메뉴 건너뛰기




Volumn 231, Issue 1-2, 1999, Pages 93-104

Selectively infective phage (SIP) technology: Scope and limitations

Author keywords

Affinity maturation; Disulfide bonds; Phage display; ScFv fragments

Indexed keywords

ARTICLE; BINDING AFFINITY; DISULFIDE BOND; LIGAND BINDING; PHAGE DISPLAY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY;

EID: 0033499651     PISSN: 00221759     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-1759(99)00143-X     Document Type: Article
Times cited : (36)

References (38)
  • 1
    • 0019841225 scopus 로고
    • Domain structure of bacteriophage fd adsorption protein
    • Armstrong, J., Perham, R.N., Walker, J.E., 1981. Domain structure of bacteriophage fd adsorption protein. FEBS Lett. 135, 167.
    • (1981) FEBS Lett , vol.135 , pp. 167
    • Armstrong, J.1    Perham, R.N.2    Walker, J.E.3
  • 4
    • 0030801376 scopus 로고    scopus 로고
    • Filamentous phage infection: Required interactions with the TolA protein
    • Click, E.M., Webster, R.E., 1997. Filamentous phage infection: required interactions with the TolA protein. J. Bacteriol. 179, 6464.
    • (1997) J. Bacteriol. , vol.179 , pp. 6464
    • Click, E.M.1    Webster, R.E.2
  • 5
    • 0031894126 scopus 로고    scopus 로고
    • The TolQRA proteins are required for membrane insertion of the major capsid protein of the filamentous phage f1 during infection
    • Click, E.M., Webster, R.E., 1998. The TolQRA proteins are required for membrane insertion of the major capsid protein of the filamentous phage f1 during infection. J. Bacteriol. 180, 1723.
    • (1998) J. Bacteriol. , vol.180 , pp. 1723
    • Click, E.M.1    Webster, R.E.2
  • 6
    • 0021352584 scopus 로고
    • Gene-III protein of filamentous phages: Evidence for a carboxyl-terminal domain with a role in morphogenesis
    • Crissman, J.W., Smith, G.P., 1984. Gene-III protein of filamentous phages: evidence for a carboxyl-terminal domain with a role in morphogenesis. Virology 132, 445.
    • (1984) Virology , vol.132 , pp. 445
    • Crissman, J.W.1    Smith, G.P.2
  • 7
    • 0033585380 scopus 로고    scopus 로고
    • Interaction of the globular domains of pIII protein of filamentous bacteriophage fd with the F-pilus of Escherichia coli
    • Deng, L.W., Malik, P., Perham, R.N., 1999. Interaction of the globular domains of pIII protein of filamentous bacteriophage fd with the F-pilus of Escherichia coli. Virology 253, 271.
    • (1999) Virology , vol.253 , pp. 271
    • Deng, L.W.1    Malik, P.2    Perham, R.N.3
  • 8
    • 0028136310 scopus 로고
    • Multimerization behaviour of single chain Fv variants for the tumour-binding antibody B72.3
    • Desplancq, D., King, D.J., Lawson, A.D., Mountain, A., 1994. Multimerization behaviour of single chain Fv variants for the tumour-binding antibody B72.3. Protein Eng. 7, 1027.
    • (1994) Protein Eng , vol.7 , pp. 1027
    • Desplancq, D.1    King, D.J.2    Lawson, A.D.3    Mountain, A.4
  • 9
    • 0027933750 scopus 로고
    • Clonal selection and amplification of phage displayed antibodies by linking antigen recognition and phage replication
    • Dueñas, M., Borrebaeck, C.A., 1994. Clonal selection and amplification of phage displayed antibodies by linking antigen recognition and phage replication. Biotechnology 12, 999.
    • (1994) Biotechnology , vol.12 , pp. 999
    • Dueñas, M.1    Borrebaeck, C.A.2
  • 11
    • 0019920698 scopus 로고
    • Interference resistant mutants of phage f1
    • Enea, V., Zinder, N.D., 1982. Interference resistant mutants of phage f1. Virology 122, 222.
    • (1982) Virology , vol.122 , pp. 222
    • Enea, V.1    Zinder, N.D.2
  • 13
    • 0028670306 scopus 로고
    • Direct interaction rescue, a novel filamentous phage technique to study protein-protein interactions
    • Gramatikoff, K., Georgiev, O., Schaffner, W., 1994. Direct interaction rescue, a novel filamentous phage technique to study protein-protein interactions. Nucleic Acids Res. 22, 5761.
    • (1994) Nucleic Acids Res , vol.22 , pp. 5761
    • Gramatikoff, K.1    Georgiev, O.2    Schaffner, W.3
  • 14
    • 0029294706 scopus 로고
    • The leucine zipper of c-Jun binds to ribosomal protein L18a: A role in Jun protein regulation?
    • Gramatikoff, K., Schaffner, W., Georgiev, O., 1995. The leucine zipper of c-Jun binds to ribosomal protein L18a: a role in Jun protein regulation? Biol. Chem. 376, 321.
    • (1995) Biol. Chem , vol.376 , pp. 321
    • Gramatikoff, K.1    Schaffner, W.2    Georgiev, O.3
  • 15
    • 0031813249 scopus 로고    scopus 로고
    • Non-repetitive single-chain Fv linkers selected by selectively infective phage (SIP) technology
    • Hennecke, F., Krebber, C., Plückthun, A., 1998. Non-repetitive single-chain Fv linkers selected by selectively infective phage (SIP) technology. Protein Eng. 11, 405.
    • (1998) Protein Eng , vol.11 , pp. 405
    • Hennecke, F.1    Krebber, C.2    Plückthun, A.3
  • 16
    • 0031568809 scopus 로고    scopus 로고
    • A conserved infection pathway for filamentous bacteriophages is suggested by the structure of the membrane penetration domain of the minor coat protein g3p from phage fd
    • Holliger, P., Riechmann, L., 1997. A conserved infection pathway for filamentous bacteriophages is suggested by the structure of the membrane penetration domain of the minor coat protein g3p from phage fd. Structure 5, 265.
    • (1997) Structure , vol.5 , pp. 265
    • Holliger, P.1    Riechmann, L.2
  • 17
    • 0033010511 scopus 로고    scopus 로고
    • Crystal structure of the two N-terminal domains of g3p from filamentous phage fd at 1.9 Å: Evidence for conformational lability
    • in press
    • Holliger, P., Riechmann, L., Williams, R.L., 1999. Crystal structure of the two N-terminal domains of g3p from filamentous phage fd at 1.9 Å: evidence for conformational lability. J. Mol. Biol., in press.
    • (1999) J. Mol. Biol.
    • Holliger, P.1    Riechmann, L.2    Williams, R.L.3
  • 18
    • 0031915294 scopus 로고    scopus 로고
    • Gene VIII-based, phage-display vectors for selection against complex mixtures of ligands
    • Jacobsson, K., Frykberg, L., 1998. Gene VIII-based, phage-display vectors for selection against complex mixtures of ligands. Biotechniques 24, 294.
    • (1998) Biotechniques , vol.24 , pp. 294
    • Jacobsson, K.1    Frykberg, L.2
  • 19
    • 0023697146 scopus 로고
    • A hybrid toxin from bacteriophage f1 attachment protein and colicin E3 has altered cell receptor specificity
    • Jakes, K.S., Davis, N.G., Zinder, N.D., 1988. A hybrid toxin from bacteriophage f1 attachment protein and colicin E3 has altered cell receptor specificity. J. Bacteriol. 170, 4231.
    • (1988) J. Bacteriol. , vol.170 , pp. 4231
    • Jakes, K.S.1    Davis, N.G.2    Zinder, N.D.3
  • 20
    • 0029585566 scopus 로고
    • Co-selection of cognate antibody-antigen pairs by selectively infective phages
    • Krebber, C., Spada, S., Desplancq, D., Plückthun, A., 1995. Co-selection of cognate antibody-antigen pairs by selectively infective phages. FEBS Lett. 377, 227.
    • (1995) FEBS Lett , vol.377 , pp. 227
    • Krebber, C.1    Spada, S.2    Desplancq, D.3    Plückthun, A.4
  • 21
    • 0031560775 scopus 로고    scopus 로고
    • Selectively infective phage (SIP): A mechanistic dissection of a novel in vivo selection for protein-ligand interactions
    • Krebber, C., Spada, S., Desplancq, D., Krebber, A., Ge, L., Plückthun, A., 1997. Selectively infective phage (SIP): a mechanistic dissection of a novel in vivo selection for protein-ligand interactions. J. Mol. Biol. 268, 607.
    • (1997) J. Mol. Biol. , vol.268 , pp. 607
    • Krebber, C.1    Spada, S.2    Desplancq, D.3    Krebber, A.4    Ge, L.5    Plückthun, A.6
  • 22
    • 0031759422 scopus 로고    scopus 로고
    • Proteolytic selection for protein folding using filamentous bacteriophages
    • Kristensen, P., Winter, G., 1998. Proteolytic selection for protein folding using filamentous bacteriophages. Folding Des. 3, 321.
    • (1998) Folding Des , vol.3 , pp. 321
    • Kristensen, P.1    Winter, G.2
  • 23
    • 0031911439 scopus 로고    scopus 로고
    • The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3p
    • Lubkowski, J., Hennecke, F., Plückthun, A., Wlodawer, A., 1998. The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3p. Nat. Struct. Biol. 5, 140.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 140
    • Lubkowski, J.1    Hennecke, F.2    Plückthun, A.3    Wlodawer, A.4
  • 24
    • 0000046526 scopus 로고    scopus 로고
    • Filamentous phage infection: Crystal structure of g3p in complex with its coreceptor, the C-terminal domain of TolA
    • Lubkowski, J., Hennecke, F., Plückthun, A., Wlodawer, A., 1999. Filamentous phage infection: crystal structure of g3p in complex with its coreceptor, the C-terminal domain of TolA. Structure 7, 711.
    • (1999) Structure , vol.7 , pp. 711
    • Lubkowski, J.1    Hennecke, F.2    Plückthun, A.3    Wlodawer, A.4
  • 25
    • 0032054113 scopus 로고    scopus 로고
    • Filamentous phage structure, infection and assembly
    • Marvin, D.A., 1998. Filamentous phage structure, infection and assembly. Curr. Opin. Struct. Biol. 8, 150-158.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 150-158
    • Marvin, D.A.1
  • 26
    • 0019351126 scopus 로고
    • Filamentous phage DNA cloning vectors: A noninfective mutant with a nonpolar deletion in gene III
    • Nelson, F.K., Friedman, S.M., Smith, G.P., 1981. Filamentous phage DNA cloning vectors: a noninfective mutant with a nonpolar deletion in gene III. Virology 108, 338.
    • (1981) Virology , vol.108 , pp. 338
    • Nelson, F.K.1    Friedman, S.M.2    Smith, G.P.3
  • 27
    • 0030869953 scopus 로고    scopus 로고
    • Affinity and folding properties both influence the selection of antibodies with the selectively infective phage (SIP) methodology
    • Pedrazzi, G., Schwesinger, F., Honegger, A., Krebber, C., Plückthun, A., 1997. Affinity and folding properties both influence the selection of antibodies with the selectively infective phage (SIP) methodology. FEBS Lett. 415, 289.
    • (1997) FEBS Lett , vol.415 , pp. 289
    • Pedrazzi, G.1    Schwesinger, F.2    Honegger, A.3    Krebber, C.4    Plückthun, A.5
  • 28
    • 0030797114 scopus 로고    scopus 로고
    • The C-terminal domain of TolA is the coreceptor for filamentous phage infection of E. coli
    • Riechmann, L., Holliger, P., 1997. The C-terminal domain of TolA is the coreceptor for filamentous phage infection of E. coli. Cell 90, 351.
    • (1997) Cell , vol.90 , pp. 351
    • Riechmann, L.1    Holliger, P.2
  • 29
    • 0026587998 scopus 로고
    • Structural evidence for induced fit as a mechanism for antibody-antigen recognition
    • Rini, J.M., Schulze-Gahmen, U., Wilson, I.A., 1992. Structural evidence for induced fit as a mechanism for antibody-antigen recognition. Science 255, 959.
    • (1992) Science , vol.255 , pp. 959
    • Rini, J.M.1    Schulze-Gahmen, U.2    Wilson, I.A.3
  • 30
    • 0032573599 scopus 로고    scopus 로고
    • A phage-based system to select multiple protein-protein interactions simultaneously from combinatorial libraries
    • Rudert, F., Woltering, C., Frisch, C., Rottenberger, C., Ilag, L.L., 1998. A phage-based system to select multiple protein-protein interactions simultaneously from combinatorial libraries. FEBS Lett. 440, 135.
    • (1998) FEBS Lett , vol.440 , pp. 135
    • Rudert, F.1    Woltering, C.2    Frisch, C.3    Rottenberger, C.4    Ilag, L.L.5
  • 31
    • 0023716790 scopus 로고
    • Low-frequency infection of F-bacteria by transducing particles of filamentous bacteriophages
    • Russel, M., Whirlow, H., Sun, T.P., Webster, R.E., 1988. Low-frequency infection of F-bacteria by transducing particles of filamentous bacteriophages. J. Bacteriol. 170, 5312.
    • (1988) J. Bacteriol. , vol.170 , pp. 5312
    • Russel, M.1    Whirlow, H.2    Sun, T.P.3    Webster, R.E.4
  • 32
    • 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., 1993. 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, 1098.
    • (1993) J. Mol. Biol. , vol.234 , pp. 1098
    • Schulze-Gahmen, U.1    Rini, J.M.2    Wilson, I.A.3
  • 33
    • 0031729179 scopus 로고    scopus 로고
    • Selecting proteins with improved stability by a phage-based method
    • Sieber, V., Plückthun, A., Schmid, F.X., 1998. Selecting proteins with improved stability by a phage-based method. Nat. Biotechnol. 16, 955.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 955
    • Sieber, V.1    Plückthun, A.2    Schmid, F.X.3
  • 34
    • 0032561128 scopus 로고    scopus 로고
    • Reproducing the natural evolution of protein structural features with the selectively infective phage (SIP) technology. the kink in the first strand of antibody kappa domains
    • Spada, S., Honegger, A., Plückthun, A., 1998. Reproducing the natural evolution of protein structural features with the selectively infective phage (SIP) technology. The kink in the first strand of antibody kappa domains. J. Mol. Biol. 283, 395.
    • (1998) J. Mol. Biol. , vol.283 , pp. 395
    • Spada, S.1    Honegger, A.2    Plückthun, A.3
  • 35
    • 0000516715 scopus 로고
    • Translation of the sequence AGG-AGG yields 50% ribosomal frameshift
    • Spanjaard, R.A., van Duin, J., 1988. Translation of the sequence AGG-AGG yields 50% ribosomal frameshift. Proc. Natl. Acad. Sci. U.S.A. 85, 7967.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 7967
    • Spanjaard, R.A.1    Van Duin, J.2
  • 36
    • 0025273561 scopus 로고
    • Dissection of functional domains in phage fd adsorption protein. Discrimination between attachment and penetration sites
    • Stengele, I., Bross, P., Garces, X., Giray, J., Rasched, I., 1990. Dissection of functional domains in phage fd adsorption protein. Discrimination between attachment and penetration sites. J. Mol. Biol. 212, 143.
    • (1990) J. Mol. Biol. , vol.212 , pp. 143
    • Stengele, I.1    Bross, P.2    Garces, X.3    Giray, J.4    Rasched, I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.