메뉴 건너뛰기




Volumn 45, Issue 5, 1996, Pages 629-637

Extracellular PagC-HlyA(s) fusion protein for the generation and identification of Salmonella specific antibodies

Author keywords

[No Author keywords available]

Indexed keywords

HYBRID PROTEIN; MONOCLONAL ANTIBODY; OUTER MEMBRANE PROTEIN; SYNTHETIC PEPTIDE; BACTERIAL PROTEIN; BACTERIUM ANTIBODY; ESCHERICHIA COLI PROTEIN; HEMOLYSIN; HLYA PROTEIN, E COLI; MEMBRANE PROTEIN; PAGC PROTEIN, SALMONELLA TYPHIMURIUM;

EID: 0029665415     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002530050740     Document Type: Article
Times cited : (12)

References (35)
  • 1
    • 0026498184 scopus 로고
    • Salmonella typhimurium activates virulence gene transcription within acidified macrophage phagosomes
    • Alpuche Aranda CM, Swanson JA, Loomis WP, Miller SI (1992) Salmonella typhimurium activates virulence gene transcription within acidified macrophage phagosomes. Proc Natl Acad Sci USA 89:10079-10083
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10079-10083
    • Alpuche Aranda, C.M.1    Swanson, J.A.2    Loomis, W.P.3    Miller, S.I.4
  • 2
    • 0025079241 scopus 로고
    • A bacterial virulence determinant encodes by lysogenic coliphage 2
    • Barondess JJ, Beckwith J (1990) A bacterial virulence determinant encodes by lysogenic coliphage 2. Nature 346:871-874
    • (1990) Nature , vol.346 , pp. 871-874
    • Barondess, J.J.1    Beckwith, J.2
  • 3
    • 0025346159 scopus 로고
    • Change in the cellular localization of alkaline phosphatase by alteration of its carboxy-terminal sequence
    • Gentschev I, Hess J, Goebel W (1990) Change in the cellular localization of alkaline phosphatase by alteration of its carboxy-terminal sequence. Mol Gen Genet 222:211-216
    • (1990) Mol Gen Genet , vol.222 , pp. 211-216
    • Gentschev, I.1    Hess, J.2    Goebel, W.3
  • 4
    • 0026460952 scopus 로고
    • Identification of p60 antibodies in human sera and presentation of this Listerial antigen on the surface of attenuated salmonellae by the HlyB-HlyD secretion system
    • Gentschev I, Sokolovic Z, Köhler S, Krone GF, Hof H, Wagner J, Goebel W (1992) Identification of p60 antibodies in human sera and presentation of this Listerial antigen on the surface of attenuated salmonellae by the HlyB-HlyD secretion system. Infect Immun 60:5091-5098
    • (1992) Infect Immun , vol.60 , pp. 5091-5098
    • Gentschev, I.1    Sokolovic, Z.2    Köhler, S.3    Krone, G.F.4    Hof, H.5    Wagner, J.6    Goebel, W.7
  • 5
    • 0020415823 scopus 로고
    • Cloning and functional characterization of the plasmid-encoded hemolysin determinant of Escherichia coli
    • Goebel W, Hedgpeth J (1982) Cloning and functional characterization of the plasmid-encoded hemolysin determinant of Escherichia coli. J Bacteriol 151:1290-1298
    • (1982) J Bacteriol , vol.151 , pp. 1290-1298
    • Goebel, W.1    Hedgpeth, J.2
  • 7
    • 0026537238 scopus 로고
    • The Salmonella typhimurium virulence plasmid complement resistance gene rck is homologous to a family of virulence-related outer membrane protein genes, including pagC and ail
    • Heffernan EJ, Harwood J, Fierer J, Guiney D (1992) The Salmonella typhimurium virulence plasmid complement resistance gene rck is homologous to a family of virulence-related outer membrane protein genes, including pagC and ail. J. Bacteriol 174:84-91
    • (1992) J. Bacteriol , vol.174 , pp. 84-91
    • Heffernan, E.J.1    Harwood, J.2    Fierer, J.3    Guiney, D.4
  • 8
    • 0025605708 scopus 로고
    • Analysis of the haemolysin secretion system by PhoA-HlyA fusion proteins
    • Hess J, Gentschev I, Goebel W, Jarchau T (1990) Analysis of the haemolysin secretion system by PhoA-HlyA fusion proteins. Mol Gen Genet 224:201-208
    • (1990) Mol Gen Genet , vol.224 , pp. 201-208
    • Hess, J.1    Gentschev, I.2    Goebel, W.3    Jarchau, T.4
  • 9
    • 0022481284 scopus 로고
    • Electroelution of fixed and stained membrane proteins from preparative SDS-polyacrylamide gels into a membrane trap
    • Jacobs E, Clad A (1986) Electroelution of fixed and stained membrane proteins from preparative SDS-polyacrylamide gels into a membrane trap. Anal Biochem 154:583-589
    • (1986) Anal Biochem , vol.154 , pp. 583-589
    • Jacobs, E.1    Clad, A.2
  • 10
    • 0028019381 scopus 로고
    • Selection for transport competence of C-terminal polypeptides from Escherichia coli hemolysin: The shortest peptide capable of autonomous HlyB/HlyD-dependent secretion comprises the 62 C-terminal amino acids of HlyA
    • Jarchau T, Chakraborty T, Garcia F, Goebel W (1994) Selection for transport competence of C-terminal polypeptides from Escherichia coli hemolysin: the shortest peptide capable of autonomous HlyB/HlyD-dependent secretion comprises the 62 C-terminal amino acids of HlyA. Mol Gen Genet 245:53-60
    • (1994) Mol Gen Genet , vol.245 , pp. 53-60
    • Jarchau, T.1    Chakraborty, T.2    Garcia, F.3    Goebel, W.4
  • 11
    • 0000092473 scopus 로고
    • Hybridomas and monoclonal antibodies
    • Paul WE (ed) Raven Press, New York
    • Kearny JF (1984) Hybridomas and monoclonal antibodies. Paul WE (ed) Fundamental immunology. Raven Press, New York, pp 751-756
    • (1984) Fundamental Immunology , pp. 751-756
    • Kearny, J.F.1
  • 12
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157:105-132
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 13
    • 0024386073 scopus 로고
    • Isolation and analysis of the C-terminal signal directing the export of Escherichia coli haemolysin protein across both bacterial membranes
    • Koronakis V, Koronakis E, Hughes C (1989) Isolation and analysis of the C-terminal signal directing the export of Escherichia coli haemolysin protein across both bacterial membranes. EMBO J 8:595-605
    • (1989) EMBO J , vol.8 , pp. 595-605
    • Koronakis, V.1    Koronakis, E.2    Hughes, C.3
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 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
  • 15
    • 0023158054 scopus 로고
    • Mutations affecting activity and transport of hemolysin in Escherichia coli
    • Ludwig A, Vogel M, Goebel W (1987) Mutations affecting activity and transport of hemolysin in Escherichia coli. Mol Gen Genet 206:238-245
    • (1987) Mol Gen Genet , vol.206 , pp. 238-245
    • Ludwig, A.1    Vogel, M.2    Goebel, W.3
  • 16
    • 0023411758 scopus 로고
    • Release of a chimeric protein into the medium from Escherichia coli using the C-terminal signal of hemolysin
    • Mackman N, Baker K, Gray L, Haigh R, Nicaud J-M, Holland IB (1987) Release of a chimeric protein into the medium from Escherichia coli using the C-terminal signal of hemolysin. EMBO J 6:2835-2841
    • (1987) EMBO J , vol.6 , pp. 2835-2841
    • Mackman, N.1    Baker, K.2    Gray, L.3    Haigh, R.4    Nicaud, J.-M.5    Holland, I.B.6
  • 17
    • 0024537074 scopus 로고
    • Coordinate regulation and sensory transduction in the control of bacterial virulence
    • Miller JF, Mekalanos JJ, Falkow S (1989) Coordinate regulation and sensory transduction in the control of bacterial virulence. Science 243:916-922
    • (1989) Science , vol.243 , pp. 916-922
    • Miller, J.F.1    Mekalanos, J.J.2    Falkow, S.3
  • 19
    • 0025733456 scopus 로고
    • PhoP/PhoQ: Macrophage-specific modulators of Samonella virulence
    • Miller SI (1991) PhoP/PhoQ: macrophage-specific modulators of Samonella virulence. Mol Microbiol 5:2073-2078
    • (1991) Mol Microbiol , vol.5 , pp. 2073-2078
    • Miller, S.I.1
  • 20
    • 0003582512 scopus 로고
    • A two-component regulatory system (phoP-phoQ) controls Salmonella typhimurium virulence
    • Miller SI, Kukral AM, Mekalanos JJ (1989) A two-component regulatory system (phoP-phoQ) controls Salmonella typhimurium virulence. Proc Natl Acad Sci USA 86:5054-5058
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 5054-5058
    • Miller, S.I.1    Kukral, A.M.2    Mekalanos, J.J.3
  • 21
    • 0025008909 scopus 로고
    • Nucleotide sequence of the Yersinia enterocolitica ail gene and characterization of the Ail protein product
    • Miller VL, Bliska JB, Falkow S (1990) Nucleotide sequence of the Yersinia enterocolitica ail gene and characterization of the Ail protein product. J Bacteriol 172:1062-1069
    • (1990) J Bacteriol , vol.172 , pp. 1062-1069
    • Miller, V.L.1    Bliska, J.B.2    Falkow, S.3
  • 22
    • 0026761743 scopus 로고
    • An unusual payC::TnphoA mutation leads to an invasion- and virulence-defective phenotype in salmonellae
    • Miller VL, Beer KB, Loomis WP, Olson JA, Miller SI (1992) An unusual payC::TnphoA mutation leads to an invasion- and virulence-defective phenotype in salmonellae. Infect Immun 60:3763-3770
    • (1992) Infect Immun , vol.60 , pp. 3763-3770
    • Miller, V.L.1    Beer, K.B.2    Loomis, W.P.3    Olson, J.A.4    Miller, S.I.5
  • 23
    • 8944233065 scopus 로고
    • PhD thesis. University of Würzburg, Germany
    • Mollenkopf, H-J (1995) PhD thesis. University of Würzburg, Germany
    • (1995)
    • Mollenkopf, H.-J.1
  • 24
    • 76549170704 scopus 로고
    • The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts
    • Neu HC, Heppel LA (1965) The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts. J Bacteriol 240:3685-3692
    • (1965) J Bacteriol , vol.240 , pp. 3685-3692
    • Neu, H.C.1    Heppel, L.A.2
  • 25
    • 0026051251 scopus 로고
    • A Salmonella typhimurium virulence protein is similar to a Yersinia enterocolitica invasion protein and a bacteriophage lambda outer membrane protein
    • Pulkkinen WS, Miller SI (1991) A Salmonella typhimurium virulence protein is similar to a Yersinia enterocolitica invasion protein and a bacteriophage lambda outer membrane protein. J Bacteriol 173:86-93
    • (1991) J Bacteriol , vol.173 , pp. 86-93
    • Pulkkinen, W.S.1    Miller, S.I.2
  • 27
    • 0023610908 scopus 로고
    • Cloning of a betalactam resistance determinant of Enterobacter cloacae affecting outer membrane proteins of Enterobacteriaceae
    • Stoorvogel J, Bussel MJAWM van, Tommassen J, Klundert JAM van de (1987) Cloning of a betalactam resistance determinant of Enterobacter cloacae affecting outer membrane proteins of Enterobacteriaceae. FEMS Microbiol Lett 48:277-281
    • (1987) FEMS Microbiol Lett , vol.48 , pp. 277-281
    • Stoorvogel, J.1    Van Bussel, M.J.A.W.M.2    Tommassen, J.3    Van De Klundert, J.A.M.4
  • 29
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76:4350-4354
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 31
    • 0020442864 scopus 로고
    • The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with universal primers
    • Vieira J, Messing J (1982) The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with universal primers. Gene 19:259-268
    • (1982) Gene , vol.19 , pp. 259-268
    • Vieira, J.1    Messing, J.2
  • 32
    • 0023915338 scopus 로고
    • Characterization of a sequence (hlyR) which enhances synthesis and secretion of hemolysin in Escherichia coli
    • Vogel M, Hess J, Then I, Juarez A, Goebel W (1988) Characterization of a sequence (hlyR) which enhances synthesis and secretion of hemolysin in Escherichia coli. Mol Gen Genet 212:76-84
    • (1988) Mol Gen Genet , vol.212 , pp. 76-84
    • Vogel, M.1    Hess, J.2    Then, I.3    Juarez, A.4    Goebel, W.5
  • 33
    • 0020629077 scopus 로고
    • Transport of hemolysin across the outer membrane of 'Escherichia coli requires two functions
    • Wagner W, Vogel M, Goebel W (1983) Transport of hemolysin across the outer membrane of 'Escherichia coli requires two functions. J Bacteriol 154:200-210
    • (1983) J Bacteriol , vol.154 , pp. 200-210
    • Wagner, W.1    Vogel, M.2    Goebel, W.3
  • 34
    • 0025372570 scopus 로고
    • TolC, an Escherichia coli outer membrane protein required for hemolysin secretion
    • Wandersman C, Delepelaire P (1990) TolC, an Escherichia coli outer membrane protein required for hemolysin secretion. Proc Natl Acad Sci USA 87:4776-4780
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4776-4780
    • Wandersman, C.1    Delepelaire, P.2
  • 35
    • 8944238175 scopus 로고
    • PhD thesis. University of Würzburg, Germany
    • Weig M (1994) PhD thesis. University of Würzburg, Germany
    • (1994)
    • Weig, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.