메뉴 건너뛰기




Volumn 10, Issue 11, 2004, Pages 648-658

Cyclic peptides selected by phage display mimic the natural epitope recognized by a monoclonal anti-colicin A antibody

Author keywords

Decapeptide library; Disulfide linked peptide; Epitope mapping; Phage display

Indexed keywords

COLICIN A; CYCLOPEPTIDE; EPITOPE; MONOCLONAL ANTIBODY; PEPTIDE LIBRARY;

EID: 8644263987     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/psc.574     Document Type: Article
Times cited : (4)

References (39)
  • 1
    • 0022519337 scopus 로고
    • Three-dimensional structure of an antigen-antibody complex at 2.8Å resolution
    • Amit AG, Mariuzza RA, Phillips SE, Poljak RJ. Three-dimensional structure of an antigen-antibody complex at 2.8Å resolution. Science 1986; 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
    • 0026488690 scopus 로고
    • Structural basis of antigenic specificity and design of new vaccines
    • Arnon R, Van Regenmortel MH. Structural basis of antigenic specificity and design of new vaccines. FASEB J. 1992; 6: 3265-3274.
    • (1992) FASEB J. , vol.6 , pp. 3265-3274
    • Arnon, R.1    Van Regenmortel, M.H.2
  • 5
    • 0022033631 scopus 로고
    • Precise epitope mapping of the murine transformation-associated protein, p53
    • Wade-Evans A, Jenkins JR. Precise epitope mapping of the murine transformation-associated protein, p53. EMBO J. 1985; 4 699-706.
    • (1985) EMBO J. , vol.4 , pp. 699-706
    • Wade-Evans, A.1    Jenkins, J.R.2
  • 6
    • 0026769713 scopus 로고
    • An immunochemical analysis of the human nuclear phosphoprotein p53. New monoclonal antibodies and epitope mapping using recombinant p53
    • Vojtesek B, Bartek J, Midgley CA, Lane DP. An immunochemical analysis of the human nuclear phosphoprotein p53. New monoclonal antibodies and epitope mapping using recombinant p53. J. Immunol. Methods 1992; 151: 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
  • 7
    • 0025112794 scopus 로고
    • Searching for peptide ligands with an epitope library
    • Scott JK, Smith GP. Searching for peptide ligands with an epitope library. Science 1990; 249: 386-390.
    • (1990) Science , vol.249 , pp. 386-390
    • Scott, J.K.1    Smith, G.P.2
  • 8
    • 0028592703 scopus 로고
    • An in vitro polysome display system for identifying ligands from very large peptide libraries
    • Mattheakis LC, Bhatt RR, Dower WJ. An in vitro polysome display system for identifying ligands from very large peptide libraries. Proc. Natl Acad. Sci. USA 1994; 91: 9022-9026.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 9022-9026
    • Mattheakis, L.C.1    Bhatt, R.R.2    Dower, W.J.3
  • 9
    • 0030974119 scopus 로고    scopus 로고
    • In vitro selection and evolution of functional proteins by using ribosome display
    • Hanes J, Plückthun A. In vitro selection and evolution of functional proteins by using ribosome display. Proc. Natl Acad. Sci. USA 1997; 94: 4937-4942.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 4937-4942
    • Hanes, J.1    Plückthun, A.2
  • 11
    • 0026411004 scopus 로고
    • Selection of antibody ligands from a large library of oligopeptides expressed on a multivalent exposition vector
    • Felici F, Castagnoli L, Musacchio A, Jappelli R, Cesareni G. Selection of antibody ligands from a large library of oligopeptides expressed on a multivalent exposition vector. J. Mol. Biol. 1991; 222: 301-310.
    • (1991) J. Mol. Biol. , vol.222 , pp. 301-310
    • Felici, F.1    Castagnoli, L.2    Musacchio, A.3    Jappelli, R.4    Cesareni, G.5
  • 12
    • 0028915250 scopus 로고
    • Characterisation of epitopes on human p53 using phage-displayed peptide libraries: Insights into antibody-peptide interactions
    • Stephen CW, Helminen P, Lane DP. Characterisation of epitopes on human p53 using phage-displayed peptide libraries: insights into antibody-peptide interactions. J. Mol. Biol. 1995; 248: 58-78.
    • (1995) J. Mol. Biol. , vol.248 , pp. 58-78
    • Stephen, C.W.1    Helminen, P.2    Lane, D.P.3
  • 13
    • 0035183986 scopus 로고    scopus 로고
    • Rapid and precise epitope mapping of monoclonal antibodies against Plasmodium falciparum AMA1 by combined phage display of fragments and random peptides
    • Coley AM, Campanale NV, Casey JL, Hodder AN, Crewther PE, Anders RF, Tilley LM, Foley M. Rapid and precise epitope mapping of monoclonal antibodies against Plasmodium falciparum AMA1 by combined phage display of fragments and random peptides. Protein Eng 2001; 14: 691-698.
    • (2001) Protein Eng. , vol.14 , pp. 691-698
    • Coley, A.M.1    Campanale, N.V.2    Casey, J.L.3    Hodder, A.N.4    Crewther, P.E.5    Anders, R.F.6    Tilley, L.M.7    Foley, M.8
  • 14
    • 0036970470 scopus 로고    scopus 로고
    • Quantifying beta-sheet stability by phage display
    • Distefano MD, Zhong A, Cochran AG. Quantifying beta-sheet stability by phage display. J. Mol. Biol. 2002; 322: 179-188.
    • (2002) J. Mol. Biol. , vol.322 , pp. 179-188
    • Distefano, M.D.1    Zhong, A.2    Cochran, A.G.3
  • 16
    • 0034930363 scopus 로고    scopus 로고
    • A rapid, generally applicable method to engineer zinc fingers illustrated by targeting the HIV-1 promoter
    • Isalan M, Klug A, Choo Y. A rapid, generally applicable method to engineer zinc fingers illustrated by targeting the HIV-1 promoter. Nat. Biotechnol. 2001; 19: 656-660.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 656-660
    • Isalan, M.1    Klug, A.2    Choo, Y.3
  • 17
    • 0036828234 scopus 로고    scopus 로고
    • Identification of a peptide antagonist to the peripheral-type benzodiazepine receptor that inhibits hormone-stimulated leydig cell steroid formation
    • Gazouli M, Han Z, Papadopoulos V. Identification of a peptide antagonist to the peripheral-type benzodiazepine receptor that inhibits hormone-stimulated leydig cell steroid formation. J. Pharmacol. Exp. Ther. 2002; 303: 627-632.
    • (2002) J. Pharmacol. Exp. Ther. , vol.303 , pp. 627-632
    • Gazouli, M.1    Han, Z.2    Papadopoulos, V.3
  • 19
    • 0036323958 scopus 로고    scopus 로고
    • Identification and characterization of peptides that bind human ErbB-2 selected from a bacteriophage display library
    • Karasseva NG, Glinsky VV, Chen NX, Komatireddy R, Quinn TP. Identification and characterization of peptides that bind human ErbB-2 selected from a bacteriophage display library. J. Protein Chem. 2002; 21: 287-296.
    • (2002) J. Protein Chem. , vol.21 , pp. 287-296
    • Karasseva, N.G.1    Glinsky, V.V.2    Chen, N.X.3    Komatireddy, R.4    Quinn, T.P.5
  • 22
    • 0027247924 scopus 로고
    • Biotin binders selected from a random peptide library expressed on phage
    • Saggio I, Laufer R. Biotin binders selected from a random peptide library expressed on phage. Biochem. J. 1993; 293: 613-616.
    • (1993) Biochem. J. , vol.293 , pp. 613-616
    • Saggio, I.1    Laufer, R.2
  • 23
    • 0027253452 scopus 로고
    • M 13 bacteriophage displaying disulfide-constrained microproteins
    • McLafferty MA, Kent RB, Ladner RC, Markland W. M 13 bacteriophage displaying disulfide-constrained microproteins. Gene 1993; 128: 29-36.
    • (1993) Gene , vol.128 , pp. 29-36
    • McLafferty, M.A.1    Kent, R.B.2    Ladner, R.C.3    Markland, W.4
  • 24
    • 0035811031 scopus 로고    scopus 로고
    • A beta -hairpin structure in a 13-mer peptide that binds alpha -bungarotoxin with high affinity and neutralizes its toxicity
    • Scherf T, Kasher R, Balass M, Fridkin M, Fuchs S, Katchalski-Katzir E. A beta -hairpin structure in a 13-mer peptide that binds alpha -bungarotoxin with high affinity and neutralizes its toxicity. Proc. Natl Acad. Sci. USA 2001; 98: 6629-6634.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 6629-6634
    • Scherf, T.1    Kasher, R.2    Balass, M.3    Fridkin, M.4    Fuchs, S.5    Katchalski-Katzir, E.6
  • 26
    • 0034492786 scopus 로고    scopus 로고
    • Isolation of peptide ligands that inhibit glutamate racemase activity from a random phage display library
    • Kim WC, Rhee HI, Park BK, Suk KH, Cha SH. Isolation of peptide ligands that inhibit glutamate racemase activity from a random phage display library. J. Biomol. Screen 2000; 5: 435-440.
    • (2000) J. Biomol. Screen , vol.5 , pp. 435-440
    • Kim, W.C.1    Rhee, H.I.2    Park, B.K.3    Suk, K.H.4    Cha, S.H.5
  • 27
    • 0027316004 scopus 로고
    • Substrate phage: Selection of protease substrates by monovalent phage display
    • Matthews DJ, Wells JA. Substrate phage: selection of protease substrates by monovalent phage display. Science 1993; 260: 1113-1117.
    • (1993) Science , vol.260 , pp. 1113-1117
    • Matthews, D.J.1    Wells, J.A.2
  • 30
    • 0022512078 scopus 로고
    • A molecular, genetic and immunological approach to the functioning of colicin A, a pore-forming protein
    • Cavard D, Crozel V, Gorvel JP, Pattus F, Baty D, Lazdunski C. A molecular, genetic and immunological approach to the functioning of colicin A, a pore-forming protein. J. Mol. Biol. 1986; 187: 449-459.
    • (1986) J. Mol. Biol. , vol.187 , pp. 449-459
    • Cavard, D.1    Crozel, V.2    Gorvel, J.P.3    Pattus, F.4    Baty, D.5    Lazdunski, C.6
  • 31
    • 0031936581 scopus 로고    scopus 로고
    • Intracellular immunization of prokaryotic cells against a bacteriotoxin
    • Chames P, Fieschi J, Baty D, Duché D. Intracellular immunization of prokaryotic cells against a bacteriotoxin. J. Bacteriol. 1998; 180: 514-518.
    • (1998) J. Bacteriol. , vol.180 , pp. 514-518
    • Chames, P.1    Fieschi, J.2    Baty, D.3    Duché, D.4
  • 33
    • 0027281133 scopus 로고
    • Recognition of the colicin A N-terminal epitope 1C 11 in vitro and in vivo in Escherichia coli by its cognate monoclonal antibody
    • Géli V, Lloubès R, Zaat SA, van Spaendonk RM, Rollin C, Bénédetti H, Lazdunski C. Recognition of the colicin A N terminal epitope 1C 11 in vitro and in vivo in Escherichia coli by its cognate monoclonal antibody. FEMS Microbiol. Lett. 1993; 109: 335-342.
    • (1993) FEMS Microbiol. Lett. , vol.109 , pp. 335-342
    • Géli, V.1    Lloubès, R.2    Zaat, S.A.3    van Spaendonk, R.M.4    Rollin, C.5    Bénédetti, H.6    Lazdunski, C.7
  • 34
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press. Cold Spring Harbor: New York
    • Harlow E, Lane DP. Antibodies: A Laboratory Manual. Cold Spring Harbor Laboratory Press. Cold Spring Harbor: New York, 1988.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.P.2
  • 35
    • 0027266779 scopus 로고
    • Libraries of peptides and proteins displayed on filamentous phage
    • Smith GP, Scott JK. Libraries of peptides and proteins displayed on filamentous phage. Methods Enzymol. 1993; 217: 228-257.
    • (1993) Methods Enzymol. , vol.217 , pp. 228-257
    • Smith, G.P.1    Scott, J.K.2
  • 36
    • 0030576498 scopus 로고    scopus 로고
    • Peptide libraries define the fine specificity of anti-polysaccharide antibodies to Cryptococcus neoformans
    • Valadon P, Nussbaum G, Boyd LF, Margulies DH, Scharff MD. Peptide libraries define the fine specificity of anti-polysaccharide antibodies to Cryptococcus neoformans. J. Mol. Biol. 1996; 261 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
  • 37
    • 0027632992 scopus 로고
    • Development of a fully automated multichannel peptide synthesizer with integrated TFA cleavage capability
    • Neimark J, Briand JP. Development of a fully automated multichannel peptide synthesizer with integrated TFA cleavage capability. Pept. Res. 1993; 6: 219-228.
    • (1993) Pept. Res. , vol.6 , pp. 219-228
    • Neimark, J.1    Briand, J.P.2
  • 38
    • 0025103048 scopus 로고
    • A cleavage method which minimizes side reactions following Fmoc solid phase peptide synthesis
    • King DS, Fields CG, Fields GB. A cleavage method which minimizes side reactions following Fmoc solid phase peptide synthesis. Int. J. Pept. Protein Res. 1990; 36: 255-266.
    • (1990) Int. J. Pept. Protein Res. , vol.36 , pp. 255-266
    • King, D.S.1    Fields, C.G.2    Fields, G.B.3
  • 39


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.