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Volumn 267, Issue 1-2, 2004, Pages 75-82

Reactivity of typhoid patients sera with stress induced 55 kDa phenotype in Salmonella enterica serovar Typhi

Author keywords

Expression; Outermembrane protein; Reactivity; Salmonella typhi; Stress; Typhoid sera

Indexed keywords

CARBOXYLIC ACID; EPITOPE; HEAT SHOCK PROTEIN; INORGANIC ACID; OUTER MEMBRANE PROTEIN;

EID: 9444238528     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:MCBI.0000049367.69142.0b     Document Type: Article
Times cited : (9)

References (42)
  • 1
    • 0026069484 scopus 로고
    • Patterns of morbidity and mortality in typhoid fever dependent on age and gender. Review of 552 hospitalized patients with diarrhea
    • Butler T, Islam A, Kabir I, Jones PK: Patterns of morbidity and mortality in typhoid fever dependent on age and gender. Review of 552 hospitalized patients with diarrhea. Rev Infect Dis 13: 85-90, 1991
    • (1991) Rev. Infect. Dis. , vol.13 , pp. 85-90
    • Butler, T.1    Islam, A.2    Kabir, I.3    Jones, P.K.4
  • 2
    • 0031031511 scopus 로고    scopus 로고
    • Multidrug resistant Salmonella typhi: A worldwide epidemic
    • Rowe B, Ward LR, Threfall EJ: Multidrug resistant Salmonella typhi: A worldwide epidemic. Clin Infect Dis 24: S106-S109, 1997
    • (1997) Clin. Infect. Dis. , vol.24
    • Rowe, B.1    Ward, L.R.2    Threfall, E.J.3
  • 3
    • 0031005010 scopus 로고    scopus 로고
    • Induction and characterization of heat shock proteins of Salmonella typhi and their reactivity with sera from patients with typhoid fever
    • Tang W, Abubakar S, Devi S, Puthucheary S, Pang T: Induction and characterization of heat shock proteins of Salmonella typhi and their reactivity with sera from patients with typhoid fever. Infect Immun 65: 2983-2986, 1997.
    • (1997) Infect. Immun. , vol.65 , pp. 2983-2986
    • Tang, W.1    Abubakar, S.2    Devi, S.3    Puthucheary, S.4    Pang, T.5
  • 4
    • 0029986088 scopus 로고    scopus 로고
    • Role of the acid tolerance response in virulence of Salmonella typhimurium
    • Wilmes-Risenberg MR, Bearson B, Foster JW, Curtiss R: Role of the acid tolerance response in virulence of Salmonella typhimurium. Infect Immun 64: 1085-1092, 1996
    • (1996) Infect. Immun. , vol.64 , pp. 1085-1092
    • Wilmes-Risenberg, M.R.1    Bearson, B.2    Foster, J.W.3    Curtiss, R.4
  • 5
    • 0031717130 scopus 로고    scopus 로고
    • Induction of acid resistance of Salmonella typhimurium by exposure to short chain fatty acids
    • Kwon YM, Ricke SC. Induction of acid resistance of Salmonella typhimurium by exposure to short chain fatty acids. Appl Eviron Microbiol 64: 3458-3463, 1998
    • (1998) Appl. Eviron. Microbiol. , vol.64 , pp. 3458-3463
    • Kwon, Y.M.1    Ricke, S.C.2
  • 7
    • 0024598527 scopus 로고
    • Immune response to the iron-deprivation-induced proteins of Salmonella typhi in typhoid fever
    • Fernandez-Beros ME, Gonzalez C, McInstosh MA, Cabello FC: Immune response to the iron-deprivation-induced proteins of Salmonella typhi in typhoid fever. Infect Immun 57: 1271-1275, 1989
    • (1989) Infect. Immun. , vol.57 , pp. 1271-1275
    • Fernandez-Beros, M.E.1    Gonzalez, C.2    McInstosh, M.A.3    Cabello, F.C.4
  • 8
    • 0034500527 scopus 로고    scopus 로고
    • Role of anaerobiosis in virulence of Salmonella typhimurium
    • Singh RD, Khullar M, Ganguly NK: Role of anaerobiosis in virulence of Salmonella typhimurium. Mol Cell Biochem 215: 39-46, 2000
    • (2000) Mol. Cell Biochem. , vol.215 , pp. 39-46
    • Singh, R.D.1    Khullar, M.2    Ganguly, N.K.3
  • 9
    • 0022466867 scopus 로고
    • Global control in Salmonella typhimurium: Two dimensional electrophoretic analysis of starvation, anaerobic and heat shock inducible proteins
    • Spector MP, Aliabadi Z, Gonzalez T, Foster JW: Global control in Salmonella typhimurium: Two dimensional electrophoretic analysis of starvation, anaerobic and heat shock inducible proteins. J Bacteriol 168: 420-424, 1986
    • (1986) J. Bacteriol. , vol.168 , pp. 420-424
    • Spector, M.P.1    Aliabadi, Z.2    Gonzalez, T.3    Foster, J.W.4
  • 11
    • 0028938217 scopus 로고
    • Acid tolerance of enterohemorrhagic Escherichia coli
    • Benjamin MM, Datta AR: Acid tolerance of enterohemorrhagic Escherichia coli. Appl Environ Microbiol 61: 1669-1672, 1995
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1669-1672
    • Benjamin, M.M.1    Datta, A.R.2
  • 12
    • 0027941632 scopus 로고
    • Adaptive acid tolerance response by Salmonella typhi and candidate for live oral typhoid vaccine strains
    • Hone DM, Harris AM, Levine MM: Adaptive acid tolerance response by Salmonella typhi and candidate for live oral typhoid vaccine strains. Vaccine 12: 895-898, 1994
    • (1994) Vaccine , vol.12 , pp. 895-898
    • Hone, D.M.1    Harris, A.M.2    Levine, M.M.3
  • 13
    • 0031969352 scopus 로고    scopus 로고
    • A low pH-inducible phop-dependent acid tolerance response protects Salmonella typhimurium against inorganic acid stress
    • Bearson BL, Wilson L, Foster JW: A low pH-inducible phop-dependent acid tolerance response protects Salmonella typhimurium against inorganic acid stress. J Bacteriol 180: 2049-2417, 1998
    • (1998) J. Bacteriol. , vol.180 , pp. 2049-2417
    • Bearson, B.L.1    Wilson, L.2    Foster, J.W.3
  • 14
    • 0029959309 scopus 로고    scopus 로고
    • The acid tolerance response of Salmonella typhimurium provides protection against organic acids
    • Baik HS, Bearson S, Dunbar S, Foster JW: The acid tolerance response of Salmonella typhimurium provides protection against organic acids. Microbiol 142: 3195-3200, 1998
    • (1998) Microbiol. , vol.142 , pp. 3195-3200
    • Baik, H.S.1    Bearson, S.2    Dunbar, S.3    Foster, J.W.4
  • 15
    • 0032704187 scopus 로고    scopus 로고
    • The cod A gene of Vibrio cholerae is induced during infection and plays a role in acid tolerance
    • Merrell DS, Camilli A: The cod A gene of Vibrio cholerae is induced during infection and plays a role in acid tolerance. Mol Microbiol 34: 836-849, 1999
    • (1999) Mol. Microbiol. , vol.34 , pp. 836-849
    • Merrell, D.S.1    Camilli, A.2
  • 16
    • 0033797747 scopus 로고    scopus 로고
    • Regulation of Vibrio cholerae genes required for acid tolerance by a member of the "Tox R-like" family of transcriptional regulators
    • Merrell DS, Camilli A: Regulation of Vibrio cholerae genes required for acFd tolerance by a member of the "TOx R-like" family of transcriptional regulators. J Bacteriol 182: 5342-5350, 2000
    • (2000) J. Bacteriol. , vol.182 , pp. 5342-5350
    • Merrell, D.S.1    Camilli, A.2
  • 17
    • 0035045057 scopus 로고    scopus 로고
    • The ToxR-mediated organic acid tolerance response of Vibrio Cholerae requires ompU
    • Merrell DS, Camilli B, Kaper JB, Camilli A: The ToxR-mediated organic acid tolerance response of Vibrio Cholerae requires ompU. J Bactreiol 183: 2746-2750, 2001
    • (2001) J. Bactreiol. , vol.183 , pp. 2746-2750
    • Merrell, D.S.1    Camilli, B.2    Kaper, J.B.3    Camilli, A.4
  • 19
    • 0029992278 scopus 로고    scopus 로고
    • Moleculer chaperones in cellular protein folding
    • Hartl FU: Moleculer chaperones in cellular protein folding. Nature 381: 571-580, 1996
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 20
    • 0035085033 scopus 로고    scopus 로고
    • Borrelia burgdorferi proteins whose expression is similarly affected by culture temperature and pH
    • Ramamoorthy R, Schoel-Meeker D: Borrelia burgdorferi proteins whose expression is similarly affected by culture temperature and pH. Infect Immun 69: 2739-2742, 2001
    • (2001) Infect. Immun. , vol.69 , pp. 2739-2742
    • Ramamoorthy, R.1    Schoel-Meeker, D.2
  • 21
    • 0035055499 scopus 로고    scopus 로고
    • Heat inducible surface stress protein (HSP70) mediates sulfatide recognition of the respiratory pathogen Haemophilus influenzae
    • Hartmann E, Lingwood CA, Reidl J: Heat inducible surface stress protein (HSP70) mediates sulfatide recognition of the respiratory pathogen Haemophilus influenzae. Infect Immun 69: 3438-3441, 2001
    • (2001) Infect. Immun. , vol.69 , pp. 3438-3441
    • Hartmann, E.1    Lingwood, C.A.2    Reidl, J.3
  • 22
    • 0036098506 scopus 로고    scopus 로고
    • Characterization of HSPR-mediated stress response in Helicobacter pylori
    • Spohn G, Delany I, Rappouli R, Scarlato V: Characterization of HSPR-mediated stress response in Helicobacter pylori. J Bacteriol 184: 2925-2930, 2002
    • (2002) J. Bacteriol. , vol.184 , pp. 2925-2930
    • Spohn, G.1    Delany, I.2    Rappouli, R.3    Scarlato, V.4
  • 23
    • 0036151140 scopus 로고    scopus 로고
    • Surface accessibility of the 70-kilodalton Chlamydia trachomatis heat shock protein following reduction of outemembrane protein disulfide bonds
    • Raulston JE, Davis CH, Paul TR, Hobbs JD, Wyrick PB: Surface accessibility of the 70-kilodalton Chlamydia trachomatis heat shock protein following reduction of outemembrane protein disulfide bonds. Infect Immun 79: 535-543, 2002
    • (2002) Infect. Immun. , vol.79 , pp. 535-543
    • Raulston, J.E.1    Davis, C.H.2    Paul, T.R.3    Hobbs, J.D.4    Wyrick, P.B.5
  • 24
    • 0025037611 scopus 로고
    • Adaptive acidification tolerance response of Salmonella typhimurium
    • Foster JW, Hall H: Adaptive acidification tolerance response of Salmonella typhimurium. J Bacteriol 172: 771-778, 1990
    • (1990) J. Bacteriol. , vol.172 , pp. 771-778
    • Foster, J.W.1    Hall, H.2
  • 26
    • 0018178434 scopus 로고
    • A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples
    • Markwell MAK, Tolberi NE: A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal Biochem 87: 206-210, 1978
    • (1978) Anal. Biochem. , vol.87 , pp. 206-210
    • Markwell, M.A.K.1    Tolberi, N.E.2
  • 28
    • 0024493549 scopus 로고
    • Purification, localization and immunological characterization of the iron-regulated high molecular weight proteins of highly pathogenic Yersinia
    • Carniel E, Antonine JC, Guiyoule A, Guiro N, Mollart HH: Purification, localization and immunological characterization of the iron-regulated high molecular weight proteins of highly pathogenic Yersinia. Infect Immun 57: 540-545, 1989
    • (1989) Infect. Immun. , vol.57 , pp. 540-545
    • Carniel, E.1    Antonine, J.C.2    Guiyoule, A.3    Guiro, N.4    Mollart, H.H.5
  • 31
    • 0027194901 scopus 로고
    • Identification of surface exposed B-cell epitopes recognized by Haemophilus influenzae type b specific monoclonal antibodies
    • Panezutti H, James O, Hanson EJ, Chei Y, Harkness RE, Klein MH, Chang P: Identification of surface exposed B-cell epitopes recognized by Haemophilus influenzae type b specific monoclonal antibodies. Infect Immun 61: 1867-1872, 1993
    • (1993) Infect. Immun. , vol.61 , pp. 1867-1872
    • Panezutti, H.1    James, O.2    Hanson, E.J.3    Chei, Y.4    Harkness, R.E.5    Klein, M.H.6    Chang, P.7
  • 32
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from acrylamide gels onto nitrocellulose sheet: Procedure and some applications
    • Towbin H, Staachelin T, Gordon J: Electrophoretic transfer of proteins from acrylamide gels onto nitrocellulose sheet: Procedure and some applications. Proc Natl Acad Sci USA 76: 4350-4354, 1979
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staachelin, T.2    Gordon, J.3
  • 33
    • 0030873751 scopus 로고    scopus 로고
    • Combat between host and microbes: The role of stress proteins
    • Singh RD, Sarin S, Tandon CD: Combat between host and microbes: The role of stress proteins. Med Sci Res 25: 573-575, 1997
    • (1997) Med. Sci. Res. , vol.25 , pp. 573-575
    • Singh, R.D.1    Sarin, S.2    Tandon, C.D.3
  • 34
    • 0032102035 scopus 로고    scopus 로고
    • What happens to bacterial pathogens in vivo
    • Smith H: What happens to bacterial pathogens in vivo. Trends Microbiol 6: 239-243, 1998
    • (1998) Trends Microbiol. , vol.6 , pp. 239-243
    • Smith, H.1
  • 35
    • 0026661296 scopus 로고
    • Effect of Salmonella typhimurium ferric uptake regulater (Fur) mutations on iron and pH regulated protein synthesis
    • Foster JW, Hall HK: Effect of Salmonella typhimurium ferric uptake regulater (Fur) mutations on iron and pH regulated protein synthesis. J Bacteriol 174: 4317-4323, 1992
    • (1992) J. Bacteriol. , vol.174 , pp. 4317-4323
    • Foster, J.W.1    Hall, H.K.2
  • 36
    • 0029929131 scopus 로고    scopus 로고
    • Acidic pH changes the receptor binding specificity of Helicobacter pylori: A binary adhesion model in which surface heat shock (stress) proteins mediate sulfatide recognition in gastric colonization
    • Huesca M, Borgia S, Hoffman P, Lingwood CA: Acidic pH changes the receptor binding specificity of Helicobacter pylori: A binary adhesion model in which surface heat shock (stress) proteins mediate sulfatide recognition in gastric colonization. Infect Immun 64: 2643-2648, 1996
    • (1996) Infect. Immun. , vol.64 , pp. 2643-2648
    • Huesca, M.1    Borgia, S.2    Hoffman, P.3    Lingwood, C.A.4
  • 37
    • 0025011064 scopus 로고    scopus 로고
    • Heat Shock protein synthesis and thermotolerance in Salmonella typhimurium
    • Mackey BM, Derrick C: Heat Shock protein synthesis and thermotolerance in Salmonella typhimurium. J Appl Bacteriol 69: 373-383, 1996
    • (1996) J. Appl. Bacteriol. , vol.69 , pp. 373-383
    • Mackey, B.M.1    Derrick, C.2
  • 38
    • 0031857518 scopus 로고    scopus 로고
    • Expression of heat shock proteins in Streptococcus pyogenes and their immunoreactivity with sera from patients with streptococcal diseases
    • Lemos JAC, Giambiagi-de Marval M, Castro ACD: Expression of heat shock proteins in Streptococcus pyogenes and their immunoreactivity with sera from patients with streptococcal diseases. J Med Microbiol 47: 711-715, 1998
    • (1998) J. Med. Microbiol. , vol.47 , pp. 711-715
    • Lemos, J.A.C.1    Giambiagi-de Marval, M.2    Castro, A.C.D.3
  • 39
    • 9444254275 scopus 로고
    • A 66 Kilodalton heat shock protein of Salmonella typhimurium is responsible for binding of the bacterium to intestinal mucus
    • Ensgraber M, Loos M: A 66 Kilodalton heat shock protein of Salmonella typhimurium is responsible for binding of the bacterium to intestinal mucus. Infect Immun 57: 1271-1275, 1992
    • (1992) Infect. Immun. , vol.57 , pp. 1271-1275
    • Ensgraber, M.1    Loos, M.2
  • 41
    • 0029101833 scopus 로고
    • ATP hydrolysis is required for the DnaJ dependent activation of DnaK chaperone for binding to both native and denatured protein substrates
    • Wawryznow A, Banecki B, Wall D, Liberek K, Georgopoulous C, Sylicz M: ATP hydrolysis is required for the DnaJ dependent activation of DnaK chaperone for binding to both native and denatured protein substrates. J Biol Chem 270: 19307-19311, 1995
    • (1995) J. Biol. Chem. , vol.270 , pp. 19307-19311
    • Wawryznow, A.1    Banecki, B.2    Wall, D.3    Liberek, K.4    Georgopoulous, C.5    Sylicz, M.6
  • 42
    • 0006198640 scopus 로고
    • Hydrogen peroxide inducible proteins in Salmonella typhimurium overlap with heat shock and other stress proteins
    • Morgan RW, Christman MF, Jacobson SF, Storz G, Ames BN: Hydrogen peroxide inducible proteins in Salmonella typhimurium overlap with heat shock and other stress proteins. Proc Natl Acad Sci USA 83: 8059-8063, 1986
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8059-8063
    • Morgan, R.W.1    Christman, M.F.2    Jacobson, S.F.3    Storz, G.4    Ames, B.N.5


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