) J. Immunol. , vol.168 , pp. 1315-1321
    • Sing, A.1    Roggenkamp, A.2    Geiger, A.M.3    Heesemann, J.4
  • 31
    • 85030828681 scopus 로고    scopus 로고
    • Potency, stability, and safety of recombinant Yersinia pestis F1-V fusion protein vaccine as assessed in the mouse model for plague
    • in preparation
    • G.P. Andrews, B.S. Powell, C. Bolt, S.L. Welkos, J.J. Adamovicz, Potency, stability, and safety of recombinant Yersinia pestis F1-V fusion protein vaccine as assessed in the mouse model for plague, Vaccine, in preparation
    • Vaccine
    • Andrews, G.P.1    Powell, B.S.2    Bolt, C.3    Welkos, S.L.4    Adamovicz, J.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.