메뉴 건너뛰기




Volumn 19, Issue 5, 2006, Pages 413-422

Design and validation of a synthetic VH repertoire with tailored diversity for protein recognition

Author keywords

Antigen binding site; CDR, D1.3; Complementary determining regions; HEL; Hen egg white lysozyme; Hypervariable loops; Igs; Immunoglobulins; Phage display

Indexed keywords

HEN EGG LYSOZYME; IMMUNOGLOBULIN HEAVY CHAIN; LYSOZYME; PEPTIDE;

EID: 33748934623     PISSN: 09523499     EISSN: 10991352     Source Type: Journal    
DOI: 10.1002/jmr.796     Document Type: Article
Times cited : (14)

References (40)
  • 1
    • 1642307201 scopus 로고    scopus 로고
    • Identification of differences in the specificity-determining residues of antibodies that recognize antigens of different size: Implications for the rational design of antibody repertoires
    • Almagro JC. 2004. Identification of differences in the specificity-determining residues of antibodies that recognize antigens of different size: implications for the rational design of antibody repertoires. J. Mol. Recognit. 17: 132-143.
    • (2004) J. Mol. Recognit. , vol.17 , pp. 132-143
    • Almagro, J.C.1
  • 2
    • 0022519337 scopus 로고
    • Three-dimensional structure of an antigen-antibody complex at 2.8 A resolution
    • Amit AG, Mariuzza RA, Phillips SE, Poljak RJ. 1986. Three-dimensional structure of an antigen-antibody complex at 2.8 A resolution. Science. 233: 747-753.
    • (1986) Science , vol.233 , pp. 747-753
    • Amit, A.G.1    Mariuzza, R.A.2    Phillips, S.E.3    Poljak, R.J.4
  • 3
    • 0018654090 scopus 로고
    • Three-dimensional structure of immunoglobulins
    • Amzel LM, Poljak RJ. 1979. Three-dimensional structure of immunoglobulins. Annu. Rev. Biochem. 48: 961-997.
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 961-997
    • Amzel, L.M.1    Poljak, R.J.2
  • 5
    • 0023173201 scopus 로고
    • Prediction of the folding of short polypeptide segments by uniform conformational sampling
    • Bruccoleri RE, Karplus M. 1987. Prediction of the folding of short polypeptide segments by uniform conformational sampling. Biopolymers. 26: 137-168.
    • (1987) Biopolymers , vol.26 , pp. 137-168
    • Bruccoleri, R.E.1    Karplus, M.2
  • 6
    • 0023278330 scopus 로고
    • Canonical structures for the hypervariable regions of immunoglobulins
    • Chothia C, Lesk AM. 1987. Canonical structures for the hypervariable regions of immunoglobulins. J. Mol. Biol. 196: 901-917.
    • (1987) J. Mol. Biol. , vol.196 , pp. 901-917
    • Chothia, C.1    Lesk, A.M.2
  • 7
    • 0037227422 scopus 로고    scopus 로고
    • Analysis of the antigen combining site: Correlations between length and sequence composition of the hypervariable loops and the nature of the antigen
    • Collis AV, Brouwer AP, Martin AC. 2003. Analysis of the antigen combining site: correlations between length and sequence composition of the hypervariable loops and the nature of the antigen. J. Mol. Biol. 325: 337-354.
    • (2003) J. Mol. Biol. , vol.325 , pp. 337-354
    • Collis, A.V.1    Brouwer, A.P.2    Martin, A.C.3
  • 8
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleic acids
    • Connolly ML. 1983. Solvent-accessible surfaces of proteins and nucleic acids. Science. 221: 709-713.
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 11
    • 0033558333 scopus 로고    scopus 로고
    • Functional characterization of the somatic hypermutation process leading to antibody D1.3, a high affinity antibody directed against lysozyme
    • England P, Nageotte R, Renard M, Page AL, Bedouelle H. 1999. Functional characterization of the somatic hypermutation process leading to antibody D1.3, a high affinity antibody directed against lysozyme. J. Immunol. 162: 2129-2136.
    • (1999) J. Immunol. , vol.162 , pp. 2129-2136
    • England, P.1    Nageotte, R.2    Renard, M.3    Page, A.L.4    Bedouelle, H.5
  • 12
    • 4344714933 scopus 로고    scopus 로고
    • Synthetic antibodies from a four-amino-acid code: A dominant role for tyrosine in antigen recognition
    • Fellouse FA, Wiesmann C, Sidhu SS. 2004. Synthetic antibodies from a four-amino-acid code: a dominant role for tyrosine in antigen recognition. Proc. Natl. Acad. Sci. U S A. 101: 12467-12472.
    • (2004) Proc. Natl. Acad. Sci. U S A , vol.101 , pp. 12467-12472
    • Fellouse, F.A.1    Wiesmann, C.2    Sidhu, S.S.3
  • 14
    • 33644783935 scopus 로고    scopus 로고
    • Tyrosine plays a dominant functional role in the paratope of a synthetic antibody derived from a four amino acid code
    • Fellouse FA, Barthelemy PA, Kelley RF, Sidhu SS. 2006. Tyrosine plays a dominant functional role in the paratope of a synthetic antibody derived from a four amino acid code. J. Mol. Biol. 357: 100-114.
    • (2006) J. Mol. Biol. , vol.357 , pp. 100-114
    • Fellouse, F.A.1    Barthelemy, P.A.2    Kelley, R.F.3    Sidhu, S.S.4
  • 15
    • 0026559783 scopus 로고
    • Antibody framework residues affecting the conformation of the hypervariable loops
    • Foote J, Winter G. 1992. Antibody framework residues affecting the conformation of the hypervariable loops. J. Mol. Biol. 224: 487-499.
    • (1992) J. Mol. Biol. , vol.224 , pp. 487-499
    • Foote, J.1    Winter, G.2
  • 16
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill SC, von Hippel PH. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182: 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 20
    • 27144431943 scopus 로고    scopus 로고
    • Selecting and screening recombinant antibody libraries
    • Hoogenboom HR. 2005. Selecting and screening recombinant antibody libraries. Nat. Biotechnol. 23: 1105-1116.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1105-1116
    • Hoogenboom, H.R.1
  • 21
    • 0036290860 scopus 로고    scopus 로고
    • Reversible dimer formation and stability of the anti-tumour single-chain Fv antibody MFE-23 by neutron scattering, analytical ultracentrifugation, and NMR and FT-IR spectroscopy
    • Lee YC, Boehm MK, Chester KA, Begent RH, Perkins SJ. 2002. Reversible dimer formation and stability of the anti-tumour single-chain Fv antibody MFE-23 by neutron scattering, analytical ultracentrifugation, and NMR and FT-IR spectroscopy. J. Mol. Biol. 320: 107-127.
    • (2002) J. Mol. Biol. , vol.320 , pp. 107-127
    • Lee, Y.C.1    Boehm, M.K.2    Chester, K.A.3    Begent, R.H.4    Perkins, S.J.5
  • 22
    • 3242760800 scopus 로고    scopus 로고
    • High-affinity human antibodies from phage-displayed synthetic Fab libraries with a single framework scaffold
    • Lee CV, Liang WC, Dennis MS, Eigenbrot C, Sidhu SS, Fuh G. 2004. High-affinity human antibodies from phage-displayed synthetic Fab libraries with a single framework scaffold. J. Mol. Biol. 340: 1073-1093.
    • (2004) J. Mol. Biol. , vol.340 , pp. 1073-1093
    • Lee, C.V.1    Liang, W.C.2    Dennis, M.S.3    Eigenbrot, C.4    Sidhu, S.S.5    Fuh, G.6
  • 23
    • 0030580057 scopus 로고    scopus 로고
    • Antibody-antigen interactions: Contact analysis and binding site topography
    • MacCallum RM, Martin AC, Thornton JM. 1996. Antibody-antigen interactions: contact analysis and binding site topography. J. Mol. Biol. 262: 732-745.
    • (1996) J. Mol. Biol. , vol.262 , pp. 732-745
    • MacCallum, R.M.1    Martin, A.C.2    Thornton, J.M.3
  • 25
    • 0031775443 scopus 로고    scopus 로고
    • The complete nucleotide sequence of the human immunoglobulin heavy chain variable region locus
    • Matsuda F, Ishii K, Bourvagnet P, Kuma K, Hayashida H, MiyataT, Honjo T. 1998. The complete nucleotide sequence of the human immunoglobulin heavy chain variable region locus. J. Exp. Med. 188: 2151-2162.
    • (1998) J. Exp. Med. , vol.188 , pp. 2151-2162
    • Matsuda, F.1    Ishii, K.2    Bourvagnet, P.3    Kuma, K.4    Hayashida, H.5    Miyata, T.6    Honjo, T.7
  • 26
    • 0032536197 scopus 로고    scopus 로고
    • Conformations of the third hypervariable region in the VH domain of immunoglobulins
    • Morea V, Tramontano A, Rustici M, Chothia C, Lesk AM. 1998. Conformations of the third hypervariable region in the VH domain of immunoglobulins. J. Mol. Biol. 275: 269-294.
    • (1998) J. Mol. Biol. , vol.275 , pp. 269-294
    • Morea, V.1    Tramontano, A.2    Rustici, M.3    Chothia, C.4    Lesk, A.M.5
  • 27
    • 17644406997 scopus 로고    scopus 로고
    • From rodent reagents to human therapeutics using antibody guided selection
    • Osbourn J, Groves M, Vaughan T. 2005. From rodent reagents to human therapeutics using antibody guided selection. Methods. 36: 61-68.
    • (2005) Methods , vol.36 , pp. 61-68
    • Osbourn, J.1    Groves, M.2    Vaughan, T.3
  • 28
    • 0028798104 scopus 로고
    • Identification of specificity-determining residues in antibodies
    • Padlan EA, Abergel C, Tipper JP. 1995. Identification of specificity-determining residues in antibodies. FASEB J. 9: 133-139.
    • (1995) FASEB J. , vol.9 , pp. 133-139
    • Padlan, E.A.1    Abergel, C.2    Tipper, J.P.3
  • 29
    • 33344476078 scopus 로고    scopus 로고
    • A focused antibody library for improved hapten recognition
    • Persson H, Lantto J, Ohlin M. 2006. A focused antibody library for improved hapten recognition. J. Mol. Biol. 357: 607-620.
    • (2006) J. Mol. Biol. , vol.357 , pp. 607-620
    • Persson, H.1    Lantto, J.2    Ohlin, M.3
  • 31
    • 0033058759 scopus 로고    scopus 로고
    • H3-rules: Identification of CDR-H3 structures in antibodies
    • Shirai H, Kidera A, Nakamura H. 1999. H3-rules: identification of CDR-H3 structures in antibodies. FEBS Lett. 455: 188-197.
    • (1999) FEBS Lett. , vol.455 , pp. 188-197
    • Shirai, H.1    Kidera, A.2    Nakamura, H.3
  • 32
    • 1842609526 scopus 로고    scopus 로고
    • Phage-displayed antibody libraries of synthetic heavy chain complementarity determining regions
    • Sidhu SS, Li B, Chen Y, Fellouse FA, Eigenbrot C, Fuh G. 2004. Phage-displayed antibody libraries of synthetic heavy chain complementarity determining regions. J. Mol. Biol. 338: 299-310.
    • (2004) J. Mol. Biol. , vol.338 , pp. 299-310
    • Sidhu, S.S.1    Li, B.2    Chen, Y.3    Fellouse, F.A.4    Eigenbrot, C.5    Fuh, G.6
  • 33
    • 0028784138 scopus 로고
    • Single-step assembly of a gene and entire plasmid from large numbers of oligodeoxyribonucleotides
    • Stemmer WP, Crameri A, Ha KD, Brennan TM, Heyneker HL. 1995. Single-step assembly of a gene and entire plasmid from large numbers of oligodeoxyribonucleotides. Gene. 164: 49-53.
    • (1995) Gene , vol.164 , pp. 49-53
    • Stemmer, W.P.1    Crameri, A.2    Ha, K.D.3    Brennan, T.M.4    Heyneker, H.L.5
  • 35
    • 0022591495 scopus 로고
    • The classification of amino acid conservation
    • Taylor WR. 1986. The classification of amino acid conservation. J. Theor. Biol. 119: 205-218.
    • (1986) J. Theor. Biol. , vol.119 , pp. 205-218
    • Taylor, W.R.1
  • 36
    • 0029610794 scopus 로고
    • Canonical structure repertoire of the antigen-binding site of immunoglobulins suggests strong geometrical restrictions associated to the mechanism of immune recognition
    • Vargas-Madrazo E., Lara-Ochoa F, Almagro JC. 1995. Canonical structure repertoire of the antigen-binding site of immunoglobulins suggests strong geometrical restrictions associated to the mechanism of immune recognition. J. Mol. Biol. 254: 497-504.
    • (1995) J. Mol. Biol. , vol.254 , pp. 497-504
    • Vargas-Madrazo, E.1    Lara-Ochoa, F.2    Almagro, J.C.3
  • 39
    • 0014828908 scopus 로고
    • An analysis of the sequences of the variable regions of Bence Jones proteins and myeloma light chains and their implications for antibody complementary
    • Wu TT, Kabat EA. 1970. An analysis of the sequences of the variable regions of Bence Jones proteins and myeloma light chains and their implications for antibody complementary. J. Exp. Med. 132: 211-250.
    • (1970) J. Exp. Med. , vol.132 , pp. 211-250
    • Wu, T.T.1    Kabat, E.A.2
  • 40
    • 0031106828 scopus 로고    scopus 로고
    • Thermodynamic analysis of antigen-antibody binding using biosensor measurements at different temperatures
    • Zeder-Lutz G, Zuber E, Witz J, Van Regenmortel MH. 1997. Thermodynamic analysis of antigen-antibody binding using biosensor measurements at different temperatures. Anal. Biochem. 246: 123-132.
    • (1997) Anal. Biochem. , vol.246 , pp. 123-132
    • Zeder-Lutz, G.1    Zuber, E.2    Witz, J.3    Van Regenmortel, M.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.