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Volumn 44, Issue 2, 2003, Pages 320-330

pH6 antigen of Yersinia pestis interacts with plasma lipoproteins and cell membranes

Author keywords

Apolipoprotein B; Erythrocytes; Lipid rafts; Liposomes; Low density lipoproteins; THP I macrophages

Indexed keywords

ADHESIN; ANTIBODY; ANTIGEN; APOLIPOPROTEIN B; APOLIPOPROTEIN B ANTIBODY; GALACTOSYLCERAMIDE; LIPID EMULSION; LIPOSOME; LOW DENSITY LIPOPROTEIN; LOW DENSITY LIPOPROTEIN RECEPTOR; METHYL BETA CYCLODEXTRIN; PH6 ANTIGEN; TRITON X 100; UNCLASSIFIED DRUG;

EID: 0142091765     PISSN: 00222275     EISSN: None     Source Type: Journal    
DOI: 10.1194/jlr.M200182-JLR200     Document Type: Article
Times cited : (52)

References (39)
  • 1
    • 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
  • 3
    • 0023711836 scopus 로고
    • Inhibition of phagocytosis in Yersinia pseudotuberculosis: A virulence plasmid-encoded ability involving the Yop2b protein
    • Rosqvist, R., I. Bölin, and H. Wolf-Watz. 1988. Inhibition of phagocytosis in Yersinia pseudotuberculosis: a virulence plasmid-encoded ability involving the Yop2b protein. Infect. Immun. 56: 2139-2143.
    • (1988) Infect. Immun. , vol.56 , pp. 2139-2143
    • Rosqvist, R.1    Bölin, I.2    Wolf-Watz, H.3
  • 5
    • 0028031879 scopus 로고
    • Polarized transfer and regulation of Yersinia Yop proteins involved in antiphagocytosis
    • Forsberg, A., R. Rosqvist, and H. Wolf-Watz. 1994. Polarized transfer and regulation of Yersinia Yop proteins involved in antiphagocytosis. Treds Microbiol. 2: 14-19.
    • (1994) Treds Microbiol. , vol.2 , pp. 14-19
    • Forsberg, A.1    Rosqvist, R.2    Wolf-Watz, H.3
  • 6
    • 0031780201 scopus 로고    scopus 로고
    • YopJ of Yersinia pseudotuberculosis is required for the inhibition of macrophage TNFα 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 TNFα 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
  • 7
    • 0031775572 scopus 로고    scopus 로고
    • The yopJlocus is required for Yersinia-mediated inhibition of NF-κB activation and cytokine expression: YopJ contains a eukaryotic SH2-like domain that is essential for its repressing activity
    • Schesser, K., A. Spiik, J-M. Dukuzumuremyi, M. F. Neurath, S. Pettersson, and H. Wolf-Watz. 1998. The yopJlocus is required for Yersinia-mediated inhibition of NF-κB activation and cytokine expression: YopJ contains a eukaryotic SH2-like domain that is essential for its repressing activity. Mol. Microbiol. 28: 1067-1079.
    • (1998) Mol. Microbiol. , vol.28 , pp. 1067-1079
    • Schesser, K.1    Spiik, A.2    Dukuzumuremyi, J.-M.3    Neurath, M.F.4    Pettersson, S.5    Wolf-Watz, H.6
  • 8
    • 0000634969 scopus 로고    scopus 로고
    • Type III secretion systems in animal-and plant-interacting bacteria
    • P. Cossart, P. Boquet, S. Normark, and E. Rappouli, editors. ASM Press, Washington, DC
    • Schesser, K., M. S. Francis, Å. Forsberg, and H. Wolf-Watz. 2000. Type III secretion systems in animal-and plant-interacting bacteria. In Cellular Microbiology. P. Cossart, P. Boquet, S. Normark, and E. Rappouli, editors. ASM Press, Washington, DC. 239-263.
    • (2000) Cellular Microbiology , pp. 239-263
    • Schesser, K.1    Francis, M.S.2    Forsberg, Å.3    Wolf-Watz, H.4
  • 9
    • 0025788249 scopus 로고
    • Intracellular targeting of the Yersinia YopE cytotoxin in mammalian cells induces actin microfilament disruption
    • Rosqvist, R., Å. 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, Å.2    Wolf-Watz, H.3
  • 10
    • 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
  • 11
    • 0030044340 scopus 로고    scopus 로고
    • Invasin production by Yersinia pestis is abolished by insertion of an IS200-like element within the inv gene
    • Simonet, M., B. Riot, N. Fortineau, and P. Berche. 1996. Invasin production by Yersinia pestis is abolished by insertion of an IS200-like element within the inv gene. Infect. Immun. 64: 375-379.
    • (1996) Infect. Immun. , vol.64 , pp. 375-379
    • Simonet, M.1    Riot, B.2    Fortineau, N.3    Berche, P.4
  • 13
    • 0033943626 scopus 로고    scopus 로고
    • Invasion of epithelial cells by Yersinia pestis: Evidence for a Y. pestis-specific invasin
    • Cowan, C., H. A. Jones, Y. H. Kaya, R. D. Perry, and S. C. Straley. 2000. Invasion of epithelial cells by Yersinia pestis: evidence for a Y. pestis-specific invasin. Infect. Immun. 68: 4523-4530.
    • (2000) Infect. Immun. , vol.68 , pp. 4523-4530
    • Cowan, C.1    Jones, H.A.2    Kaya, Y.H.3    Perry, R.D.4    Straley, S.C.5
  • 14
    • 0142105709 scopus 로고
    • New antigenic component of Pasteurella pestis formed under specific conditions of pH and temperature
    • Ben-Efraim, S., M. Aronson, and L. Bichowsky-Slomnicki. 1961. New antigenic component of Pasteurella pestis formed under specific conditions of pH and temperature. J. Bacteriol. 81: 704-714.
    • (1961) J. Bacteriol. , vol.81 , pp. 704-714
    • Ben-Efraim, S.1    Aronson, M.2    Bichowsky-Slomnicki, L.3
  • 15
    • 0027152069 scopus 로고
    • Yersinia pestis pH 6 antigen forms a fimbria and is induced by intracellular association with macrophages
    • Lindler, L. E., and B. D. Tall. 1993. Yersinia pestis pH 6 antigen forms a fimbria and is induced by intracellular association with macrophages. Mol. Microbiol. 8: 311-324.
    • (1993) Mol. Microbiol. , vol.8 , pp. 311-324
    • Lindler, L.E.1    Tall, B.D.2
  • 16
    • 0032989015 scopus 로고    scopus 로고
    • Bacterial adhesins: Common themes and variations in architecture and assembly
    • Soto, G. E., and S. J. Hultgren. 1999. Bacterial adhesins: common themes and variations in architecture and assembly. J. Bacteriol. 181:1059-1071.
    • (1999) J. Bacteriol. , vol.181 , pp. 1059-1071
    • Soto, G.E.1    Hultgren, S.J.2
  • 17
    • 0029976469 scopus 로고    scopus 로고
    • The psa locus of Yersinia pseudotuberculosis is responsible for thermoinducible binding to cultured cells
    • Yang, Y., J. J. Merriam, J. P. Mueller, and R. R. Isberg. 1996. The psa locus of Yersinia pseudotuberculosis is responsible for thermoinducible binding to cultured cells. Infect. Immun. 64: 2483-2489.
    • (1996) Infect. Immun. , vol.64 , pp. 2483-2489
    • Yang, Y.1    Merriam, J.J.2    Mueller, J.P.3    Isberg, R.R.4
  • 18
    • 0031719490 scopus 로고    scopus 로고
    • The pH6 antigen of Yersinia pestis binds to β-1-linked galactosyl residues in glycosphingolipids
    • Payne, D., D. Tatham, E. D. Williamson, and R. W. Titball. 1998. The pH6 antigen of Yersinia pestis binds to β-1-linked galactosyl residues in glycosphingolipids. Infect. Immun. 66: 4545-4548.
    • (1998) Infect. Immun. , vol.66 , pp. 4545-4548
    • Payne, D.1    Tatham, D.2    Williamson, E.D.3    Titball, R.W.4
  • 19
    • 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. Stranley. 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    Stranley, S.C.3
  • 20
    • 0023939138 scopus 로고
    • Transcriptional activation of the lipoprotein lipase and apolipoprotein E genes accompanies differentiation in some human macrophage-like cell lines
    • Auwerx, J. H., S. Deeb, J. D. Brunzell, R. Peng, and A. Chait. 1988. Transcriptional activation of the lipoprotein lipase and apolipoprotein E genes accompanies differentiation in some human macrophage-like cell lines. Biochemistry. 27: 2651-2655.
    • (1988) Biochemistry , vol.27 , pp. 2651-2655
    • Auwerx, J.H.1    Deeb, S.2    Brunzell, J.D.3    Peng, R.4    Chait, A.5
  • 22
    • 0022556072 scopus 로고
    • Precautionary measures for collecting blood destined for lipoprotein isolation
    • Edelstein, C., and A. M. Scanu. 1986. Precautionary measures for collecting blood destined for lipoprotein isolation. Methods Enzymol. 128: 151-155.
    • (1986) Methods Enzymol. , vol.128 , pp. 151-155
    • Edelstein, C.1    Scanu, A.M.2
  • 23
    • 0018178434 scopus 로고
    • A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples
    • Markwell, M. A., S. M. Haas, L. L. Bieber, and N. E. Tolbert. 1978. A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal. Biochem. 87: 206-210.
    • (1978) Anal. Biochem. , vol.87 , pp. 206-210
    • Markwell, M.A.1    Haas, S.M.2    Bieber, L.L.3    Tolbert, N.E.4
  • 24
    • 0014148255 scopus 로고
    • I-131-labeling of proteins at high activity level with I-131-Cl produced by oxidation of total iodine in Na-I-131 preparations
    • Helmkamp, R. W., M. A. Contreras, and M. J. Izzo. 1967. I-131-labeling of proteins at high activity level with I-131-Cl produced by oxidation of total iodine in Na-I-131 preparations. Int. J. Appl. Radiat. Isot. 18: 747-754.
    • (1967) Int. J. Appl. Radiat. Isot. , vol.18 , pp. 747-754
    • Helmkamp, R.W.1    Contreras, M.A.2    Izzo, M.J.3
  • 25
    • 0028365891 scopus 로고
    • Determination of apolipoproteins B-48 and B-100 in triglyceride-rich lipoproteins by analytical SDS-PAGE
    • Karpe, F., and A. Hamsten. 1994. Determination of apolipoproteins B-48 and B-100 in triglyceride-rich lipoproteins by analytical SDS-PAGE. J. Lipid Res. 35: 1311-1317.
    • (1994) J. Lipid Res. , vol.35 , pp. 1311-1317
    • Karpe, F.1    Hamsten, A.2
  • 27
    • 75549112549 scopus 로고
    • Biological activities in extracts of Pasturella pestis and their relation to the pH6 antigen
    • Bichowsky-Slomnicki, L., and S. Ben-Efraim. 1963. Biological activities in extracts of Pasturella pestis and their relation to the pH6 antigen. J. Bacteriol. 86: 101-111.
    • (1963) J. Bacteriol. , vol.86 , pp. 101-111
    • Bichowsky-Slomnicki, L.1    Ben-Efraim, S.2
  • 28
    • 0020973547 scopus 로고
    • Receptor-mediated endocytosis of low-density lipoprotein in cultured cells
    • Goldstein, J. L., S. K. Basu, and M. S. Brown. 1983. Receptor-mediated endocytosis of low-density lipoprotein in cultured cells. Methods Enzymol. 98: 241-260.
    • (1983) Methods Enzymol. , vol.98 , pp. 241-260
    • Goldstein, J.L.1    Basu, S.K.2    Brown, M.S.3
  • 29
    • 0022003140 scopus 로고
    • Deglycosylation of asparagine-linked glycans by Pepetide:N-Glycosidase F
    • Tarentino, A. L., C. M. Gómez, and T. H. Plummer, Jr. 1985. Deglycosylation of asparagine-linked glycans by Pepetide:N-Glycosidase F. Biochemistry. 24: 4665-4671.
    • (1985) Biochemistry , vol.24 , pp. 4665-4671
    • Tarentino, A.L.1    Gómez, C.M.2    Plummer T.H., Jr.3
  • 30
    • 0023161210 scopus 로고
    • Enzymatic deglycosylation of glycoproteins
    • Thotakura, N. R., and O. P. Bahl. 1987. Enzymatic deglycosylation of glycoproteins. Methods Enzymol. 138: 350-359.
    • (1987) Methods Enzymol. , vol.138 , pp. 350-359
    • Thotakura, N.R.1    Bahl, O.P.2
  • 31
    • 0023889910 scopus 로고
    • Rat monoclonal antibodies to rabbit and human serum low-density lipoprotein
    • Gherardi, E., A. Hutchings, G. Galfre, and D. E. Bowyer. 1988. Rat monoclonal antibodies to rabbit and human serum low-density lipoprotein. Biochem. J. 252: 237-245.
    • (1988) Biochem. J. , vol.252 , pp. 237-245
    • Gherardi, E.1    Hutchings, A.2    Galfre, G.3    Bowyer, D.E.4
  • 32
    • 0035920107 scopus 로고    scopus 로고
    • Binding of low density lipoproteins to lipoprotein lipase is dependent on lipids but not on apolipoprotein B
    • Borén, J., A. Lookene, E. Makoveichuk, S. Xiang, M. Gustafsson, H. Liu, P. Talmud, and G. Olivecrona. 2001. Binding of low density lipoproteins to lipoprotein lipase is dependent on lipids but not on apolipoprotein B. J. Biol. Chem. 276: 26916-26922.
    • (2001) J. Biol. Chem. , vol.276 , pp. 26916-26922
    • Borén, J.1    Lookene, A.2    Makoveichuk, E.3    Xiang, S.4    Gustafsson, M.5    Liu, H.6    Talmud, P.7    Olivecrona, G.8
  • 33
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • Brown, D. A., and E. London. 2000. Structure and function of sphingolipid- and cholesterol-rich membrane rafts. J. Biol. Chem. 275: 17221-17224.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 34
    • 0034331817 scopus 로고    scopus 로고
    • Transmembrane and cytoplasmic domains of syndecan mediate a multi-step endocytic pathway involving detergent-insoluble membrane rafts
    • Fuki, I. V., M. E. Meyer, and K. J. Williams. 2000. Transmembrane and cytoplasmic domains of syndecan mediate a multi-step endocytic pathway involving detergent-insoluble membrane rafts. Biochem. J. 351: 607-612.
    • (2000) Biochem. J. , vol.351 , pp. 607-612
    • Fuki, I.V.1    Meyer, M.E.2    Williams, K.J.3
  • 35
    • 4243500405 scopus 로고
    • Physical properties, chemical composition and structure of circulating lipoproteins
    • H. Peeters, editor. Plenum Press, New York, London
    • Kézdy, F. J. 1978. Physical properties, chemical composition and structure of circulating lipoproteins. In The Lipoprotein Molecule. H. Peeters, editor. Plenum Press, New York, London. 83-90.
    • (1978) The Lipoprotein Molecule , pp. 83-90
    • Kézdy, F.J.1
  • 37
    • 0028057494 scopus 로고
    • Ultrastractural localization of gangliosides; GM1 is concentrated in caveolae
    • Parton, R. G. 1994. Ultrastractural localization of gangliosides; GM1 is concentrated in caveolae. J. Histochem. Cytochem. 42: 155-166.
    • (1994) J. Histochem. Cytochem. , vol.42 , pp. 155-166
    • Parton, R.G.1
  • 38
    • 0035028838 scopus 로고    scopus 로고
    • Raft membrane domains: From a liquid-ordered membrane phase to a site of pathogen attack
    • van der Goot, F. G., and T. Harder. 2001. Raft membrane domains: from a liquid-ordered membrane phase to a site of pathogen attack. Semin. Immunol. 13: 89-97.
    • (2001) Semin. Immunol. , vol.13 , pp. 89-97
    • Van der Goot, F.G.1    Harder, T.2
  • 39
    • 0037085471 scopus 로고    scopus 로고
    • Blocking the secretion of hepatic very low density lipoproteins renders the liver more susceptible to toxin-induced injury
    • Björkegren, J., A. Beigneux, M. O. Bergö, J. J. Maher, and S. G. Young. 2002. Blocking the secretion of hepatic very low density lipoproteins renders the liver more susceptible to toxin-induced injury. J. Biol. Chem. 277: 5476-5483.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5476-5483
    • Björkegren, J.1    Beigneux, A.2    Bergö, M.O.3    Maher, J.J.4    Young, S.G.5


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