메뉴 건너뛰기




Volumn 274, Issue 4, 1997, Pages 622-634

The three-dimensional structures of a polysaccharide binding antibody to cryptococcus neoformans and its complex with a peptide from a phage display library: Implications for the identification of peptide mimotopes

Author keywords

Antibody structure; Cryptococcus; Peptide; Phage library; Polysaccharide

Indexed keywords

CARBOHYDRATE BINDING PROTEIN; FUNGUS ANTIBODY; POLYSACCHARIDE;

EID: 17744417978     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1407     Document Type: Article
Times cited : (77)

References (44)
  • 1
    • 0019959784 scopus 로고
    • Protection against foot-and-mouth disease by immunization with a chemically synthesized peptide predicted from the viral nucleotide sequence
    • Bittle J. L., Houghten R. A., Alexander H., Shinnick T. M., Sutcliffe J. G., Lerner R. A., Rowlands D. J., Brown F. Protection against foot-and-mouth disease by immunization with a chemically synthesized peptide predicted from the viral nucleotide sequence. Nature. 298:1982;30-33.
    • (1982) Nature , vol.298 , pp. 30-33
    • Bittle, J.L.1    Houghten, R.A.2    Alexander, H.3    Shinnick, T.M.4    Sutcliffe, J.G.5    Lerner, R.A.6    Rowlands, D.J.7    Brown, F.8
  • 2
    • 0028939035 scopus 로고
    • Comprehensive epitope analysis of monoclonal anti-proenkephalin antibodies using phage display libraries and synthetic peptides: Revelation of antibody fine specificities caused by somatic mutations in the variable region genes
    • Bottger V., Bottger A., Lane E. B., Spruce B. A. Comprehensive epitope analysis of monoclonal anti-proenkephalin antibodies using phage display libraries and synthetic peptides: revelation of antibody fine specificities caused by somatic mutations in the variable region genes. J. Mol. Biol. 247:1995;932-946.
    • (1995) J. Mol. Biol. , vol.247 , pp. 932-946
    • Bottger, V.1    Bottger, A.2    Lane, E.B.3    Spruce, B.A.4
  • 5
    • 0000538815 scopus 로고
    • Analytical molecular surface calculation
    • Connolly M. L. Analytical molecular surface calculation. J. Appl. Crystallog. 16:1983;548-558.
    • (1983) J. Appl. Crystallog. , vol.16 , pp. 548-558
    • Connolly, M.L.1
  • 6
    • 0026319774 scopus 로고
    • Recognitionof a cell-surface oligosaccharide of pathogenicSalmonella
    • Cygler M., Rose D. R., Bundle D. R. Recognitionof a cell-surface oligosaccharide of pathogenicSalmonella. Science. 253:1991;442-445.
    • (1991) Science , vol.253 , pp. 442-445
    • Cygler, M.1    Rose, D.R.2    Bundle, D.R.3
  • 8
    • 0030040277 scopus 로고    scopus 로고
    • Interactions of protein antigens with antibodies
    • Davies D. R., Cohen G. H. Interactions of protein antigens with antibodies. Proc. Natl Acad. Sci. USA. 93:1996;7-12.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 7-12
    • Davies, D.R.1    Cohen, G.H.2
  • 9
    • 0020517993 scopus 로고
    • Priming for and induction of anti-poliovirus neutralizing antibodies by synthetic peptides
    • Emini E. A., Jameson B. A., Wimmer E. Priming for and induction of anti-poliovirus neutralizing antibodies by synthetic peptides. Nature. 304:1983;699-703.
    • (1983) Nature , vol.304 , pp. 699-703
    • Emini, E.A.1    Jameson, B.A.2    Wimmer, E.3
  • 10
    • 0027609916 scopus 로고
    • SETOR: Hardware-lighted three-dimensional solid model representations of macromolecules
    • Evans S. V. SETOR: hardware-lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph. 11:1993;134-138.
    • (1993) J. Mol. Graph. , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 12
    • 0026757989 scopus 로고
    • Three-dimensional structure of an angiotensin II-Fab complex at 3 Å: Hormone recognition by an anti-idiotypic antibody
    • Garcia K. C., Ronco P. M., Verroust P. J., Brunger A. T., Amzel L. M. Three-dimensional structure of an angiotensin II-Fab complex at 3 Å: hormone recognition by an anti-idiotypic antibody. Science. 257:1992;502-507.
    • (1992) Science , vol.257 , pp. 502-507
    • Garcia, K.C.1    Ronco, P.M.2    Verroust, P.J.3    Brunger, A.T.4    Amzel, L.M.5
  • 16
    • 0023182368 scopus 로고
    • Human immunodeficiency virus neutralizing antibodies recognize several conserved domains on the envelope glycoproteins
    • Ho D. D., Sarngadharan M. G., Hirsch M. S., Schooley R. T., Rota T. R., Kennedy R. C., Chanh T. C., Sato V. L. Human immunodeficiency virus neutralizing antibodies recognize several conserved domains on the envelope glycoproteins. J. Virol. 61:1987;2024-2028.
    • (1987) J. Virol. , vol.61 , pp. 2024-2028
    • Ho, D.D.1    Sarngadharan, M.G.2    Hirsch, M.S.3    Schooley, R.T.4    Rota, T.R.5    Kennedy, R.C.6    Chanh, T.C.7    Sato, V.L.8
  • 17
    • 0027215581 scopus 로고
    • Identification of a peptide which binds to the carbohydrate-specific monoclonal antibody-B3
    • Hoess R., Brinkmann U., Handel T., Pastan I. Identification of a peptide which binds to the carbohydrate-specific monoclonal antibody-B3. Gene. 128:1993;43-49.
    • (1993) Gene , vol.128 , pp. 43-49
    • Hoess, R.1    Brinkmann, U.2    Handel, T.3    Pastan, I.4
  • 21
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R. A., MacArthur M. N., Moss D. S., Thornton J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.N.2    Moss, D.S.3    Thornton, J.M.4
  • 22
    • 0027410832 scopus 로고
    • The basics of binding: Mechanisms of antigen recognition and mimicry by antibodies
    • Mariuzza R. A., Poljak R. J. The basics of binding: mechanisms of antigen recognition and mimicry by antibodies. Curr. Opin. Immunol. 5:1993;50-55.
    • (1993) Curr. Opin. Immunol. , vol.5 , pp. 50-55
    • Mariuzza, R.A.1    Poljak, R.J.2
  • 23
    • 0026495128 scopus 로고
    • Protective murine monoclonal antibodies toCryptococcus neoformans
    • Mukherjee J., Scharff M. D., Casadevall A. Protective murine monoclonal antibodies toCryptococcus neoformans. Infect. Immun. 60:1992;4534-4541.
    • (1992) Infect. Immun. , vol.60 , pp. 4534-4541
    • Mukherjee, J.1    Scharff, M.D.2    Casadevall, A.3
  • 24
    • 0027403745 scopus 로고
    • Molecular characterization of the humoral responses toCryptococcus neoformans
    • Mukherjee J., Casadevall A., Scharff M. D. Molecular characterization of the humoral responses toCryptococcus neoformans. J. Exp. Med. 177:1993;1105-1116.
    • (1993) J. Exp. Med. , vol.177 , pp. 1105-1116
    • Mukherjee, J.1    Casadevall, A.2    Scharff, M.D.3
  • 25
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K. A., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 26
    • 0028140144 scopus 로고
    • Protein-polysaccharide interactions. A monoclonal antibody specific for the capsular polysaccharide ofCryptococcus neoformans
    • Otteson E. W., Welch W. H., Kozel T. R. Protein-polysaccharide interactions. A monoclonal antibody specific for the capsular polysaccharide ofCryptococcus neoformans. J. Biol. Chem. 269:1994;1858-1864.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1858-1864
    • Otteson, E.W.1    Welch, W.H.2    Kozel, T.R.3
  • 27
    • 0026587998 scopus 로고
    • Structural evidence for induced fit as a mechanism for antibody-antigen recognition
    • Rini J. M., Schulze-Gahmen U., Wilson I. A. Structural evidence for induced fit as a mechanism for antibody-antigen recognition. Science. 255:1992;959-965.
    • (1992) Science , vol.255 , pp. 959-965
    • Rini, J.M.1    Schulze-Gahmen, U.2    Wilson, I.A.3
  • 28
    • 0027325038 scopus 로고
    • Crystal structure of a human immunodeficiency virus type 1 neutralizing antibody, 50.1, in complex with its V3 loop peptide antigen
    • Rini J. M., Stanfield R. L., Stura E. A., Salinas P. A., Profy A. T., Wilson I. A. Crystal structure of a human immunodeficiency virus type 1 neutralizing antibody, 50.1, in complex with its V3 loop peptide antigen. Proc. Natl Acad. Sci. USA. 90:1993;6325-6329.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6325-6329
    • Rini, J.M.1    Stanfield, R.L.2    Stura, E.A.3    Salinas, P.A.4    Profy, A.T.5    Wilson, I.A.6
  • 30
    • 0027133936 scopus 로고
    • Detailed analysis of the free and bound conformations of an antibody. X-ray structures of Fab 17/9 and three different Fab-peptide complexes
    • Schulze-Gahmen U., Rini J. M., Wilson I. A. Detailed analysis of the free and bound conformations of an antibody. X-ray structures of Fab 17/9 and three different Fab-peptide complexes. J. Mol. Biol. 234:1993;1098-1118.
    • (1993) J. Mol. Biol. , vol.234 , pp. 1098-1118
    • Schulze-Gahmen, U.1    Rini, J.M.2    Wilson, I.A.3
  • 31
    • 0026654781 scopus 로고
    • Discovering peptide ligands using epitope libraries
    • Scott J. K. Discovering peptide ligands using epitope libraries. Trends Biochem. Sci. 17:1992;241-245.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 241-245
    • Scott, J.K.1
  • 32
    • 0025112794 scopus 로고
    • Searching for peotide ligands with an epitope library
    • Scott J. K., Smith G. P. Searching for peotide ligands with an epitope library. Science. 249:1990;386-390.
    • (1990) Science , vol.249 , pp. 386-390
    • Scott, J.K.1    Smith, G.P.2
  • 33
    • 0027301875 scopus 로고
    • Crystal structure of an anticholera toxin peptide complex at 2.3 Å
    • Shoham M. Crystal structure of an anticholera toxin peptide complex at 2.3 Å J. Mol. Biol. 232:1993;1169-1175.
    • (1993) J. Mol. Biol. , vol.232 , pp. 1169-1175
    • Shoham, M.1
  • 34
    • 0000289157 scopus 로고
    • X-ray crystallographic studies of antibody-peptide complexes
    • Stanfield R. L., Wilson I. A. X-ray crystallographic studies of antibody-peptide complexes. Immunomethods. 3:1993;211-221.
    • (1993) Immunomethods , vol.3 , pp. 211-221
    • Stanfield, R.L.1    Wilson, I.A.2
  • 35
    • 0025321903 scopus 로고
    • Crystal structures of an antibody to a peptide and its complex with peptide antigen at 2.8 Å
    • Stanfield R. L., Fieser T. M., Lerner R. A., Wilson I. A. Crystal structures of an antibody to a peptide and its complex with peptide antigen at 2.8 Å Science. 248:1990;712-719.
    • (1990) Science , vol.248 , pp. 712-719
    • Stanfield, R.L.1    Fieser, T.M.2    Lerner, R.A.3    Wilson, I.A.4
  • 37
    • 0028304866 scopus 로고
    • Crystal structure of a human rhinovirus neutralizing antibody complexed with a peptide derived from viral capsid protein VP2
    • Tormo J., Blaas D., Parry N. R., Rowlands D., Stuart D., Fita I. Crystal structure of a human rhinovirus neutralizing antibody complexed with a peptide derived from viral capsid protein VP2. EMBO J. 13:1994;2247-2256.
    • (1994) EMBO J. , vol.13 , pp. 2247-2256
    • Tormo, J.1    Blaas, D.2    Parry, N.R.3    Rowlands, D.4    Stuart, D.5    Fita, I.6
  • 38
    • 84913050729 scopus 로고
    • An efficient general purpose least-squares refinement program for macromolecular structures
    • Tronrud D. E., Ten Eyck L. F., Matthews B. W. An efficient general purpose least-squares refinement program for macromolecular structures. Acta Crystallog. sect. A. 43:1987;489-501.
    • (1987) Acta Crystallog. Sect. A , vol.43 , pp. 489-501
    • Tronrud, D.E.1    Ten Eyck, L.F.2    Matthews, B.W.3
  • 39
    • 0030576498 scopus 로고    scopus 로고
    • Peptide libraries define the fine specificity of anti-polysaccharide antibodies toCryptococcus neoformans
    • Valadon P., Nussbaum G., Boyd L. F., Margulies D. H., Scharff M. D. Peptide libraries define the fine specificity of anti-polysaccharide antibodies toCryptococcus neoformans. J. Mol. Biol. 261:1996;11-22.
    • (1996) J. Mol. Biol. , vol.261 , pp. 11-22
    • Valadon, P.1    Nussbaum, G.2    Boyd, L.F.3    Margulies, D.H.4    Scharff, M.D.5
  • 40
    • 0029019739 scopus 로고
    • Structure of the major antigenic loop of foot-and-mouth disease virus complexed with a neutralizing antibody: Direct involvement of the Arg-Gly-Asp motif in the interaction
    • Verdaguer N., Mateu M. G., Andreu D., Giralt E., Domingo E., Fita I. Structure of the major antigenic loop of foot-and-mouth disease virus complexed with a neutralizing antibody: direct involvement of the Arg-Gly-Asp motif in the interaction. EMBO J. 14:1995;1690-1696.
    • (1995) EMBO J. , vol.14 , pp. 1690-1696
    • Verdaguer, N.1    Mateu, M.G.2    Andreu, D.3    Giralt, E.4    Domingo, E.5    Fita, I.6
  • 41
    • 0029867609 scopus 로고    scopus 로고
    • Induced pocket to accommodate the cell attachment Arg-Gly-Asp motif in a neutralizing antibody against foot-and-mounth-disease virus
    • Verdaguer N., Mateu M. G., Bravo J., Domingo E., Fita I. Induced pocket to accommodate the cell attachment Arg-Gly-Asp motif in a neutralizing antibody against foot-and-mounth-disease virus. J. Mol. Biol. 256:1996;364-376.
    • (1996) J. Mol. Biol. , vol.256 , pp. 364-376
    • Verdaguer, N.1    Mateu, M.G.2    Bravo, J.3    Domingo, E.4    Fita, I.5
  • 42
    • 0028938936 scopus 로고
    • Structure of the complex between the Fab fragment of a neutralizing antibody for type 1 poliovirus and its viral epitope
    • Wien M. W., Filman D. J., Stura E. A., Guillot S., Delpeyroux F., Crainic R., Hogle J. M. Structure of the complex between the Fab fragment of a neutralizing antibody for type 1 poliovirus and its viral epitope. Nature Struct. Biol. 2:1995;232-243.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 232-243
    • Wien, M.W.1    Filman, D.J.2    Stura, E.A.3    Guillot, S.4    Delpeyroux, F.5    Crainic, R.6    Hogle, J.M.7
  • 43
    • 0028606741 scopus 로고
    • Antibody-antigen interactions: New structures and new conformational changes
    • Wilson I. A., Stanfield R. L. Antibody-antigen interactions: new structures and new conformational changes. Curr. Opin. Struct. Biol. 4:1994;857-867.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 857-867
    • Wilson, I.A.1    Stanfield, R.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.