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Volumn 49, Issue 28, 2010, Pages 5954-5967

Identification and characterization of the carbohydrate ligands recognized by pertussis toxin via a glycan microarray and surface plasmon resonance

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE LIGANDS; CLINICAL DISEASE; CONFORMATIONAL SPACE; GLYCAN MICROARRAYS; GLYCANS; GLYCOLIPIDS; MUTATIONAL ANALYSIS; N-GLYCAN; N-GLYCANS; N-LINKED GLYCANS; N-TERMINALS; O-LINKED; PERTUSSIS TOXIN; QUANTITATIVE ANALYSIS; SECOND GROUP; SIALIC ACIDS;

EID: 77954572993     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100474z     Document Type: Article
Times cited : (31)

References (56)
  • 1
    • 0036480204 scopus 로고    scopus 로고
    • Pertussis-United States, 1997-2000
    • Centers for Disease Control and Prevention. Centers for Disease Control and Prevention, Atlanta
    • Centers for Disease Control and Prevention (2002) Pertussis-United States, 1997-2000. Morbidity and Mortality Weekly Report, Vol. 51, pp 73 - 76, Centers for Disease Control and Prevention, Atlanta.
    • (2002) Morbidity and Mortality Weekly Report , vol.51 , pp. 73-76
  • 2
    • 32544461447 scopus 로고    scopus 로고
    • Pertussis-United States, 2001-2003
    • Centers for Disease Control and Prevention. Centers for Disease Control and Prevention, Atlanta
    • Centers for Disease Control and Prevention (2005) Pertussis-United States, 2001-2003. Morbidity and Mortality Weekly Report, Vol. 54, pp 1283 - 1286, Centers for Disease Control and Prevention, Atlanta.
    • (2005) Morbidity and Mortality Weekly Report , vol.54 , pp. 1283-1286
  • 3
    • 0021251437 scopus 로고
    • Pertussis toxin and extracytoplasmic adenylate cyclase as virulence factors of Bordetella pertussis
    • Weiss, A. A., Hewlett, E. L., Myers, G. A., and Falkow, S. (1984) Pertussis toxin and extracytoplasmic adenylate cyclase as virulence factors of Bordetella pertussis J. Infect. Dis. 150, 219-222
    • (1984) J. Infect. Dis. , vol.150 , pp. 219-222
    • Weiss, A.A.1    Hewlett, E.L.2    Myers, G.A.3    Falkow, S.4
  • 4
    • 0018465015 scopus 로고
    • Pertussis toxin: The cause of the harmful effects and prolonged immunity of whooping cough. A hypothesis
    • Pittman, M. (1979) Pertussis toxin: The cause of the harmful effects and prolonged immunity of whooping cough. A hypothesis Rev. Infect. Dis. 1, 401-412
    • (1979) Rev. Infect. Dis. , vol.1 , pp. 401-412
    • Pittman, M.1
  • 5
    • 0021182482 scopus 로고
    • The concept of pertussis as a toxin-mediated disease
    • Pittman, M. (1984) The concept of pertussis as a toxin-mediated disease Pediatr. Infect. Dis. 3, 467-486
    • (1984) Pediatr. Infect. Dis. , vol.3 , pp. 467-486
    • Pittman, M.1
  • 6
    • 0017159334 scopus 로고
    • Isolation and properties of the leukocytosis- and lymphocytosis-promoting factor of Bordetella pertussis
    • Morse, S. I. and Morse, J. H. (1976) Isolation and properties of the leukocytosis- and lymphocytosis-promoting factor of Bordetella pertussis J. Exp. Med. 143, 1483-1502
    • (1976) J. Exp. Med. , vol.143 , pp. 1483-1502
    • Morse, S.I.1    Morse, J.H.2
  • 7
    • 7444258406 scopus 로고
    • The white blood cell count and the erythrocyte sedimentation rate in pertussis
    • Lagergren, J. (1963) The white blood cell count and the erythrocyte sedimentation rate in pertussis Acta Paediatr. 52, 405-409
    • (1963) Acta Paediatr. , vol.52 , pp. 405-409
    • Lagergren, J.1
  • 8
    • 0020362248 scopus 로고
    • Subunit structure of islet-activating protein, pertussis toxin, in conformity with the A-B model
    • Tamura, M., Nogimori, K., Murai, S., Yajima, M., Ito, K., Katada, T., Ui, M., and Ishii, S. (1982) Subunit structure of islet-activating protein, pertussis toxin, in conformity with the A-B model Biochemistry 21, 5516-5522
    • (1982) Biochemistry , vol.21 , pp. 5516-5522
    • Tamura, M.1    Nogimori, K.2    Murai, S.3    Yajima, M.4    Ito, K.5    Katada, T.6    Ui, M.7    Ishii, S.8
  • 9
    • 0020791359 scopus 로고
    • The A protomer of islet-activating protein, pertussis toxin, as an active peptide catalyzing ADP-ribosylation of a membrane protein
    • Katada, T., Tamura, M., and Ui, M. (1983) The A protomer of islet-activating protein, pertussis toxin, as an active peptide catalyzing ADP-ribosylation of a membrane protein Arch. Biochem. Biophys. 224, 290-298
    • (1983) Arch. Biochem. Biophys. , vol.224 , pp. 290-298
    • Katada, T.1    Tamura, M.2    Ui, M.3
  • 10
    • 0020520658 scopus 로고
    • A role of the B-oligomer moiety of islet-activating protein, pertussis toxin, in development of the biological effects on intact cells
    • Tamura, M., Nogimori, K., Yajima, M., Ase, K., and Ui, M. (1983) A role of the B-oligomer moiety of islet-activating protein, pertussis toxin, in development of the biological effects on intact cells J. Biol. Chem. 258, 6756-6761
    • (1983) J. Biol. Chem. , vol.258 , pp. 6756-6761
    • Tamura, M.1    Nogimori, K.2    Yajima, M.3    Ase, K.4    Ui, M.5
  • 11
    • 77954584381 scopus 로고
    • The mitogenic responce of mouse lyphocytosis to the lymphocytosis- promoting factor (LPF) of Bordetella pertussis
    • Kong, A. S. and Morse, S. I. (1975) The mitogenic responce of mouse lyphocytosis to the lymphocytosis-promoting factor (LPF) of Bordetella pertussis Fed. Proc. 34, 951
    • (1975) Fed. Proc. , vol.34 , pp. 951
    • Kong, A.S.1    Morse, S.I.2
  • 12
    • 0023239742 scopus 로고
    • Pertussis toxin triggers rapid second messenger production in human T lymphocytes
    • Rosoff, P. M., Walker, R., and Winberry, L. (1987) Pertussis toxin triggers rapid second messenger production in human T lymphocytes J. Immunol. 139, 2419-2423
    • (1987) J. Immunol. , vol.139 , pp. 2419-2423
    • Rosoff, P.M.1    Walker, R.2    Winberry, L.3
  • 13
    • 0023610240 scopus 로고
    • Human T lymphocyte mitogenesis in response to the B oligomer of pertussis toxin is associated with an early elevation in cytosolic calcium concentrations
    • Strnad, C. F. and Carchman, R. A. (1987) Human T lymphocyte mitogenesis in response to the B oligomer of pertussis toxin is associated with an early elevation in cytosolic calcium concentrations FEBS Lett. 225, 16-20
    • (1987) FEBS Lett. , vol.225 , pp. 16-20
    • Strnad, C.F.1    Carchman, R.A.2
  • 14
    • 0024553652 scopus 로고
    • Pertussis toxin effects on T lymphocytes are mediated through CD3 and not by pertussis toxin catalyzed modification of a G protein
    • Gray, L. S., Huber, K. S., Gray, M. C., Hewlett, E. L., and Engelhard, V. H. (1989) Pertussis toxin effects on T lymphocytes are mediated through CD3 and not by pertussis toxin catalyzed modification of a G protein J. Immunol. 142, 1631-1638
    • (1989) J. Immunol. , vol.142 , pp. 1631-1638
    • Gray, L.S.1    Huber, K.S.2    Gray, M.C.3    Hewlett, E.L.4    Engelhard, V.H.5
  • 16
    • 0027930716 scopus 로고
    • Pertussis toxin activates platelets through an interaction with platelet glycoprotein Ib
    • Sindt, K. A., Hewlett, E. L., Redpath, G. T., Rappuoli, R., Gray, L. S., and Vandenberg, S. R. (1994) Pertussis toxin activates platelets through an interaction with platelet glycoprotein Ib Infect. Immun. 62, 3108-3114
    • (1994) Infect. Immun. , vol.62 , pp. 3108-3114
    • Sindt, K.A.1    Hewlett, E.L.2    Redpath, G.T.3    Rappuoli, R.4    Gray, L.S.5    Vandenberg, S.R.6
  • 17
    • 33845198084 scopus 로고    scopus 로고
    • Pertussis Toxin and Its Binding Unit Inhibit HIV-1 Infection of Human Cervical Tissue and Macrophages Involving a CD14 Pathway
    • Hu, Q., Younson, J., Griffin, G. E., Kelly, C., and Shattock, R. J. (2006) Pertussis Toxin and Its Binding Unit Inhibit HIV-1 Infection of Human Cervical Tissue and Macrophages Involving a CD14 Pathway J. Infect. Dis. 194, 1547-1556
    • (2006) J. Infect. Dis. , vol.194 , pp. 1547-1556
    • Hu, Q.1    Younson, J.2    Griffin, G.E.3    Kelly, C.4    Shattock, R.J.5
  • 18
    • 33746035677 scopus 로고    scopus 로고
    • Induction of dendritic cell maturation by pertussis toxin and its B subunit differentially initiate Toll-like receptor 4-dependent signal transduction pathways
    • Wang, Z. Y., Yang, D., Chen, Q., Leifer, C. A., Segal, D. M., Su, S. B., Caspi, R. R., Howard, Z. O., and Oppenheim, J. J. (2006) Induction of dendritic cell maturation by pertussis toxin and its B subunit differentially initiate Toll-like receptor 4-dependent signal transduction pathways Exp. Hematol. 34, 1115-1124
    • (2006) Exp. Hematol. , vol.34 , pp. 1115-1124
    • Wang, Z.Y.1    Yang, D.2    Chen, Q.3    Leifer, C.A.4    Segal, D.M.5    Su, S.B.6    Caspi, R.R.7    Howard, Z.O.8    Oppenheim, J.J.9
  • 19
    • 0029970109 scopus 로고    scopus 로고
    • Mechanisms of pertussis toxin-induced myelomonocytic cell adhesion: Role of Mac-1(CD11b/CD18) and urokinase receptor (CD87)
    • Wong, W. S., Simon, D. I., Rosoff, P. M., Rao, N. K., and Chapman, H. A. (1996) Mechanisms of pertussis toxin-induced myelomonocytic cell adhesion: Role of Mac-1(CD11b/CD18) and urokinase receptor (CD87) Immunology 88, 90-97
    • (1996) Immunology , vol.88 , pp. 90-97
    • Wong, W.S.1    Simon, D.I.2    Rosoff, P.M.3    Rao, N.K.4    Chapman, H.A.5
  • 20
    • 0033854453 scopus 로고    scopus 로고
    • Mechanisms of pertussis toxin-induced myelomonocytic cell adhesion: Role of CD14 and urokinase receptor
    • Li, H. and Wong, W. S. (2000) Mechanisms of pertussis toxin-induced myelomonocytic cell adhesion: Role of CD14 and urokinase receptor Immunology 100, 502-509
    • (2000) Immunology , vol.100 , pp. 502-509
    • Li, H.1    Wong, W.S.2
  • 21
    • 0022977666 scopus 로고
    • Protein-chemical analysis of pertussis toxin reveals homology between the subunits S2 and S3, between S1 and the A chains of enterotoxins of Vibrio cholerae and Escherichia coli and identifies S2 as the haptoglobin-binding subunit
    • Capiau, C., Petre, J., Van Damme, J., Puype, M., and Vandekerckhove, J. (1986) Protein-chemical analysis of pertussis toxin reveals homology between the subunits S2 and S3, between S1 and the A chains of enterotoxins of Vibrio cholerae and Escherichia coli and identifies S2 as the haptoglobin-binding subunit FEBS Lett. 204, 336-340
    • (1986) FEBS Lett. , vol.204 , pp. 336-340
    • Capiau, C.1    Petre, J.2    Van Damme, J.3    Puype, M.4    Vandekerckhove, J.5
  • 22
    • 2142686873 scopus 로고
    • Pertussis toxin: Structural elements involved in the interaction with cells
    • Sekura, R. D., Moss, J., and Vaughan, M., Eds., Academic Press, Inc., Orlando, FL
    • Sekura, R. D. and Zhang, Y. (1985) Pertussis toxin: Structural elements involved in the interaction with cells. In Pertussis Toxin (Sekura, R. D., Moss, J., and Vaughan, M., Eds.) pp 45 - 64, Academic Press, Inc., Orlando, FL.
    • (1985) Pertussis Toxin , pp. 45-64
    • Sekura, R.D.1    Zhang, Y.2
  • 23
    • 0008822161 scopus 로고
    • Monoclonal antibodies specific for pertussis toxin subunits and identification of the haptoglobin-binding site
    • Lerner, R. A., Ginsberg, H., Chanock, R. M., and Brown, F., Eds. Cold Spring Harbor Laboratory Press, Plainview, NY
    • Francotte, M., Locht, C., Feron, C., Capiau, C., and De Wilde, M. (1989) Monoclonal antibodies specific for pertussis toxin subunits and identification of the haptoglobin-binding site. In Vaccines 89 (Lerner, R. A., Ginsberg, H., Chanock, R. M., and Brown, F., Eds.) pp 243 - 247, Cold Spring Harbor Laboratory Press, Plainview, NY.
    • (1989) Vaccines 89 , pp. 243-247
    • Francotte, M.1    Locht, C.2    Feron, C.3    Capiau, C.4    De Wilde, M.5
  • 24
    • 0024356890 scopus 로고
    • Structures of asparagine-linked oligosaccharides of the glycoprotein fetuin having sialic acid linked to N-acetylglucosamine
    • Cumming, D. A., Hellerqvist, C. G., Harris-Brandts, M., Michnick, S. W., Carver, J. P., and Bendiak, B. (1989) Structures of asparagine-linked oligosaccharides of the glycoprotein fetuin having sialic acid linked to N-acetylglucosamine Biochemistry 28, 6500-6512
    • (1989) Biochemistry , vol.28 , pp. 6500-6512
    • Cumming, D.A.1    Hellerqvist, C.G.2    Harris-Brandts, M.3    Michnick, S.W.4    Carver, J.P.5    Bendiak, B.6
  • 25
    • 0025224835 scopus 로고
    • Comparison of the lectin-like activity of pertussis toxin with two plant lectins that have differential specificities for α(2-6) and α(2-3)-linked sialic acid
    • Heerze, L. D. and Armstrong, G. D. (1990) Comparison of the lectin-like activity of pertussis toxin with two plant lectins that have differential specificities for α(2-6) and α(2-3)-linked sialic acid Biochem. Biophys. Res. Commun. 172, 1224-1229
    • (1990) Biochem. Biophys. Res. Commun. , vol.172 , pp. 1224-1229
    • Heerze, L.D.1    Armstrong, G.D.2
  • 26
    • 33747883626 scopus 로고    scopus 로고
    • Development of a carbohydrate binding assay for the B-oligomer of pertussis toxin and toxoid
    • Gomez, S. R., Xing, D. K., Corbel, M. J., Coote, J., Parton, R., and Yuen, C. T. (2006) Development of a carbohydrate binding assay for the B-oligomer of pertussis toxin and toxoid Anal. Biochem. 356, 244-253
    • (2006) Anal. Biochem. , vol.356 , pp. 244-253
    • Gomez, S.R.1    Xing, D.K.2    Corbel, M.J.3    Coote, J.4    Parton, R.5    Yuen, C.T.6
  • 27
    • 0027246026 scopus 로고
    • Characterization of pertussis toxin analogs containing mutations in B-oligomer subunits
    • Loosmore, S., Zealey, G., Cockle, S., Boux, H., Chong, P., Yacoob, R., and Klein, M. (1993) Characterization of pertussis toxin analogs containing mutations in B-oligomer subunits Infect. Immun. 61, 2316-2324
    • (1993) Infect. Immun. , vol.61 , pp. 2316-2324
    • Loosmore, S.1    Zealey, G.2    Cockle, S.3    Boux, H.4    Chong, P.5    Yacoob, R.6    Klein, M.7
  • 28
    • 0024491740 scopus 로고
    • Mapping of linear B-cell epitopes of the S2 subunit of pertussis toxin
    • Schmidt, W. and Schmidt, M. A. (1989) Mapping of linear B-cell epitopes of the S2 subunit of pertussis toxin Infect. Immun. 57, 438-445
    • (1989) Infect. Immun. , vol.57 , pp. 438-445
    • Schmidt, W.1    Schmidt, M.A.2
  • 29
    • 0024329267 scopus 로고
    • Inhibition of pertussis toxin binding to model receptors by antipeptide antibodies directed at an antigenic domain of the S2 subunit
    • Schmidt, M. A. and Schmidt, W. (1989) Inhibition of pertussis toxin binding to model receptors by antipeptide antibodies directed at an antigenic domain of the S2 subunit Infect. Immun. 57, 3828-3833
    • (1989) Infect. Immun. , vol.57 , pp. 3828-3833
    • Schmidt, M.A.1    Schmidt, W.2
  • 30
    • 0026029045 scopus 로고
    • Identification of linear B-cell determinants of pertussis toxin associated with the receptor recognition site of the S3 subunit
    • Schmidt, M. A., Raupach, B., Szulczynski, M., and Marzillier, J. (1991) Identification of linear B-cell determinants of pertussis toxin associated with the receptor recognition site of the S3 subunit Infect. Immun. 59, 1402-1408
    • (1991) Infect. Immun. , vol.59 , pp. 1402-1408
    • Schmidt, M.A.1    Raupach, B.2    Szulczynski, M.3    Marzillier, J.4
  • 32
    • 0027514682 scopus 로고
    • Site-specific alterations in the B oligomer that affect receptor-binding activities and mitogenicity of pertussis toxin
    • DOI 10.1084/jem.177.1.79
    • Lobet, Y., Feron, C., Dequesne, G., Simoen, E., Hauser, P., and Locht, C. (1993) Site-specific alterations in the B oligomer that affect receptor-binding activities and mitogenicity of pertussis toxin J. Exp. Med. 177, 79-87 (Pubitemid 23008087)
    • (1993) Journal of Experimental Medicine , vol.177 , Issue.1 , pp. 79-87
    • Lobet, Y.1    Feron, C.2    Dequesne, G.3    Simoen, E.4    Hauser, P.5    Locht, C.6
  • 33
    • 0027296749 scopus 로고
    • Prokaryotic peptides that block leukocyte adherence to selectins
    • Rozdzinski, E., Burnette, W. N., Jones, T., Mar, V., and Tuomanen, E. (1993) Prokaryotic peptides that block leukocyte adherence to selectins J. Exp. Med. 178, 917-924
    • (1993) J. Exp. Med. , vol.178 , pp. 917-924
    • Rozdzinski, E.1    Burnette, W.N.2    Jones, T.3    Mar, V.4    Tuomanen, E.5
  • 34
    • 0028575328 scopus 로고
    • Lectin domains in the toxin of Bordetella pertussis: Selectin mimicry linked to microbial pathogenesis
    • Sandros, J., Rozdzinski, E., Zheng, J., Cowburn, D., and Tuomanen, E. (1994) Lectin domains in the toxin of Bordetella pertussis: Selectin mimicry linked to microbial pathogenesis Glycoconjugate J. 11, 501-506
    • (1994) Glycoconjugate J. , vol.11 , pp. 501-506
    • Sandros, J.1    Rozdzinski, E.2    Zheng, J.3    Cowburn, D.4    Tuomanen, E.5
  • 36
    • 0004741267 scopus 로고
    • Subunit S1 of pertussis toxin: Mapping of the regions essential for ADP-ribosyltransferase activity
    • Pizza, M., Bartoloni, A., Prugnola, A., Silvestri, S., and Rappuoli, R. (1988) Subunit S1 of pertussis toxin: Mapping of the regions essential for ADP-ribosyltransferase activity Proc. Natl. Acad. Sci. U.S.A. 85, 7521-7525
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 7521-7525
    • Pizza, M.1    Bartoloni, A.2    Prugnola, A.3    Silvestri, S.4    Rappuoli, R.5
  • 38
    • 18644380977 scopus 로고    scopus 로고
    • Pertussis toxin (PTX) B subunit and the nontoxic PTX mutant PT9K/129G inhibit Tat-induced TGF-β production by NK cells and TGF-β-mediated NK cell apoptosis
    • Zocchi, M. R., Contini, P., Alfano, M., and Poggi, A. (2005) Pertussis toxin (PTX) B subunit and the nontoxic PTX mutant PT9K/129G inhibit Tat-induced TGF-β production by NK cells and TGF-β-mediated NK cell apoptosis J. Immunol. 174, 6054-6061
    • (2005) J. Immunol. , vol.174 , pp. 6054-6061
    • Zocchi, M.R.1    Contini, P.2    Alfano, M.3    Poggi, A.4
  • 39
    • 0021714472 scopus 로고
    • Monoclonal antibody against pertussis toxin: Effect on toxin activity and pertussis infections
    • Sato, H., Ito, A., Chiba, J., and Sato, Y. (1984) Monoclonal antibody against pertussis toxin: Effect on toxin activity and pertussis infections Infect. Immun. 46, 422-428
    • (1984) Infect. Immun. , vol.46 , pp. 422-428
    • Sato, H.1    Ito, A.2    Chiba, J.3    Sato, Y.4
  • 40
    • 0025042990 scopus 로고
    • Protective activities in mice of monoclonal antibodies against pertussis toxin
    • Sato, H. and Sato, Y. (1990) Protective activities in mice of monoclonal antibodies against pertussis toxin Infect. Immun. 58, 3369-3374
    • (1990) Infect. Immun. , vol.58 , pp. 3369-3374
    • Sato, H.1    Sato, Y.2
  • 41
    • 0023110713 scopus 로고
    • Effect of monoclonal antibody to pertussis toxin on toxin activity
    • Sato, H., Sato, Y., Ito, A., and Ohishi, I. (1987) Effect of monoclonal antibody to pertussis toxin on toxin activity Infect. Immun. 55, 909-915
    • (1987) Infect. Immun. , vol.55 , pp. 909-915
    • Sato, H.1    Sato, Y.2    Ito, A.3    Ohishi, I.4
  • 43
    • 70349560033 scopus 로고    scopus 로고
    • Factors affecting protein-glycan specificity: Effect of spacers and incubation time
    • Lewallen, D. M., Siler, D., and Iyer, S. S. (2009) Factors affecting protein-glycan specificity: Effect of spacers and incubation time ChemBioChem 10, 1486-1489
    • (2009) ChemBioChem , vol.10 , pp. 1486-1489
    • Lewallen, D.M.1    Siler, D.2    Iyer, S.S.3
  • 44
    • 0023877979 scopus 로고
    • Lectin-like binding of pertussis toxin to a 165-kilodalton Chinese hamster ovary cell glycoprotein
    • Brennan, M. J., David, J. L., Kenimer, J. G., and Manclark, C. R. (1988) Lectin-like binding of pertussis toxin to a 165-kilodalton Chinese hamster ovary cell glycoprotein J. Biol. Chem. 263, 4895-4899
    • (1988) J. Biol. Chem. , vol.263 , pp. 4895-4899
    • Brennan, M.J.1    David, J.L.2    Kenimer, J.G.3    Manclark, C.R.4
  • 45
    • 0344527792 scopus 로고    scopus 로고
    • Nonrestricted differential intoxication of cells by pertussis toxin
    • el Baya, A., Bruckener, K., and Schmidt, M. A. (1999) Nonrestricted differential intoxication of cells by pertussis toxin Infect. Immun. 67, 433-435
    • (1999) Infect. Immun. , vol.67 , pp. 433-435
    • El Baya, A.1    Bruckener, K.2    Schmidt, M.A.3
  • 46
    • 0008822161 scopus 로고
    • Monoclonal antibodies specific for pertussis toxin subunits and identification of the haptoglobin-binding site
    • Lerner, R. A., Ginsberg, H., Chanock, R. M., and Brown, F., Eds., Cold Spring Harbor Laboratory Press, Plainview, NY.
    • Francotte, M., Locht, C., Feron, C., Capiau, C., and de Wilde, M. (1989) Monoclonal antibodies specific for pertussis toxin subunits and identification of the haptoglobin-binding site. In Vaccines (Lerner, R. A., Ginsberg, H., Chanock, R. M., and Brown, F., Eds.) pp 243 - 247, Cold Spring Harbor Laboratory Press, Plainview, NY.
    • (1989) Vaccines , pp. 243-247
    • Francotte, M.1    Locht, C.2    Feron, C.3    Capiau, C.4    De Wilde, M.5
  • 49
    • 0032546785 scopus 로고    scopus 로고
    • The molecular basis for the absence of N-glycolylneuraminic acid in humans
    • Irie, A., Koyama, S., Kozutsumi, Y., Kawasaki, T., and Suzuki, A. (1998) The molecular basis for the absence of N-glycolylneuraminic acid in humans J. Biol. Chem. 273, 15866-15871
    • (1998) J. Biol. Chem. , vol.273 , pp. 15866-15871
    • Irie, A.1    Koyama, S.2    Kozutsumi, Y.3    Kawasaki, T.4    Suzuki, A.5
  • 50
    • 0346991736 scopus 로고    scopus 로고
    • Temporal expression of pertussis toxin and Ptl secretion proteins by Bordetella pertussis
    • Rambow-Larsen, A. A. and Weiss, A. A. (2004) Temporal expression of pertussis toxin and Ptl secretion proteins by Bordetella pertussis J. Bacteriol. 186, 43-50
    • (2004) J. Bacteriol. , vol.186 , pp. 43-50
    • Rambow-Larsen, A.A.1    Weiss, A.A.2
  • 51
    • 0027389529 scopus 로고
    • Binding of pertussis toxin to lipid vesicles containing glycolipids
    • Hausman, S. Z. and Burns, D. L. (1993) Binding of pertussis toxin to lipid vesicles containing glycolipids Infect. Immun. 61, 335-337
    • (1993) Infect. Immun. , vol.61 , pp. 335-337
    • Hausman, S.Z.1    Burns, D.L.2
  • 52
    • 0029065020 scopus 로고
    • Effects of solute multivalence on the evaluation of binding constants by biosensor technology: Studies with concanavalin A and interleukin-6 as partitioning proteins
    • Kalinin, N. L., Ward, L. D., and Winzor, D. J. (1995) Effects of solute multivalence on the evaluation of binding constants by biosensor technology: Studies with concanavalin A and interleukin-6 as partitioning proteins Anal. Biochem. 228, 238-244
    • (1995) Anal. Biochem. , vol.228 , pp. 238-244
    • Kalinin, N.L.1    Ward, L.D.2    Winzor, D.J.3
  • 53
    • 24044481642 scopus 로고    scopus 로고
    • New mutant Chinese hamster ovary cell representing an unknown gene for attachment of glycosylphosphatidylinositol to proteins
    • Hong, Y., Kang, J. Y., Kim, Y. U., Shin, D. J., Choy, H. E., Maeda, Y., and Kinoshita, T. (2005) New mutant Chinese hamster ovary cell representing an unknown gene for attachment of glycosylphosphatidylinositol to proteins Biochem. Biophys. Res. Commun. 335, 1060-1069
    • (2005) Biochem. Biophys. Res. Commun. , vol.335 , pp. 1060-1069
    • Hong, Y.1    Kang, J.Y.2    Kim, Y.U.3    Shin, D.J.4    Choy, H.E.5    Maeda, Y.6    Kinoshita, T.7
  • 54
    • 0036792614 scopus 로고    scopus 로고
    • Requirement of N-glycan on GPI-anchored proteins for efficient binding of aerolysin but not Clostridium septicum α-toxin
    • Hong, Y., Ohishi, K., Inoue, N., Kang, J. Y., Shime, H., Horiguchi, Y., van der Goot, F. G., Sugimoto, N., and Kinoshita, T. (2002) Requirement of N-glycan on GPI-anchored proteins for efficient binding of aerolysin but not Clostridium septicum α-toxin EMBO J. 21, 5047-5056
    • (2002) EMBO J. , vol.21 , pp. 5047-5056
    • Hong, Y.1    Ohishi, K.2    Inoue, N.3    Kang, J.Y.4    Shime, H.5    Horiguchi, Y.6    Van Der Goot, F.G.7    Sugimoto, N.8    Kinoshita, T.9
  • 55
    • 33947602811 scopus 로고    scopus 로고
    • Siglecs and their roles in the immune system
    • Crocker, P. R., Paulson, J. C., and Varki, A. (2007) Siglecs and their roles in the immune system Nat. Rev. Immunol. 7, 255-266
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 255-266
    • Crocker, P.R.1    Paulson, J.C.2    Varki, A.3
  • 56
    • 33751524059 scopus 로고    scopus 로고
    • Probing the cis interactions of the inhibitory receptor Siglec-7 with α2,8-disialylated ligands on natural killer cells and other leukocytes using glycan-specific antibodies and by analysis of α2,8-sialyltransferase gene expression
    • Avril, T., North, S. J., Haslam, S. M., Willison, H. J., and Crocker, P. R. (2006) Probing the cis interactions of the inhibitory receptor Siglec-7 with α2,8-disialylated ligands on natural killer cells and other leukocytes using glycan-specific antibodies and by analysis of α2,8-sialyltransferase gene expression J. Leukocyte Biol. 80, 787-796
    • (2006) J. Leukocyte Biol. , vol.80 , pp. 787-796
    • Avril, T.1    North, S.J.2    Haslam, S.M.3    Willison, H.J.4    Crocker, P.R.5


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