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Volumn 246, Issue 2, 1997, Pages 320-327

Comparison of the diphtheria mutant toxin, CRM197, with a Haemophilus influenzae type-b polysaccharide-CRM197 conjugate by optical spectroscopy

Author keywords

Circular dichroism; Fluorescence spectroscopy; Haemophilus influenzae; Polysaccharide; Vaccine

Indexed keywords

DIPHTHERIA TOXIN; HAEMOPHILUS INFLUENZAE TYPE B VACCINE;

EID: 0030958582     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00320.x     Document Type: Article
Times cited : (32)

References (41)
  • 1
    • 0022500925 scopus 로고
    • Vaccines consisting of periodate-cleaved oligosaccharides from the capsule of Haemophilus influenzae type b coupied to a protein carrier: Structural and temporal requirements for priming in the human infant
    • Anderson, P. W., Pichichero, M. E., Insel, R. A., Betts, R., Eby, R. & Smith, D. H. (1986) Vaccines consisting of periodate-cleaved oligosaccharides from the capsule of Haemophilus influenzae type b coupied to a protein carrier: structural and temporal requirements for priming in the human infant, J. Immunol. 137, 1181-1186.
    • (1986) J. Immunol. , vol.137 , pp. 1181-1186
    • Anderson, P.W.1    Pichichero, M.E.2    Insel, R.A.3    Betts, R.4    Eby, R.5    Smith, D.H.6
  • 2
    • 0030031666 scopus 로고    scopus 로고
    • Crystal structure of diphtheria toxin bound to nicotinamide adenine dinucleotide
    • Bell, C. E. & Eisenberg, D. (1996) Crystal structure of diphtheria toxin bound to nicotinamide adenine dinucleotide, Biochemistry 35, 1137-1149.
    • (1996) Biochemistry , vol.35 , pp. 1137-1149
    • Bell, C.E.1    Eisenberg, D.2
  • 3
    • 0028204771 scopus 로고
    • Domain swapping: Entangling alliances between proteins
    • Bennett, M. J., Choe, S. & Eisenberg, D. (1994) Domain swapping: entangling alliances between proteins, Proc. Natl Acad. Sci. USA 91, 3127-3131.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 3127-3131
    • Bennett, M.J.1    Choe, S.2    Eisenberg, D.3
  • 4
    • 0028077639 scopus 로고
    • Refined structure of monomeric diphtheria toxin at 2.3 Å resolution
    • Bennett, M. J. & Eisenberg, D. (1994) Refined structure of monomeric diphtheria toxin at 2.3 Å resolution, Protein Science 3, 1464-1475.
    • (1994) Protein Science , vol.3 , pp. 1464-1475
    • Bennett, M.J.1    Eisenberg, D.2
  • 5
    • 0023667488 scopus 로고
    • Conformational changes in diphtheria toxoids:analysis with monoclonal antibodies
    • Bigio, M., Rossi, R., Nucci, D., Antoni, G., Rappouli, R. & Ratti, G. (1987) Conformational changes in diphtheria toxoids:analysis with monoclonal antibodies, FEBS Lett. 218, 271-276.
    • (1987) FEBS Lett. , vol.218 , pp. 271-276
    • Bigio, M.1    Rossi, R.2    Nucci, D.3    Antoni, G.4    Rappouli, R.5    Ratti, G.6
  • 6
    • 0026033321 scopus 로고
    • Efficacy in infancy of oligosaccharide conjugate Haemophilus influenzae type b (HbOC) vaccine in a United States population of 61,080 children
    • Black, S. B., Shinefield, H. R., Fireman, B., Hiatt, R., Polen, M. & Vittinghoff, E. J. (1991) Efficacy in infancy of oligosaccharide conjugate Haemophilus influenzae type b (HbOC) vaccine in a United States population of 61,080 children, Pediatr. Inf. Dis. J. 10, 97-104.
    • (1991) Pediatr. Inf. Dis. J. , vol.10 , pp. 97-104
    • Black, S.B.1    Shinefield, H.R.2    Fireman, B.3    Hiatt, R.4    Polen, M.5    Vittinghoff, E.J.6
  • 7
    • 0022397324 scopus 로고
    • Effect of pH on the conformation of diphtheria toxin and its implications for membrane penetration
    • Blewitt, M. G., Chung, L. A. & London, E. (1985) Effect of pH on the conformation of diphtheria toxin and its implications for membrane penetration, Biochemistry 24, 5458-5464.
    • (1985) Biochemistry , vol.24 , pp. 5458-5464
    • Blewitt, M.G.1    Chung, L.A.2    London, E.3
  • 8
    • 0021765180 scopus 로고
    • Fluorescence characterization of the low pH-induced change in diphtheria toxin conformation: Effect of salt
    • Blewitt, M. G., Zhao, J.-M., McKeever, B., Sarma, R. & London, E. (1984) Fluorescence characterization of the low pH-induced change in diphtheria toxin conformation: effect of salt, Biochem. Biophys. Res. Commun. 120, 286-290.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 286-290
    • Blewitt, M.G.1    Zhao, J.-M.2    McKeever, B.3    Sarma, R.4    London, E.5
  • 9
    • 0029441978 scopus 로고
    • Structural information on proteins from circular dichroism spectroscopy: Possibilities and limitations
    • (Herron, J. N., Jiskoot, W. & Crommelin, D. J. A., eds) Plenum Press, New York
    • Bloemendal, M. & Johnson, N. C. Jr (1995) Structural information on proteins from circular dichroism spectroscopy: possibilities and limitations, in Physical methods to characterize pharmaceutical proteins (Herron, J. N., Jiskoot, W. & Crommelin, D. J. A., eds) pp. 65-100, Plenum Press, New York.
    • (1995) Physical Methods to Characterize Pharmaceutical Proteins , pp. 65-100
    • Bloemendal, M.1    Johnson Jr., N.C.2
  • 11
    • 0022002539 scopus 로고
    • Circular dichroism of diphtheria toxin, Pseudomonas aeruginsoa exotoxin A, and various derivatives
    • Collins, C. M. & Collier, R. J. (1985) Circular dichroism of diphtheria toxin, Pseudomonas aeruginsoa exotoxin A, and various derivatives, Biochem. Biophys. Acta 828, 138-143.
    • (1985) Biochem. Biophys. Acta , vol.828 , pp. 138-143
    • Collins, C.M.1    Collier, R.J.2
  • 12
    • 0022504570 scopus 로고
    • Pseudomonas aeruginosa polysaccharide-tetanus toxoid conjugate vaccine: Safety and immunogenicity in humans
    • Cryz, S. J. Jr, Sadoff, J. C., Fürer, E. & Germanier, R. (1986) Pseudomonas aeruginosa polysaccharide-tetanus toxoid conjugate vaccine: safety and immunogenicity in humans, J. Infect. Dis. 154, 682-688.
    • (1986) J. Infect. Dis. , vol.154 , pp. 682-688
    • Cryz Jr., S.J.1    Sadoff, J.C.2    Fürer, E.3    Germanier, R.4
  • 13
    • 0023905346 scopus 로고
    • The pH-dependent conformational change of diphtheria toxin
    • Dumont, M. E. & Richards, F. M. (1988) The pH-dependent conformational change of diphtheria toxin, J. Biol. Chem. 263, 2087-2097.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2087-2097
    • Dumont, M.E.1    Richards, F.M.2
  • 14
    • 0019593952 scopus 로고
    • Fluorescence quenching studies with proteins
    • Eftink, M. R. & Ghiron, C. A. (1981) Fluorescence quenching studies with proteins, Anal. Biochem. 114, 199-227.
    • (1981) Anal. Biochem. , vol.114 , pp. 199-227
    • Eftink, M.R.1    Ghiron, C.A.2
  • 15
    • 0026348591 scopus 로고
    • Comparative immunogenicity of conjugates composed of the Staphylococcus aureus type 8 capsular polysaccharide bound to carrier proteins by adipic acid dihydrazide or N-succinimidyl-3-(2-pyridyldithio)propionate
    • Fattom, A., Shiloach, J., Bryla, D., Fitzgerald, D., Pastan, I., Karakawa, W. W., Robbins, J. B. & Schneerson, R. (1992) Comparative immunogenicity of conjugates composed of the Staphylococcus aureus type 8 capsular polysaccharide bound to carrier proteins by adipic acid dihydrazide or N-succinimidyl-3-(2-pyridyldithio)propionate, Infect. Immunity 60, 584-589.
    • (1992) Infect. Immunity , vol.60 , pp. 584-589
    • Fattom, A.1    Shiloach, J.2    Bryla, D.3    Fitzgerald, D.4    Pastan, I.5    Karakawa, W.W.6    Robbins, J.B.7    Schneerson, R.8
  • 16
    • 0021770611 scopus 로고
    • The amino-acid sequence of two non-toxic mutants of diphtheria toxin: CRM45 and CRM197
    • Giannini, G., Rappouli, R. & Ratti, G. (1984) The amino-acid sequence of two non-toxic mutants of diphtheria toxin: CRM45 and CRM197, Nucleic Acids Res. 12, 4063-4069.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 4063-4069
    • Giannini, G.1    Rappouli, R.2    Ratti, G.3
  • 17
    • 84942950518 scopus 로고
    • Effect of carrier protein priming on antibody responses to Haemophilus influenzae type b conjugate vaccines in infants
    • Granoff, D. M., Holmes, S. J., Belshe, R. B., Osterholm, M. T., McHugh, J. E. & Anderson, E. L. (1994) Effect of carrier protein priming on antibody responses to Haemophilus influenzae type b conjugate vaccines in infants, J. Am. Med. Assoc. 272, 1116-1121.
    • (1994) J. Am. Med. Assoc. , vol.272 , pp. 1116-1121
    • Granoff, D.M.1    Holmes, S.J.2    Belshe, R.B.3    Osterholm, M.T.4    McHugh, J.E.5    Anderson, E.L.6
  • 18
    • 0026536335 scopus 로고
    • Solution structure of a calmodulin-target peptide complex by multidimensional NMR
    • Ikura, M., Clore, G. M., Gronenborn, A. M., Zhu, G., Klee, C. B. & Bax, A. (1992) Solution structure of a calmodulin-target peptide complex by multidimensional NMR, Science 256, 632-638.
    • (1992) Science , vol.256 , pp. 632-638
    • Ikura, M.1    Clore, G.M.2    Gronenborn, A.M.3    Zhu, G.4    Klee, C.B.5    Bax, A.6
  • 19
    • 0030330564 scopus 로고    scopus 로고
    • Physicochemical studies of the structure and stability of polysaccharide-protein conjugate vaccines
    • Jones, C., Crane, D. T., Lemercinier, X., Bolgiano, B. & Yost, S. E. (1996) Physicochemical studies of the structure and stability of polysaccharide-protein conjugate vaccines, Dev. Biol. Stand. 87, 143-151.
    • (1996) Dev. Biol. Stand. , vol.87 , pp. 143-151
    • Jones, C.1    Crane, D.T.2    Lemercinier, X.3    Bolgiano, B.4    Yost, S.E.5
  • 20
    • 0003022448 scopus 로고
    • Luminescence of polypeptides and proteins
    • (Steiner, R. F. & Weinryb, I., eds) Plenum Press, New York
    • Longworth, J. W. (1971) Luminescence of polypeptides and proteins, in Excited states of proteins and nucleic acids (Steiner, R. F. & Weinryb, I., eds) pp. 405-408, Plenum Press, New York.
    • (1971) Excited States of Proteins and Nucleic Acids , pp. 405-408
    • Longworth, J.W.1
  • 21
    • 0019273844 scopus 로고
    • Ligand interactions of diphtheria toxin: Relationships betwen the NAD site and the P site
    • Lory, S., Carroll, S. F. & Collier, R. J. (1980) Ligand interactions of diphtheria toxin: relationships betwen the NAD site and the P site, J. Biol. Chem. 255, 12 016-12 019.
    • (1980) J. Biol. Chem. , vol.255 , pp. 12016-12019
    • Lory, S.1    Carroll, S.F.2    Collier, R.J.3
  • 22
    • 0023656828 scopus 로고
    • Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra
    • Manavalan, P. & Johnson, W. C. Jr (1987) Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra, Anal. Biochem. 67, 76-85.
    • (1987) Anal. Biochem. , vol.67 , pp. 76-85
    • Manavalan, P.1    Johnson Jr., W.C.2
  • 23
    • 0022388937 scopus 로고
    • Binding properties of diphtheria toxin to cells are altered by mutation in the fragment A domain
    • Mekada, E. & Uchida, T. (1985) Binding properties of diphtheria toxin to cells are altered by mutation in the fragment A domain, J. Biol. Chem. 260, 12 148-12 153.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12148-12153
    • Mekada, E.1    Uchida, T.2
  • 25
    • 0029880772 scopus 로고    scopus 로고
    • Molecular size characterization of Haemophilus influenzae type b polysaccharide-protein conjugate vaccines
    • Plumb, J. E. & Yost, S. E. (1996) Molecular size characterization of Haemophilus influenzae type b polysaccharide-protein conjugate vaccines, Vaccine 14, 399-404.
    • (1996) Vaccine , vol.14 , pp. 399-404
    • Plumb, J.E.1    Yost, S.E.2
  • 26
    • 0028006168 scopus 로고
    • Comparison of conjugates composed of lipopolysaccharide from Shigella flexneri type 2a detoxified by two methods and bound to tetanus toxoid
    • Polotsky, V. Y., Robbins, J. B., Bryla, D. & Schneerson, R. (1994) Comparison of conjugates composed of lipopolysaccharide from Shigella flexneri type 2a detoxified by two methods and bound to tetanus toxoid, Infect. Immunity 62, 210-214.
    • (1994) Infect. Immunity , vol.62 , pp. 210-214
    • Polotsky, V.Y.1    Robbins, J.B.2    Bryla, D.3    Schneerson, R.4
  • 27
    • 0020176542 scopus 로고
    • A constrained regularization method for inverting data represented by linear algebraic or integral equations
    • Provencher, S. W. (1982) A constrained regularization method for inverting data represented by linear algebraic or integral equations, Computer Physics Commun. 27, 213-227.
    • (1982) Computer Physics Commun. , vol.27 , pp. 213-227
    • Provencher, S.W.1
  • 28
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • Provencher, S. W. & Glöckner, J. (1981) Estimation of globular protein secondary structure from circular dichroism, Biochemistry 20, 33-37.
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glöckner, J.2
  • 29
    • 0017895366 scopus 로고
    • Conformation of diphtheria toxin and an enzymically-active fragment
    • Puett, D., Hash, J. H. & Robinson, J. P. (1978) Conformation of diphtheria toxin and an enzymically-active fragment, FEBS Lett. 89, 59-63.
    • (1978) FEBS Lett. , vol.89 , pp. 59-63
    • Puett, D.1    Hash, J.H.2    Robinson, J.P.3
  • 30
    • 0025005334 scopus 로고
    • Linked thermal and solute perturbation analysis of cooperative domain interaction in proteins: Structural stability of diphtheria toxin
    • Ramsay, G. & Freire, E. (1990) Linked thermal and solute perturbation analysis of cooperative domain interaction in proteins: structural stability of diphtheria toxin, Biochemistry 29, 8677-8683.
    • (1990) Biochemistry , vol.29 , pp. 8677-8683
    • Ramsay, G.1    Freire, E.2
  • 31
    • 0024492690 scopus 로고
    • Energetics of diphtheria toxin membrane insertion and translocation: Calorimetric characterization of the acid pH induced transition
    • Ramsay, G., Montgomery, D., Berger, D. & Freire, E. (1989) Energetics of diphtheria toxin membrane insertion and translocation: calorimetric characterization of the acid pH induced transition, Biochemistry 28, 529-533.
    • (1989) Biochemistry , vol.28 , pp. 529-533
    • Ramsay, G.1    Montgomery, D.2    Berger, D.3    Freire, E.4
  • 32
    • 0028053801 scopus 로고
    • Interaction of Haemophilus influenzae type b conjugate vaccines with diphtheria-tetanus-pertussis vaccine in control tests
    • Redhead, K., Sesardic, D., Yost, S. E., Attwell, A. M., Watkins, J., Hoy, C. S., Plumb, J. E. & Corbel, M. J. (1994) Interaction of Haemophilus influenzae type b conjugate vaccines with diphtheria-tetanus-pertussis vaccine in control tests, Vaccine 12, 1460-1466.
    • (1994) Vaccine , vol.12 , pp. 1460-1466
    • Redhead, K.1    Sesardic, D.2    Yost, S.E.3    Attwell, A.M.4    Watkins, J.5    Hoy, C.S.6    Plumb, J.E.7    Corbel, M.J.8
  • 33
    • 0028921674 scopus 로고
    • The effects of variable glycosylation on the functional activities of ribonuclease, plasminogen and tissue plasminogen activator
    • Rudd, P. M., Woods, R. J., Wormald, M. R., Opdenakker, G., Downing, A. K., Campbell, I. D. & Dwek, R. A. (1995) The effects of variable glycosylation on the functional activities of ribonuclease, plasminogen and tissue plasminogen activator, Biochim. Biophys. Acta 1248, 1-10.
    • (1995) Biochim. Biophys. Acta , vol.1248 , pp. 1-10
    • Rudd, P.M.1    Woods, R.J.2    Wormald, M.R.3    Opdenakker, G.4    Downing, A.K.5    Campbell, I.D.6    Dwek, R.A.7
  • 34
    • 0028787153 scopus 로고
    • Immunochemical analysis of the structure of diphtheria toxin shows all three domains undergo structural changes at low pH
    • Tortorella, D., Sesardic, D., Dawes, C. S. & London, E. (1995) Immunochemical analysis of the structure of diphtheria toxin shows all three domains undergo structural changes at low pH, J. Biol. Chem. 270, 27 439-27 445.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27439-27445
    • Tortorella, D.1    Sesardic, D.2    Dawes, C.S.3    London, E.4
  • 35
    • 0002877697 scopus 로고
    • Haemophilus influenzae vaccines
    • (Plotkin, S. A. & Mortimer, E. A., eds) W.B. Saunders Co., Philadelphia
    • Ward, J., Lieberman, J. M. & Cochi, S. L. (1994) Haemophilus influenzae vaccines, in Vaccines (Plotkin, S. A. & Mortimer, E. A., eds) pp. 337-386, W.B. Saunders Co., Philadelphia.
    • (1994) Vaccines , pp. 337-386
    • Ward, J.1    Lieberman, J.M.2    Cochi, S.L.3
  • 36
    • 0028913410 scopus 로고
    • Structure of the isolated catalytic domain of diphtheria toxin
    • Weiss, M. S., Blanke, S. R., Collier, R. J. & Eisenberg, D. (1995) Structure of the isolated catalytic domain of diphtheria toxin, Biochemistry 34, 773-781.
    • (1995) Biochemistry , vol.34 , pp. 773-781
    • Weiss, M.S.1    Blanke, S.R.2    Collier, R.J.3    Eisenberg, D.4
  • 37
    • 0027432395 scopus 로고
    • Stimulation of protective antibodies against type Ia and Ib Group B streptococci by a type Ia polysaccharide-tetanus toxoid conjugate vaccine
    • Wessels, M. R., Paoletti, L. C., Rodewald, A. K., Michon, F., DiFabio, J., Jennings, H. J. & Kasper, D. L. (1993) Stimulation of protective antibodies against type Ia and Ib Group B streptococci by a type Ia polysaccharide-tetanus toxoid conjugate vaccine, Infect. Immunity 61, 4760-4766.
    • (1993) Infect. Immunity , vol.61 , pp. 4760-4766
    • Wessels, M.R.1    Paoletti, L.C.2    Rodewald, A.K.3    Michon, F.4    DiFabio, J.5    Jennings, H.J.6    Kasper, D.L.7
  • 38
    • 0028048507 scopus 로고
    • Active-site mutations of diphtheria toxin: Tryptophan 50 is a major determinant of NAD affinity
    • Wilson, B. A., Blanke, S. R., Reich, K. A. & Collier, R. J. (1994) Active-site mutations of diphtheria toxin: tryptophan 50 is a major determinant of NAD affinity, J. Biol Chem. 269, 23 296-23 301.
    • (1994) J. Biol Chem. , vol.269 , pp. 23296-23301
    • Wilson, B.A.1    Blanke, S.R.2    Reich, K.A.3    Collier, R.J.4
  • 39
    • 0030250848 scopus 로고    scopus 로고
    • Physicochemical and immunological studies on the stability of free and microsphere-encapsulated tetanus toxoid in vitro
    • Xing, D. K.-L., Crane, D. T., Bolgiano, B., Corbel, M. J., Jones, C. & Sesardic, D. (1996) Physicochemical and immunological studies on the stability of free and microsphere-encapsulated tetanus toxoid in vitro, Vaccine 14, 1205-1213.
    • (1996) Vaccine , vol.14 , pp. 1205-1213
    • Xing, D.K.-L.1    Crane, D.T.2    Bolgiano, B.3    Corbel, M.J.4    Jones, C.5    Sesardic, D.6
  • 40
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Yang, J. T., Wu, C.-S. C. & Martinez, H. M. (1986) Calculation of protein conformation from circular dichroism, Methods Enzymol. 130, 208-269.
    • (1986) Methods Enzymol. , vol.130 , pp. 208-269
    • Yang, J.T.1    Wu, C.-S.C.2    Martinez, H.M.3
  • 41
    • 0001329664 scopus 로고
    • Similarity of the conformation of diphtheria toxin at high temperature to that in the membrane-penetrating low-pH state
    • Zhao, J.-M. & London, E. (1986) Similarity of the conformation of diphtheria toxin at high temperature to that in the membrane-penetrating low-pH state, Proc. Natl Acad. Sci. USA 83, 2002-2006.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 2002-2006
    • Zhao, J.-M.1    London, E.2


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