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Volumn 15, Issue 1, 1997, Pages 79-84

Functional antibody production using cell-free translation: Effects of protein disulfide isomerase and chaperones

Author keywords

Cell free translation system; Disulfide isomerase; Molecular chaperones; Protein folding; Single chain antibody

Indexed keywords

ANTIBODY; CHAPERONE; DISULFIDE; GLUTATHIONE; HEMAGGLUTININ; PROTEIN DISULFIDE ISOMERASE;

EID: 0031021109     PISSN: 10870156     EISSN: 15461696     Source Type: Journal    
DOI: 10.1038/nbt0197-79     Document Type: Article
Times cited : (156)

References (49)
  • 1
    • 0028093512 scopus 로고
    • Protein engineering techniques for antibody humanization
    • Hurle, M.R. and Gross, M. 1994. Protein engineering techniques for antibody humanization. Cuir. Opin. Biotechnol. 5:428-433.
    • (1994) Cuir. Opin. Biotechnol. , vol.5 , pp. 428-433
    • Hurle, M.R.1    Gross, M.2
  • 2
    • 0027008593 scopus 로고
    • Mono- and bivalent antibody fragments produced in Escherichia coli: Engineering, folding and antigen binding
    • Plückthun, A. 1992. Mono- and bivalent antibody fragments produced in Escherichia coli: engineering, folding and antigen binding. Immunol. Rev. 130:151-188.
    • (1992) Immunol. Rev. , vol.130 , pp. 151-188
    • Plückthun, A.1
  • 3
    • 0028877140 scopus 로고
    • Production of monoclonal antibodies in COS and CHO cells
    • Trill, J.J., Shatzman, A.R., and Ganguly, S. 1995. Production of monoclonal antibodies in COS and CHO cells. Curr. Opin. Biotechnol. 6:553-560.
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 553-560
    • Trill, J.J.1    Shatzman, A.R.2    Ganguly, S.3
  • 4
    • 0018721964 scopus 로고
    • The role of the intrachain disulfide bond in the conformation and stability of the constant fragment of the immunoglobulin light chain
    • Goto, Y. and Hamaguchi, K. 1979. The role of the intrachain disulfide bond in the conformation and stability of the constant fragment of the immunoglobulin light chain. J. Biochem. 86:1433-1441.
    • (1979) J. Biochem. , vol.86 , pp. 1433-1441
    • Goto, Y.1    Hamaguchi, K.2
  • 5
    • 0026572809 scopus 로고
    • The disulfide bonds in antibody variable domains: Effects on stability, folding In vitro, and functional expression in
    • Glockshuber, Ft., Schmidt, T., and Plückthun, A. 1992. The disulfide bonds in antibody variable domains: effects on stability, folding In vitro, and functional expression in Escherichia coli. Biochemistry 31:1270-1279.
    • (1992) Escherichia Coli. Biochemistry , vol.31 , pp. 1270-1279
    • Glockshuber, F.T.1    Schmidt, T.2    Plückthun, A.3
  • 7
    • 0027959156 scopus 로고
    • Protein disulfide isomerase: Building bridges In protein folding
    • Freedman, R.B., Hirst, T.R., and Tuite, M.F. 1994. Protein disulfide isomerase: building bridges In protein folding. Trends Biochem. 19:331-336.
    • (1994) Trends Biochem , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 8
    • 0028964420 scopus 로고
    • The formation of protein disulphide bonds
    • Freedman, R.B. 1995. The formation of protein disulphide bonds. Curr. Op. Struct. Biol. 5:85-91.
    • (1995) Curr. Op. Struct. Biol. , vol.5 , pp. 85-91
    • Freedman, R.B.1
  • 9
    • 0028885790 scopus 로고
    • The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds
    • Laboissière, M.C.A., Sturley, S.L., and Raines, R.T. 1995. The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds. J. Biol. Chem. 270:28006-28009.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28006-28009
    • Laboissière, M.C.A.1    Sturley, S.L.2    Raines, R.T.3
  • 10
    • 0026738643 scopus 로고
    • The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase
    • Tachibana, C. and Stevens, T.H. 1992. The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase. Mol. Cell. Biol. 12:4601-4611.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 4601-4611
    • Tachibana, C.1    Stevens, T.H.2
  • 11
    • 0027203922 scopus 로고
    • The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity
    • LaMantia, M.L. and Lennarz, W.J. 1993. The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity. Cell 74:899-908.
    • (1993) Cell , vol.74 , pp. 899-908
    • Lamantia, M.L.1    Lennarz, W.J.2
  • 12
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell, J.C.A., McGovern, K., and Beckwith, J. 1991. Identification of a protein required for disulfide bond formation in vivo. Cell 67:581-589.
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.A.1    McGovern, K.2    Beckwith, J.3
  • 13
    • 0026567097 scopus 로고
    • Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme
    • Kamitani, S., Akiyama, Y, and Ito, K. 1992. Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme. EMBO J. 11:57-62.
    • (1992) EMBO J , vol.11 , pp. 57-62
    • Kamitani, S.1    Akiyama, Y.2    Ito, K.3
  • 14
    • 0028971218 scopus 로고
    • Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines od DsbB and DsbA. Rroc
    • Guilhot, C, Jander, G., Martin, N.L, and Beckwith, J. 1995. Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines od DsbB and DsbA. Rroc. Natl. Acad. Sci. USA 92:9895-9899.
    • (1995) Natl. Acad. Sci. USA , vol.92 , pp. 9895-9899
    • Guilhot, C.1    Jander, G.2    Martin, N.L.3    Beckwith, J.4
  • 15
    • 0029161150 scopus 로고
    • DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA
    • Kishigami, S., Kanaya, E., Kikuchi, M., and Ito, K. 1995. DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA. J. Biol. Chem. 270:17072-17074.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17072-17074
    • Kishigami, S.1    Kanaya, E.2    Kikuchi, M.3    Ito, K.4
  • 16
    • 0028296940 scopus 로고
    • The Escherichia coli dsbC (XprA) gene encodes a periplasmic protein Involved in disulfide bond formation
    • Missiakas, D., Georgopoulos, C, and Raina, S. 1994. The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein Involved in disulfide bond formation. EMBO J. 13:2013-2020.
    • (1994) EMBO J , vol.13 , pp. 2013-2020
    • Missiakas, D.1    Georgopoulos, C.2    Raina, S.3
  • 17
    • 0028949156 scopus 로고
    • Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli
    • Zapun, A., Missiakas, D., Raina, S., and Creighton, TE. 1995. Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. Biochemistry 34:5075-5089.
    • (1995) Biochemistry , vol.34 , pp. 5075-5089
    • Zapun, A.1    Missiakas, D.2    Raina, S.3    Creighton, T.E.4
  • 18
    • 0028979629 scopus 로고
    • Identification and characterization of a new disulfide isomerase-llke protein (DsbD) in Escherichia coli
    • Missiakas, D., Schwager, F., and Raina, S. 1995. Identification and characterization of a new disulfide isomerase-llke protein (dsbD) in Escherichia coli. EMBO J. 14:3415-3424.
    • (1995) EMBO J , vol.14 , pp. 3415-3424
    • Missiakas, D.1    Schwager, F.2    Raina, S.3
  • 19
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hart, FU. 1996. Molecular chaperones in cellular protein folding. Nature 381:571-579.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hart, F.U.1
  • 20
    • 0004198722 scopus 로고
    • Protein engineering of antibody binding sites: Recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli
    • Huston, J.S., Levinson, D., Mudgett-Hunter, M., Tai, M.-S., Novotny, J., Margolies, M.N., et al. 1988. Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli. Proc. Natl. Acad. Sci. USA 85:5879-5883.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5879-5883
    • Huston, J.S.1    Levinson, D.2    Mudgett-Hunter, M.3    Tai, M.-S.4    Novotny, J.5    Margolies, M.N.6
  • 21
    • 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., and 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. 234:1098-1118.
    • (1993) J. Mol. Biol. , vol.234 , pp. 1098-1118
    • Schulze-Gahmen, U.1    Rini, J.M.2    Wilson, I.A.3
  • 22
    • 0027460290 scopus 로고
    • Characterization of single-chain antibody (SFv)-toxin fusion proteins produced in vitro in rabbit reticulocyte lysate
    • Nicholls, P.J., Johnson, V.G., Andrew, S.M., Hoogenboom, H.R., Raus, J.C.M. and Youle, R.J. 1993. Characterization of single-chain antibody (sFv)-toxin fusion proteins produced in vitro in rabbit reticulocyte lysate. J. Biol. Chem. 268:5302-5308.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5302-5308
    • Nicholls, P.J.1    Johnson, V.G.2    Rew, S.M.3    Hoogenboom, H.R.4    Raus, J.C.M.5    Youle, R.J.6
  • 23
    • 0029068068 scopus 로고
    • Functional antibody single-chain fragments from the cytoplasm of Escherichia coli: Influence of thioredoxin reductase (TrxB)
    • Proba, K., Ge, L., and Plückthun, A. 1995. Functional antibody single-chain fragments from the cytoplasm of Escherichia coli: influence of thioredoxin reductase (TrxB). Gene 159:203-207.
    • (1995) Gene , vol.159 , pp. 203-207
    • Proba, K.1    Ge, L.2    Plückthun, A.3
  • 24
    • 0027366182 scopus 로고
    • Bacterial protein disulfide isomerase: Efficient catalysis of oxidative protein folding at acidic pH
    • Wunderlich, M., Otto, A., Seckler, R., and Glockshuber, R. 1993. Bacterial protein disulfide isomerase: Efficient catalysis of oxidative protein folding at acidic pH. Biochemistry 32:12251-12256.
    • (1993) Biochemistry , vol.32 , pp. 12251-12256
    • Wunderlich, M.1    Otto, A.2    Seckler, R.3    Glockshuber, R.4
  • 25
    • 0028953741 scopus 로고
    • Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase
    • Darby, N.J. and Creighton, T.E. 1995. Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase. Biochemistry 34:3576-3587.
    • (1995) Biochemistry , vol.34 , pp. 3576-3587
    • Darby, N.J.1    Creighton, T.E.2
  • 26
    • 0029093531 scopus 로고
    • Functional properties of the individual thiore-doxin-like domains of protein disulfide isomerase
    • Darby, N.J. and Creighton, T.E. 1995. Functional properties of the individual thiore-doxin-like domains of protein disulfide isomerase. Biochemistry 34:11725-11735.
    • (1995) Biochemistry , vol.34 , pp. 11725-11735
    • Darby, N.J.1    Creighton, T.E.2
  • 27
    • 0026062381 scopus 로고
    • Catalysis of the oxidative folding of ribonu-clease A by protein disulfide isomerase: Dependence of the rate on the composition of the redox buffer
    • Lyles, M.M. and Gilbert, H.F. 1991. Catalysis of the oxidative folding of ribonu-clease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer. Biochemistry 30:613-619.
    • (1991) Biochemistry , vol.30 , pp. 613-619
    • Lyles, M.M.1    Gilbert, H.F.2
  • 28
    • 0029058524 scopus 로고
    • Chaperone-like activity of protein disulfide isomerase In the refolding of rhodanese
    • Song, J.L. and Wang, CO 1995. Chaperone-like activity of protein disulfide isomerase In the refolding of rhodanese. Eur. J. Biochem. 231:312-316.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 312-316
    • Song, J.L.1    Wang, C.O.2
  • 29
    • 0029146852 scopus 로고
    • Independence of the chaperone activity of protein disulfide isomerase from its thioredoxin-like active site
    • Quan, H., Fan, G., and Wang, CO 1995. Independence of the chaperone activity of protein disulfide isomerase from its thioredoxin-like active site. J. Biol. Chem. 270:17078-17080.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17078-17080
    • Quan, H.1    Fan, G.2    Wang, C.O.3
  • 30
    • 0023653141 scopus 로고
    • In vivo cross-linking of protein disulfide isomerase to immunoglobulins
    • Roth, R.A. and Pierce, S.B. 1987. In vivo cross-linking of protein disulfide isomerase to immunoglobulins. Biochemistry 26:4179-4182.
    • (1987) Biochemistry , vol.26 , pp. 4179-4182
    • Roth, R.A.1    Pierce, S.B.2
  • 31
    • 0025730978 scopus 로고
    • Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
    • Liberek, K., Marszalek, J., Ang, D., Georgopoulos, C, and Zylicz, M. 1991. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl. Acad. Sci. USA 88:2874-2878.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2874-2878
    • Liberek, K.1    Marszalek, J.2    Ang, D.3    Georgopoulos, C.4    Zylicz, M.5
  • 32
    • 0026596223 scopus 로고
    • Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
    • Langer, T., Lu, C, Echols, H., Flanagan, J., Hayer, M.K., and Hartl, F.U. 1992. Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature 356:683-689.
    • (1992) Nature , vol.356 , pp. 683-689
    • Langer, T.1    Lu, C.2    Echols, H.3    Flanagan, J.4    Hayer, M.K.5    Hartl, F.U.6
  • 33
    • 0028382510 scopus 로고
    • A conserved loop in the ATPase domain of the DnaK chaperone Is essential for stable binding of GrpE
    • Buchberger, A., Schröder, H., Büttner, M., Valencia, A., and Bukau, B. 1994. A conserved loop in the ATPase domain of the DnaK chaperone Is essential for stable binding of GrpE. Nature Struct. Biol. 1:95-101.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 95-101
    • Buchberger, A.1    Schröder, H.2    Büttner, M.3    Valencia, A.4    Bukau, B.5
  • 34
    • 0028361309 scopus 로고
    • Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
    • Frydman, J., Nimmesgern, E., Ohtsuka, K., and Hartl, F.U. 1994. Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature 370:111-117.
    • (1994) Nature , vol.370 , pp. 111-117
    • Frydman, J.1    Nimmesgern, E.2    Ohtsuka, K.3    Hartl, F.U.4
  • 35
    • 0023052239 scopus 로고
    • An Hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein
    • Munro, S. and Pelham, H.R.B. 1986. An Hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell 46:291-300.
    • (1986) Cell , vol.46 , pp. 291-300
    • Munro, S.1    Pelham, H.R.B.2
  • 36
    • 0028170231 scopus 로고
    • Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum
    • Melnick, J., Dui, J.L, and Argon, Y. 1994. Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum. Nature 370:373-375.
    • (1994) Nature , vol.370 , pp. 373-375
    • Melnick, J.1    Dui, J.L.2    Argon, Y.3
  • 37
    • 0025303147 scopus 로고
    • Interaction of Hsp 70 with newly synthesized proteins: Implications for protein folding and assembly
    • Beckmann, R.R, Mizzen, L.E., and Welch, W.J. 1990. Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly. Science 248:850-854.
    • (1990) Science , vol.248 , pp. 850-854
    • Beckmann, R.R.1    Mizzen, L.E.2    Welch, W.J.3
  • 38
    • 0026649409 scopus 로고
    • The translation machinery and 70 kD heat shock protein cooperate in protein synthesis
    • Nelson, R.J., Ziegelhoffer, T, Nicolet, O, Werner-Washburne, M., and Craig, E.A. 1992. The translation machinery and 70 kD heat shock protein cooperate in protein synthesis. Cell 71:97-105.
    • (1992) Cell , vol.71 , pp. 97-105
    • Nelson, R.J.1    Ziegelhoffer, T.2    Nicolet, O.3    Werner-Washburne, M.4    Craig, E.A.5
  • 39
    • 0027425585 scopus 로고
    • Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides
    • Hendrick, J.R, Langer, T., Davis, TA., Hartl, F.U., and Wiedmann, M. 1993. Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides. Proc. Natl. Acad. Sci. USA 90:10216-10220.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10216-10220
    • Hendrick, J.R.1    Langer, T.2    Davis, T.A.3    Hartl, F.U.4    Wiedmann, M.5
  • 41
    • 0024297305 scopus 로고
    • A continuous cell-free translation system capable of producing polypeptides in high yield
    • Spirin, A.S., Baranov, V.I., Ryabova, L.A., Ovodov, S. Yu., and Alakhov, Yu. B. 1988. A continuous cell-free translation system capable of producing polypeptides in high yield. Science 242:1162-1164.
    • (1988) Science , vol.242 , pp. 1162-1164
    • Spirin, A.S.1    Baranov, V.I.2    Ryabova, L.A.3    Ovodov, S.Y.4    Alakhov, Y.B.5
  • 42
    • 0027050148 scopus 로고
    • Recursive PCR: A novel technique for total gene synthesis
    • Prodromou, C. and Pearl, L.H. 1992. Recursive PCR: a novel technique for total gene synthesis. Prot. Eng. 5:827-829.
    • (1992) Prot. Eng. , vol.5 , pp. 827-829
    • Prodromou, C.1    Pearl, L.H.2
  • 43
    • 0027529014 scopus 로고
    • Characterization of the linker peptide of the single-chain Fv fragment of an antibody by NMR spectroscopy
    • Freund, C, Ross, A., Guth, B., Plückthun, A., and Holak, TA. 1993. Characterization of the linker peptide of the single-chain Fv fragment of an antibody by NMR spectroscopy. FEBS Lett. 320:97-100.
    • (1993) FEBS Lett , vol.320 , pp. 97-100
    • Freund, C.1    Ross, A.2    Guth, B.3    Plückthun, A.4    Holak, T.A.5
  • 45
    • 0020645081 scopus 로고
    • Prokaryotic coupled transcription-translation
    • Chen, H.-Z. and Zubay, G. 1983. Prokaryotic coupled transcription-translation. Methods Enzymol. 101:674-690.
    • (1983) Methods Enzymol , vol.101 , pp. 674-690
    • Chen, H.-Z.1    Zubay, G.2
  • 47
    • 0003044623 scopus 로고
    • Purification of native proteins from the cytoplasm and periplasm of Escherichia coli using IMAC and histldine tails: A comparison of proteins and protocols
    • Lindner, P., Guth, B., Wülfing, O, Krebber, O, Steipe, B., Müller, F., and Plückthun, A. 1992. Purification of native proteins from the cytoplasm and periplasm of Escherichia coli using IMAC and histldine tails: a comparison of proteins and protocols. Methods: A Companion to Meth. Enzymol. 4:41-56.
    • (1992) Methods: A Companion to Meth. Enzymol. , vol.4 , pp. 41-56
    • Lindner, P.1    Guth, B.2    Wülfing, O.3    Krebber, O.4    Steipe, B.5    Müller, F.6    Plückthun, A.7
  • 48
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 49
    • 0018177601 scopus 로고
    • A new method for preparation of an antiserum to penicillin and its application for novel enzyme Immunoassay of penicillin
    • Kitagawa, T., Kanamaru, T., Wakamatsu, H., Kato, H., Yano, S., and Asanuma, Y. 1978. A new method for preparation of an antiserum to penicillin and its application for novel enzyme Immunoassay of penicillin. J. Biochem. 84:491-494.
    • (1978) J. Biochem. , vol.84 , pp. 491-494
    • Kitagawa, T.1    Kanamaru, T.2    Wakamatsu, H.3    Kato, H.4    Yano, S.5    Asanuma, Y.6


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