메뉴 건너뛰기




Volumn 16, Issue 1, 2009, Pages 37-42

Thermodynamics and density of binding of a panel of antibodies to high-molecular-weight capsular polysaccharides

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN F(AB) FRAGMENT; MONOCLONAL ANTIBODY; MONOSACCHARIDE; POLYSACCHARIDE; POLYSACCHARIDE ANTIBODY; UNCLASSIFIED DRUG;

EID: 58149382189     PISSN: 15566811     EISSN: 1556679X     Source Type: Journal    
DOI: 10.1128/CVI.00290-08     Document Type: Article
Times cited : (6)

References (47)
  • 1
    • 0037418783 scopus 로고    scopus 로고
    • Characterization of the heterogeneous arabinoxylans by direct imaging of individual molecules by atomic force microscopy
    • Adams, E. L., P. A. Kroon, G. Williamson, and V. J. Morris. 2003. Characterization of the heterogeneous arabinoxylans by direct imaging of individual molecules by atomic force microscopy. Carbohydr. Res. 338:771-780.
    • (2003) Carbohydr. Res , vol.338 , pp. 771-780
    • Adams, E.L.1    Kroon, P.A.2    Williamson, G.3    Morris, V.J.4
  • 2
    • 0015514893 scopus 로고
    • Thermodynamics of the binding of 2,4-dinitrophenyl and 2,4,6-trinitrophenyl haptens to the homologous and heterologous rabbit antibodies
    • Barisas, B. G., S. J. Singer, and J. M. Sturtevant. 1972. Thermodynamics of the binding of 2,4-dinitrophenyl and 2,4,6-trinitrophenyl haptens to the homologous and heterologous rabbit antibodies. Biochemistry 11:2741-2744.
    • (1972) Biochemistry , vol.11 , pp. 2741-2744
    • Barisas, B.G.1    Singer, S.J.2    Sturtevant, J.M.3
  • 3
    • 0015233809 scopus 로고
    • Thermodynamics of the binding of haptens to rabbit anit-2,4-dinitrophenyl antibodies
    • Barisas, B. G., J. M. Sturtevant, and S. J. Singer. 1971. Thermodynamics of the binding of haptens to rabbit anit-2,4-dinitrophenyl antibodies. Biochemistry 10:2816-2821.
    • (1971) Biochemistry , vol.10 , pp. 2816-2821
    • Barisas, B.G.1    Sturtevant, J.M.2    Singer, S.J.3
  • 6
    • 0026683648 scopus 로고
    • Helical epitope of the group B meningococcal alpha(2-8)-linked sialic acid polysaccharide
    • Brisson, J. R., H. Baumann, A. Imberty, S. Perez, and H. J. Jennings. 1992. Helical epitope of the group B meningococcal alpha(2-8)-linked sialic acid polysaccharide. Biochemistry 31:4996-5004.
    • (1992) Biochemistry , vol.31 , pp. 4996-5004
    • Brisson, J.R.1    Baumann, H.2    Imberty, A.3    Perez, S.4    Jennings, H.J.5
  • 7
    • 0030953911 scopus 로고    scopus 로고
    • NMR and molecular dynamics studies of the conformational epitope of the type III group B Streptococcus capsular polysaccharide and derivatives
    • Brisson, J. R., S. Uhrinova, R. J. Woods, M. van der Zwan, H. C. Jarrell, L. C. Paoletti, D. L. Kasper, and H. J. Jennings. 1997. NMR and molecular dynamics studies of the conformational epitope of the type III group B Streptococcus capsular polysaccharide and derivatives. Biochemistry 36:3278-3292.
    • (1997) Biochemistry , vol.36 , pp. 3278-3292
    • Brisson, J.R.1    Uhrinova, S.2    Woods, R.J.3    van der Zwan, M.4    Jarrell, H.C.5    Paoletti, L.C.6    Kasper, D.L.7    Jennings, H.J.8
  • 10
    • 0028672570 scopus 로고
    • Determination of accurate thermodynamics of binding by titration microcalorimetry
    • Bundle, D. R., and B. W. Sigurskjold. 1994. Determination of accurate thermodynamics of binding by titration microcalorimetry. Methods Enzymol. 247:288-305.
    • (1994) Methods Enzymol , vol.247 , pp. 288-305
    • Bundle, D.R.1    Sigurskjold, B.W.2
  • 11
    • 0029043808 scopus 로고
    • Evidence for the extended helical nature of polysaccharide epitopes. The 2.8 Å resolution structure and thermodynamics of ligand binding of an antigen binding fragment specific for alpha-(238)-polysialic acid
    • Evans, S. V., B. W. Sigurskjold, H. J. Jennings, J. R. Brisson, R. To, W. C. Tse, E. Altman, M. Frosch, C. Weisgerber, H. D. Kratzin, et al. 1995. Evidence for the extended helical nature of polysaccharide epitopes. The 2.8 Å resolution structure and thermodynamics of ligand binding of an antigen binding fragment specific for alpha-(238)-polysialic acid. Biochemistry 34: 6737-6744.
    • (1995) Biochemistry , vol.34 , pp. 6737-6744
    • Evans, S.V.1    Sigurskjold, B.W.2    Jennings, H.J.3    Brisson, J.R.4    To, R.5    Tse, W.C.6    Altman, E.7    Frosch, M.8    Weisgerber, C.9    Kratzin, H.D.10
  • 12
    • 0031915833 scopus 로고    scopus 로고
    • The how and why of protein-carbohydrate interaction: A primer to the theoretical concept and a guide to application in drug design
    • Gabius, H. J. 1998. The how and why of protein-carbohydrate interaction: a primer to the theoretical concept and a guide to application in drug design. Pharm. Res. 15:23-30.
    • (1998) Pharm. Res , vol.15 , pp. 23-30
    • Gabius, H.J.1
  • 13
    • 0021766668 scopus 로고
    • Mapping of subsites in the combining area of monoclonal anti-galactan immunoglobulin A
    • Glaudemans, C. P., P. Kovac, and K. Rasmussen. 1984. Mapping of subsites in the combining area of monoclonal anti-galactan immunoglobulin A J539. Biochemistry 23:6732-6736.
    • (1984) J539. Biochemistry , vol.23 , pp. 6732-6736
    • Glaudemans, C.P.1    Kovac, P.2    Rasmussen, K.3
  • 14
    • 0016636781 scopus 로고
    • The thermodynamics of hapten and antigen binding by rabbit anti-dinitrophenyl antibody
    • Halsey, J. F., and R. L. Biltonen. 1975. The thermodynamics of hapten and antigen binding by rabbit anti-dinitrophenyl antibody. Biochemistry 14:800-804.
    • (1975) Biochemistry , vol.14 , pp. 800-804
    • Halsey, J.F.1    Biltonen, R.L.2
  • 16
    • 34248390155 scopus 로고    scopus 로고
    • Avidity of the immunoglobulin G response to a Neisseria meningitidis group C polysaccharide conjugate vaccine as measured by inhibition and chaotropic enzyme-linked immunosorbent assays
    • Harris, S. L., H. Tsao, L. Ashton, D. Goldblatt, and P. Fernsten. 2007. Avidity of the immunoglobulin G response to a Neisseria meningitidis group C polysaccharide conjugate vaccine as measured by inhibition and chaotropic enzyme-linked immunosorbent assays. Clin. Vaccine Immunol. 14:397-403.
    • (2007) Clin. Vaccine Immunol , vol.14 , pp. 397-403
    • Harris, S.L.1    Tsao, H.2    Ashton, L.3    Goldblatt, D.4    Fernsten, P.5
  • 17
    • 0028280409 scopus 로고
    • Isothermal titration calorimetric study of the association of hen egg lysozyme and the antilysozyme antibody HyHEL-5
    • Hibbits, K. A., D. S. Gill, and R. C. Willson. 1994. Isothermal titration calorimetric study of the association of hen egg lysozyme and the antilysozyme antibody HyHEL-5. Biochemistry 33:3584-3590.
    • (1994) Biochemistry , vol.33 , pp. 3584-3590
    • Hibbits, K.A.1    Gill, D.S.2    Willson, R.C.3
  • 18
    • 0015833225 scopus 로고
    • Spectral changes on binding of oligosaccharides to murine immunoglobulin A myeloma proteins
    • Jolley, M. E., S. Rudikoff, M. Potter, and C. P. Glaudemans. 1973. Spectral changes on binding of oligosaccharides to murine immunoglobulin A myeloma proteins. Biochemistry 12:3039-3044.
    • (1973) Biochemistry , vol.12 , pp. 3039-3044
    • Jolley, M.E.1    Rudikoff, S.2    Potter, M.3    Glaudemans, C.P.4
  • 19
    • 0013930475 scopus 로고
    • The nature of an antigenic determinant
    • Kabat, E. A. 1966. The nature of an antigenic determinant. J. Immunol. 97:1-11.
    • (1966) J. Immunol , vol.97 , pp. 1-11
    • Kabat, E.A.1
  • 21
    • 0031812085 scopus 로고    scopus 로고
    • Streptococcus pneumoniae type 14 polysaccharide- conjugate vaccines: Length stabilization of opsonophagocytic conformational polysaccharide epitopes
    • Laferriere, C. A., R. K. Sood, J. M. de Muys, F. Michon, and H. J. Jennings. 1998. Streptococcus pneumoniae type 14 polysaccharide- conjugate vaccines: length stabilization of opsonophagocytic conformational polysaccharide epitopes. Infect. Immun. 66:2441-2446.
    • (1998) Infect. Immun , vol.66 , pp. 2441-2446
    • Laferriere, C.A.1    Sood, R.K.2    de Muys, J.M.3    Michon, F.4    Jennings, H.J.5
  • 22
    • 0031081674 scopus 로고    scopus 로고
    • The synthesis of Streptococcus pneumoniae polysaccharide-tetanus toxoid conjugates and the effect of chain length on immunogenicity
    • Laferriere, C. A., R. K. Sood, J. M. de Muys, F. Michon, and H. J. Jennings. 1997. The synthesis of Streptococcus pneumoniae polysaccharide-tetanus toxoid conjugates and the effect of chain length on immunogenicity. Vaccine 15:179-186.
    • (1997) Vaccine , vol.15 , pp. 179-186
    • Laferriere, C.A.1    Sood, R.K.2    de Muys, J.M.3    Michon, F.4    Jennings, H.J.5
  • 23
    • 0023143005 scopus 로고
    • An integrated molecular and immunological approach towards a meningococcal group B vaccine
    • Lifely, M. R., C. Moreno, and J. C. Lindon. 1987. An integrated molecular and immunological approach towards a meningococcal group B vaccine. Vaccine 5:11-26.
    • (1987) Vaccine , vol.5 , pp. 11-26
    • Lifely, M.R.1    Moreno, C.2    Lindon, J.C.3
  • 24
    • 0023657067 scopus 로고
    • Conformational differences between linear alpha (2-8)-linked homosialooligosaccharides and the epitope of the group B meningococcal polysaccharide
    • Michon, F., J. R. Brisson, and H. J. Jennings. 1987. Conformational differences between linear alpha (2-8)-linked homosialooligosaccharides and the epitope of the group B meningococcal polysaccharide. Biochemistry 26:8399-8405.
    • (1987) Biochemistry , vol.26 , pp. 8399-8405
    • Michon, F.1    Brisson, J.R.2    Jennings, H.J.3
  • 25
    • 0017329048 scopus 로고
    • Conformation and molecular organization in fibers of the capsular polysaccharide from Escherichia coli M41 mutant
    • Moorhouse, R., W. T. Winter, S. Arnott, and M. E. Bayer. 1977. Conformation and molecular organization in fibers of the capsular polysaccharide from Escherichia coli M41 mutant. J. Mol. Biol. 109:373-391.
    • (1977) J. Mol. Biol , vol.109 , pp. 373-391
    • Moorhouse, R.1    Winter, W.T.2    Arnott, S.3    Bayer, M.E.4
  • 26
    • 17144469882 scopus 로고    scopus 로고
    • Identification of a cross-reactive epitope widely present in lipopolysaccharide from enterobacteria and recognized by the cross-protective monoclonal antibody WN1 222-5
    • Muller-Loennies, S., L. Brade, C. R. MacKenzie, F. E. Di Padova, and H. Brade. 2003. Identification of a cross-reactive epitope widely present in lipopolysaccharide from enterobacteria and recognized by the cross-protective monoclonal antibody WN1 222-5. J. Biol. Chem. 278:25618-25627.
    • (2003) J. Biol. Chem , vol.278 , pp. 25618-25627
    • Muller-Loennies, S.1    Brade, L.2    MacKenzie, C.R.3    Di Padova, F.E.4    Brade, H.5
  • 27
    • 0029873539 scopus 로고    scopus 로고
    • Observations on the binding of four anti-carbohydrate monoclonal antibodies to their homologous ligands
    • Nashed, E. M., and C. P. Glaudemans. 1996. Observations on the binding of four anti-carbohydrate monoclonal antibodies to their homologous ligands. J. Biol. Chem. 271:8209-8214.
    • (1996) J. Biol. Chem , vol.271 , pp. 8209-8214
    • Nashed, E.M.1    Glaudemans, C.P.2
  • 29
    • 0033979551 scopus 로고    scopus 로고
    • Pitner, J. B., W. F. Beyer, T. M. Venetta, C. Nycz, M. J. Mitchell, S. L. Harris, J. R. Marino-Albernas, F. I. Auzanneau, F. Forooghian, and B. M. Pinto. 2000. Bivalency and epitope specificity of a high-affinity IgG3 monoclonal antibody to the Streptococcus group A carbohydrate antigen. Molecular modeling of a Fv fragment. Carbohydr. Res. 324:17-29.
    • Pitner, J. B., W. F. Beyer, T. M. Venetta, C. Nycz, M. J. Mitchell, S. L. Harris, J. R. Marino-Albernas, F. I. Auzanneau, F. Forooghian, and B. M. Pinto. 2000. Bivalency and epitope specificity of a high-affinity IgG3 monoclonal antibody to the Streptococcus group A carbohydrate antigen. Molecular modeling of a Fv fragment. Carbohydr. Res. 324:17-29.
  • 32
    • 0028761779 scopus 로고
    • Molecular recognition of antigenic polysaccharides: A conformational comparison of capsules from Streptococcus pneumoniae serogroup 9
    • Rutherford, T. J., C. Jones, D. B. Davies, and A. C. Elliott. 1994. Molecular recognition of antigenic polysaccharides: a conformational comparison of capsules from Streptococcus pneumoniae serogroup 9. Carbohydr. Res. 265:97-111.
    • (1994) Carbohydr. Res , vol.265 , pp. 97-111
    • Rutherford, T.J.1    Jones, C.2    Davies, D.B.3    Elliott, A.C.4
  • 33
    • 0028761773 scopus 로고
    • NMR assignment and conformational analysis of the antigenic capsular polysaccharide from Streptococcus pneumoniae type 9N in aqueous solution
    • Rutherford, T. J., C. Jones, D. B. Davies, and A. C. Elliott. 1994. NMR assignment and conformational analysis of the antigenic capsular polysaccharide from Streptococcus pneumoniae type 9N in aqueous solution. Carbohydr. Res. 265:79-96.
    • (1994) Carbohydr. Res , vol.265 , pp. 79-96
    • Rutherford, T.J.1    Jones, C.2    Davies, D.B.3    Elliott, A.C.4
  • 34
    • 0037373997 scopus 로고    scopus 로고
    • Thermodynamic and kinetic aspects of antibody evolution during the immune response to hapten
    • Sagawa, T., M. Oda, M. Ishimura, K. Furukawa, and T. Azuma. 2003. Thermodynamic and kinetic aspects of antibody evolution during the immune response to hapten. Mol. Immunol. 39:801-808.
    • (2003) Mol. Immunol , vol.39 , pp. 801-808
    • Sagawa, T.1    Oda, M.2    Ishimura, M.3    Furukawa, K.4    Azuma, T.5
  • 35
    • 0015217929 scopus 로고
    • The three-dimensional structure at 6 Å resolution of a human γG1 immunoglobulin molecule
    • Sarma, V. R., E. W. Silverton, D. R. Davies, and W. D. Terry. 1971. The three-dimensional structure at 6 Å resolution of a human γG1 immunoglobulin molecule. J. Biol. Chem. 246:3753-3759.
    • (1971) J. Biol. Chem , vol.246 , pp. 3753-3759
    • Sarma, V.R.1    Silverton, E.W.2    Davies, D.R.3    Terry, W.D.4
  • 36
    • 0028956914 scopus 로고
    • Thermodynamics of antigen-antibody binding using specific antilysozyme antibodies
    • Schwarz, F. P., D. Tello, F. A. Goldbaum, R. A. Mariuzza, and R. J. Poljak. 1995. Thermodynamics of antigen-antibody binding using specific antilysozyme antibodies. Eur. J. Biochem. 228:388-394.
    • (1995) Eur. J. Biochem , vol.228 , pp. 388-394
    • Schwarz, F.P.1    Tello, D.2    Goldbaum, F.A.3    Mariuzza, R.A.4    Poljak, R.J.5
  • 38
    • 0025846921 scopus 로고
    • Sensitive titration microcalorimetric study of the binding of Salmonella O-antigenic oligosaccharides by a monoclonal antibody
    • Sigurskjold, B. W., E. Altman, and D. R. Bundle. 1991. Sensitive titration microcalorimetric study of the binding of Salmonella O-antigenic oligosaccharides by a monoclonal antibody. Eur. J. Biochem. 197:239-246.
    • (1991) Eur. J. Biochem , vol.197 , pp. 239-246
    • Sigurskjold, B.W.1    Altman, E.2    Bundle, D.R.3
  • 39
    • 0026688412 scopus 로고
    • Thermodynamics of oligosaccharide binding to a monoclonal antibody specific for a Salmonella O-antigen point to hydrophobic interactions in the binding site
    • Sigurskjold, B. W., and D. R. Bundle. 1992. Thermodynamics of oligosaccharide binding to a monoclonal antibody specific for a Salmonella O-antigen point to hydrophobic interactions in the binding site. J. Biol. Chem. 267:8371-8376.
    • (1992) J. Biol. Chem , vol.267 , pp. 8371-8376
    • Sigurskjold, B.W.1    Bundle, D.R.2
  • 40
    • 0023017207 scopus 로고
    • The galactan-binding immunoglobulin Fab J539: An X-ray diffraction study at 2.6-Å resolution
    • Suh, S. W., T. N. Bhat, M. A. Navia, G. H. Cohen, D. N. Rao, S. Rudikoff, and D. R. Davies. 1986. The galactan-binding immunoglobulin Fab J539: an X-ray diffraction study at 2.6-Å resolution. Proteins 1:74-80.
    • (1986) Proteins , vol.1 , pp. 74-80
    • Suh, S.W.1    Bhat, T.N.2    Navia, M.A.3    Cohen, G.H.4    Rao, D.N.5    Rudikoff, S.6    Davies, D.R.7
  • 41
    • 0029085689 scopus 로고
    • The affinity maturation of anti-4-hydroxy-3-nitrophenylacetyl mouse monoclonal antibody. A calorimetric study of the antigen-antibody interaction
    • Torigoe, H., T. Nakayama, M. Imazato, I. Shimada, Y. Arata, and A. Sarai. 1995. The affinity maturation of anti-4-hydroxy-3-nitrophenylacetyl mouse monoclonal antibody. A calorimetric study of the antigen-antibody interaction. J. Biol. Chem. 270:22218-22222.
    • (1995) J. Biol. Chem , vol.270 , pp. 22218-22222
    • Torigoe, H.1    Nakayama, T.2    Imazato, M.3    Shimada, I.4    Arata, Y.5    Sarai, A.6
  • 42
    • 0014202658 scopus 로고
    • Electron microscopy of an antibody-hapten complex
    • Valentine, R. C., and N. M. Green. 1967. Electron microscopy of an antibody-hapten complex. J. Mol. Biol. 27:615-617.
    • (1967) J. Mol. Biol , vol.27 , pp. 615-617
    • Valentine, R.C.1    Green, N.M.2
  • 43
    • 0037137222 scopus 로고    scopus 로고
    • Molecular recognition of oligosaccharide epitopes by a monoclonal Fab specific for Shigella flexneri Y lipopolysaccharide: X-ray structures and thermodynamics
    • Vyas, N. K., M. N. Vyas, M. C. Chervenak, M. A. Johnson, B. M. Pinto, D. R. Bundle, and F. A. Quiocho. 2002. Molecular recognition of oligosaccharide epitopes by a monoclonal Fab specific for Shigella flexneri Y lipopolysaccharide: X-ray structures and thermodynamics. Biochemistry 41:13575-13586.
    • (2002) Biochemistry , vol.41 , pp. 13575-13586
    • Vyas, N.K.1    Vyas, M.N.2    Chervenak, M.C.3    Johnson, M.A.4    Pinto, B.M.5    Bundle, D.R.6    Quiocho, F.A.7
  • 44
    • 0028788385 scopus 로고
    • Transferred nuclear Overhauser enhancement experiments show that the monoclonal antibody strep 9 selects a local minimum conformation of a Streptococcus group A trisaccharide-hapten
    • Weimar, T., S. L. Harris, J. B. Pitner, K. Bock, and B. M. Pinto. 1995. Transferred nuclear Overhauser enhancement experiments show that the monoclonal antibody strep 9 selects a local minimum conformation of a Streptococcus group A trisaccharide-hapten. Biochemistry 34:13672-13681.
    • (1995) Biochemistry , vol.34 , pp. 13672-13681
    • Weimar, T.1    Harris, S.L.2    Pitner, J.B.3    Bock, K.4    Pinto, B.M.5
  • 45
    • 0024366574 scopus 로고
    • Antibody recognition of the type 14 pneumococcal capsule. Evidence for a conformational epitope in a neutral polysaccharide
    • Wessels, M. R., and D. L. Kasper. 1989. Antibody recognition of the type 14 pneumococcal capsule. Evidence for a conformational epitope in a neutral polysaccharide. J. Exp. Med. 169:2121-2131.
    • (1989) J. Exp. Med , vol.169 , pp. 2121-2131
    • Wessels, M.R.1    Kasper, D.L.2
  • 46
    • 0023473015 scopus 로고
    • A model of high-affinity antibody binding to type III group B Streptococcus capsular polysaccharide
    • Wessels, M. R., A. Munoz, and D. L. Kasper. 1987. A model of high-affinity antibody binding to type III group B Streptococcus capsular polysaccharide. Proc. Natl. Acad. Sci. USA 84:9170-9174.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 9170-9174
    • Wessels, M.R.1    Munoz, A.2    Kasper, D.L.3
  • 47
    • 0023896585 scopus 로고
    • Thermodynamics of oligosaccharides binding to a dextran-specific monoclonal IgM
    • Zidovetzki, R., Y. Blatt, G. Schepers, and I. Pecht. 1988. Thermodynamics of oligosaccharides binding to a dextran-specific monoclonal IgM. Mol. Immunol. 25:379-383.
    • (1988) Mol. Immunol , vol.25 , pp. 379-383
    • Zidovetzki, R.1    Blatt, Y.2    Schepers, G.3    Pecht, I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.