메뉴 건너뛰기




Volumn 12, Issue 4, 2003, Pages 99-112

Predicting antigenic peptides suitable for the selection of phage antibodies

Author keywords

High throughput selection; Peptides; Phage display; Single chain antibodies

Indexed keywords

BACTERIUM ANTIBODY; POLYCLONAL ANTIBODY; PROTEIN; PROTEIN P53; PROTEIN ZNF217; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; UNCLASSIFIED DRUG;

EID: 2442660157     PISSN: 10932607     EISSN: None     Source Type: Journal    
DOI: 10.3233/hab-2003-12401     Document Type: Article
Times cited : (6)

References (56)
  • 3
    • 0034635335 scopus 로고    scopus 로고
    • Fully Synthetic Human Combinatorial Antibody Libraries (HuCAL) Based on Modular Consensus Frameworks and CDRs Randomized with Trinucleotides
    • A. Knappik, L. Ge, A. Honegger, P. Pack, M. Fischer, G. Wellnhofer, A. Hoess, J. Wolle, A. Pluckthun and B. Virnekas, Fully Synthetic Human Combinatorial Antibody Libraries (HuCAL) Based on Modular Consensus Frameworks and CDRs Randomized with Trinucleotides, J Mol Biol 296 (2000), 57-86.
    • (2000) J Mol Biol , vol.296 , pp. 57-86
    • Knappik, A.1    Ge, L.2    Honegger, A.3    Pack, P.4    Fischer, M.5    Wellnhofer, G.6    Hoess, A.7    Wolle, J.8    Pluckthun, A.9    Virnekas, B.10
  • 4
    • 0029150047 scopus 로고
    • Domain libraries: Synthetic diversity for de novo design of antibody V-regions
    • E. Soderlind, M. Vergeles and C.A. Borrebaeck, Domain libraries: synthetic diversity for de novo design of antibody V-regions, Gene 160 (1995), 269-272.
    • (1995) Gene , vol.160 , pp. 269-272
    • Soderlind, E.1    Vergeles, M.2    Borrebaeck, C.A.3
  • 5
    • 0033987925 scopus 로고    scopus 로고
    • Exploiting recombination in single bacteria to make large phage antibody libraries
    • D. Sblattero and A. Bradbury, Exploiting recombination in single bacteria to make large phage antibody libraries, Nat. Biotech. 18 (2000), 75-80.
    • (2000) Nat Biotech , vol.18 , pp. 75-80
    • Sblattero, D.1    Bradbury, A.2
  • 9
    • 0027532161 scopus 로고
    • Predicting the size of the T-cell receptor and antibody combining region from consideration of efficient self-nonself discrimination
    • J.K. Percus, O.E. Percus and A.S. Perelson, Predicting the size of the T-cell receptor and antibody combining region from consideration of efficient self-nonself discrimination, Proc Natl Acad Sci 90 (1993), 1691-1695.
    • (1993) Proc Natl Acad Sci , vol.90 , pp. 1691-1695
    • Percus, J.K.1    Percus, O.E.2    Perelson, A.S.3
  • 10
    • 0030040277 scopus 로고    scopus 로고
    • Interactions of protein antigens with antibodies
    • D.R. Davies and G.H. Cohen, Interactions of protein antigens with antibodies, Proc Natl Acad Sci 93 (1996), 7-12.
    • (1996) Proc Natl Acad Sci , vol.93 , pp. 7-12
    • Davies, D.R.1    Cohen, G.H.2
  • 11
    • 0029856410 scopus 로고    scopus 로고
    • Hydrogen bonding and solvent structure in an antigen-antibody interface. Crystal structures and thermodynamic characterization of three Fv mutants complexed with lysozyme
    • B.A. Fields, F.A. Goldbaum, W. Dall'Acqua, E.L. Malchiodi, A. Cauerhff, F.P. Schwarz, X. Ysern, R.J. Poljak and R.A. Mariuzza, Hydrogen bonding and solvent structure in an antigen-antibody interface. Crystal structures and thermodynamic characterization of three Fv mutants complexed with lysozyme, Biochemistry 35 (1996), 15494-15503.
    • (1996) Biochemistry , vol.35 , pp. 15494-15503
    • Fields, B.A.1    Goldbaum, F.A.2    Dall'Acqua, W.3    Malchiodi, E.L.4    Cauerhff, A.5    Schwarz, F.P.6    Ysern, X.7    Poljak, R.J.8    Mariuzza, R.A.9
  • 12
    • 85044100900 scopus 로고    scopus 로고
    • Production of Antipeptide Antisera
    • G.P. Crooks, ed., John Wiley & Sons, Inc.
    • J.E. Coligan, J.P. Tam and J. Shao, Production of Antipeptide Antisera, in: Current Protocols in Neuroscience, G.P. Crooks, ed., John Wiley & Sons, Inc., 1997, pp. 5.6.1-5.6.21.
    • Current Protocols in Neuroscience , vol.1997 , pp. 561-5621
    • Coligan, J.E.1    Tam, J.P.2    Shao, J.3
  • 14
    • 0028475962 scopus 로고
    • Predicting antigenic determinants in proteins: Looking for unidimensional solutions to a three-dimensional problem?
    • M.H. Van Regenmortel and J.L. Pellequer, Predicting antigenic determinants in proteins: looking for unidimensional solutions to a three-dimensional problem? Pept Res 7 (1994), 224-228.
    • (1994) Pept Res , vol.7 , pp. 224-228
    • Van Regenmortel, M.H.1    Pellequer, J.L.2
  • 15
    • 0022993892 scopus 로고
    • Antibody response to the C-terminal peptide sequence in beef myoglobin
    • H.M. Cooper, P.E. Todd and S.J. Leach, Antibody response to the C-terminal peptide sequence in beef myoglobin, Mol Immunol 23 (1986), 1289-1299.
    • (1986) Mol Immunol , vol.23 , pp. 1289-1299
    • Cooper, H.M.1    Todd, P.E.2    Leach, S.J.3
  • 17
    • 0023903983 scopus 로고
    • Synthetic peptides of Shiga toxin B subunit induce antibodies which neutralize its biological activity
    • I. Harari, A. Donohue-Rolfe, G. Keusch and R. Arnon, Synthetic peptides of Shiga toxin B subunit induce antibodies which neutralize its biological activity, Infect Immun 56 (1988), 1618-1624.
    • (1988) Infect Immun , vol.56 , pp. 1618-1624
    • Harari, I.1    Donohue-Rolfe, A.2    Keusch, G.3    Arnon, R.4
  • 18
    • 0025138489 scopus 로고
    • Protective immunogenicity of two synthetic peptides selected from the amino acid sequence of Bordetella pertussis toxin subunit S1
    • P. Askelof, K. Rodmalm, G. Wrangsell, U. Larsson, S.B. Svenson, J.L. Cowell, A. Unden and T. Bartfai, Protective immunogenicity of two synthetic peptides selected from the amino acid sequence of Bordetella pertussis toxin subunit S1, Proc Natl Acad Sci USA 87 (1990), 1347-1351.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 1347-1351
    • Askelof, P.1    Rodmalm, K.2    Wrangsell, G.3    Larsson, U.4    Svenson, S.B.5    Cowell, J.L.6    Unden, A.7    Bartfai, T.8
  • 20
    • 84907107560 scopus 로고
    • Antibodies to sperm-whale myoglobin evoked by free synthetic peptides of an antigenic site
    • C.R. Young and M.Z. Atassi, Antibodies to sperm-whale myoglobin evoked by free synthetic peptides of an antigenic site, Immunological Communications 11 (1982), 9-16.
    • (1982) Immunological Communications , vol.11 , pp. 9-16
    • Young, C.R.1    Atassi, M.Z.2
  • 22
    • 84941410360 scopus 로고
    • Cross reactions of antiserums against heterologous terminal amino acid sequences and two strains of the tobacco mosaic virus
    • F.A. Anderer and H.D. Schlumberger, [Cross reactions of antiserums against heterologous terminal amino acid sequences and two strains of the tobacco mosaic virus], Z Naturforsch B20 (1965), 564-568.
    • (1965) Z Naturforsch , vol.B20 , pp. 564-568
    • Anderer, F.A.1    Schlumberger, H.D.2
  • 23
    • 0014027005 scopus 로고
    • Cross-reactions of anti-sera against the terminal amino acid and dipeptide of tobacco mosaic virus
    • F.A. Anderer and H.D. Schlumberger, Cross-reactions of anti-sera against the terminal amino acid and dipeptide of tobacco mosaic virus, Biochim Biophys Acta 115 (1966), 222-224.
    • (1966) Biochim Biophys Acta , vol.115 , pp. 222-224
    • Anderer, F.A.1    Schlumberger, H.D.2
  • 26
    • 84907106959 scopus 로고
    • A novel approach for localization of the continuous protein antigenic sites by comprehensive synthetic surface scanning: Antibody and T-cell activity to several influenza hemagglutinin synthetic sites
    • M.Z. Atassi and J. Kurisaki, A novel approach for localization of the continuous protein antigenic sites by comprehensive synthetic surface scanning: antibody and T-cell activity to several influenza hemagglutinin synthetic sites, Immunol Commun 13 (1984), 539-551.
    • (1984) Immunol Commun , vol.13 , pp. 539-551
    • Atassi, M.Z.1    Kurisaki, J.2
  • 27
    • 0023026563 scopus 로고
    • Reactivity of anti-peptide and anti-poliovirus type 3 monoclonal antibodies with synthetic peptides
    • M. Ferguson, S.E. Reed and P.D. Minor, Reactivity of anti-peptide and anti-poliovirus type 3 monoclonal antibodies with synthetic peptides, J Gen Virol 67(11) (1986), 2527-2531.
    • (1986) J Gen Virol , vol.67 , Issue.11 , pp. 2527-2531
    • Ferguson, M.1    Reed, S.E.2    Minor, P.D.3
  • 28
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • J. Kyte and R.F. Doolittle, A simple method for displaying the hydropathic character of a protein, J Mol Biol 157 (1982), 105-132.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 29
    • 0021918946 scopus 로고
    • Prediction of chain flexibility in proteins: A tool for the selection of peptide antigens
    • P. Karplus and G. Shulz, Prediction of chain flexibility in proteins: a tool for the selection of peptide antigens, Naturwissenschaften 72 (1985), 212-213.
    • (1985) Naturwissenschaften , vol.72 , pp. 212-213
    • Karplus, P.1    Shulz, G.2
  • 31
    • 0022249654 scopus 로고
    • Induction of hepatitis A virus-neutralizing antibody by a virus-specific synthetic peptide
    • E.A. Emini, J.V. Hughes, D.S. Perlow and J. Boger, Induction of hepatitis A virus-neutralizing antibody by a virus-specific synthetic peptide, Journal of Virology 55 (1985), 836-839.
    • (1985) Journal of Virology , vol.55 , pp. 836-839
    • Emini, E.A.1    Hughes, J.V.2    Perlow, D.S.3    Boger, J.4
  • 32
    • 0023984742 scopus 로고
    • The antigenic index: A novel algorithm for predicting antigenic determinants
    • B.A. Jameson and H. Wolf, The antigenic index: a novel algorithm for predicting antigenic determinants, Comput Appl Biosci 4 (1988), 181-186.
    • (1988) Comput Appl Biosci , vol.4 , pp. 181-186
    • Jameson, B.A.1    Wolf, H.2
  • 33
    • 0032751746 scopus 로고    scopus 로고
    • Predicting protein three-dimensional structure
    • J. Moult, Predicting protein three-dimensional structure, Curr Opin Biotechnol 10 (1999), 583-588.
    • (1999) Curr Opin Biotechnol , vol.10 , pp. 583-588
    • Moult, J.1
  • 34
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein structure by profile-based neural networks
    • B. Rost, PHD: predicting one-dimensional protein structure by profile-based neural networks, Methods Enzymol 266 (1996), 525-539.
    • (1996) Methods Enzymol , vol.266 , pp. 525-539
    • Rost, B.1
  • 37
    • 0032993160 scopus 로고    scopus 로고
    • Single-chain variable fragments selected on the 57-76 p21Ras neutralising epitope from phage antibody libraries recognise the native protein
    • L. Persic, I.R. Horn, S. Rybak, A. Cattaneo, H.R. Hoogenboom and A. Bradbury, Single-chain variable fragments selected on the 57-76 p21Ras neutralising epitope from phage antibody libraries recognise the native protein, FEBS lett 443 (1999), 112-116.
    • (1999) FEBS Lett , vol.443 , pp. 112-116
    • Persic, L.1    Horn, I.R.2    Rybak, S.3    Cattaneo, A.4    Hoogenboom, H.R.5    Bradbury, A.6
  • 38
    • 0034665746 scopus 로고    scopus 로고
    • Mass spectral analysis of a protein complex using single-chain antibodies selected on a peptide target: Applications to functional genomics
    • R.W. Siegel, B. Allen, P. Pavlik, J.D. Marks and A. Bradbury, Mass spectral analysis of a protein complex using single-chain antibodies selected on a peptide target: applications to functional genomics, J Mol Biol 302 (2000), 285-293.
    • (2000) J Mol Biol , vol.302 , pp. 285-293
    • Siegel, R.W.1    Allen, B.2    Pavlik, P.3    Marks, J.D.4    Bradbury, A.5
  • 39
    • 0026650531 scopus 로고
    • A transcriptionally active DNA-binding site for human p53 protein complexes
    • W.D. Funk, D.T. Pak, R.H. Karas, W.E. Wright and J.W. Shay, A transcriptionally active DNA-binding site for human p53 protein complexes, Mol Cell Biol 12 (1992), 2866-2871.
    • (1992) Mol Cell Biol , vol.12 , pp. 2866-2871
    • Funk, W.D.1    Pak, D.T.2    Karas, R.H.3    Wright, W.E.4    Shay, J.W.5
  • 40
    • 0030867582 scopus 로고    scopus 로고
    • Conservation of the Chk1 checkpoint pathway in mammals: Linkage of DNA damage to Cdk regulation through Cdc25
    • Y. Sanchez, C. Wong, R.S. Thoma, R. Richman, Z. Wu, H. Piwnica-Worms and S.J. Elledge, Conservation of the Chk1 checkpoint pathway in mammals: linkage of DNA damage to Cdk regulation through Cdc25, Science 277 (1997), 1497-1501.
    • (1997) Science , vol.277 , pp. 1497-1501
    • Sanchez, Y.1    Wong, C.2    Thoma, R.S.3    Richman, R.4    Wu, Z.5    Piwnica-Worms, H.6    Elledge, S.J.7
  • 42
    • 0033939894 scopus 로고    scopus 로고
    • Assays for transglutaminases in cell death
    • G. Melino, E. Candi and P.M. Steinert, Assays for transglutaminases in cell death, Methods Enzymol 322 (2000), 433-472.
    • (2000) Methods Enzymol , vol.322 , pp. 433-472
    • Melino, G.1    Candi, E.2    Steinert, P.M.3
  • 45
    • 0037022619 scopus 로고    scopus 로고
    • Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity
    • S. Liu, R.A. Cerione and J. Clardy, Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity, Proc Natl Acad Sci USA 99 (2002), 2743-2747.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2743-2747
    • Liu, S.1    Cerione, R.A.2    Clardy, J.3
  • 47
    • 0017868338 scopus 로고
    • Empirical predictions of protein conformation
    • P.Y. Chou and G.D. Fasman, Empirical predictions of protein conformation, Annual Review of Biochemistry 47 (1978), 251-276.
    • (1978) Annual Review of Biochemistry , vol.47 , pp. 251-276
    • Chou, P.Y.1    Fasman, G.D.2
  • 48
    • 0028109886 scopus 로고
    • Conservation and prediction of solvent accessibility in protein families
    • B. Rost and C. Sander, Conservation and prediction of solvent accessibility in protein families, Proteins 20 (1994), 216-226.
    • (1994) Proteins , vol.20 , pp. 216-226
    • Rost, B.1    Sander, C.2
  • 49
    • 0026769713 scopus 로고
    • An immunochemical analysis of the human nuclear phosphoprotein p53. New monoclonal antibodies and epitope mapping using recombinant p53
    • B. Vojtesek, J. Bartek, C.A. Midgley and D.P. Lane, An immunochemical analysis of the human nuclear phosphoprotein p53. New monoclonal antibodies and epitope mapping using recombinant p53, J Immunol Methods 151 (1992), 237-244.
    • (1992) J Immunol Methods , vol.151 , pp. 237-244
    • Vojtesek, B.1    Bartek, J.2    Midgley, C.A.3    Lane, D.P.4
  • 51
    • 0035866390 scopus 로고    scopus 로고
    • The ZNF217 gene amplified in breast cancers promotes immortalization of human mammary epithelial cells
    • G.H. Nonet, M.R. Stampfer, K. Chin, J.W. Gray, C.C. Collins and P. Yaswen, The ZNF217 gene amplified in breast cancers promotes immortalization of human mammary epithelial cells, Cancer Res 61 (2001), 1250-1254.
    • (2001) Cancer Res , vol.61 , pp. 1250-1254
    • Nonet, G.H.1    Stampfer, M.R.2    Chin, K.3    Gray, J.W.4    Collins, C.C.5    Yaswen, P.6
  • 53
    • 0034425742 scopus 로고    scopus 로고
    • Antibody arrays for high-throughput screening of antibody-antigen interactions
    • R.M. de Wildt, C.R. Mundy, B.D. Gorick and I.M. Tomlinson, Antibody arrays for high-throughput screening of antibody-antigen interactions, Nat Biotechnol 18 (2000), 989-994.
    • (2000) Nat Biotechnol , vol.18 , pp. 989-994
    • De Wildt, R.M.1    Mundy, C.R.2    Gorick, B.D.3    Tomlinson, I.M.4
  • 55
    • 0037056219 scopus 로고    scopus 로고
    • Target validation for genomics using peptide-specific phage antibodies: A study of five gene products overexpressed in colorectal cancer. PG
    • J.R. Van Beijnum, P.T. Moerkerk, A.J. Gerbers, A.P. De Bruine, J.W. Arends, H.R. Hoogenboom and S.E. Hufton, Target validation for genomics using peptide-specific phage antibodies: a study of five gene products overexpressed in colorectal cancer. PG, Int J Cancer 101 (2002), 118-127.
    • (2002) Int J Cancer , vol.101 , pp. 118-127
    • Van Beijnum, J.R.1    Moerkerk, P.T.2    Gerbers, A.J.3    De Bruine, A.P.4    Arends, J.W.5    Hoogenboom, H.R.6    Hufton, S.E.7
  • 56
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • N. Guex and M. Peitsch, SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling, Electrophoresis 18 (1997), 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.