메뉴 건너뛰기




Volumn 64, Issue 12, 1998, Pages 4862-4869

Procaryotic expression of single-chain variable-fragment (scFv) antibodies: Secretion in L-form cells of Proteus mirabilis leads to active product and overcomes the limitations of periplasmic expression in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; IMMUNOGLOBULIN FRAGMENT;

EID: 0031766998     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.64.12.4862-4869.1998     Document Type: Article
Times cited : (54)

References (37)
  • 1
    • 0025123399 scopus 로고
    • Folding and aggregation of β-lactamase in the periplasmic space of E. coli
    • Bowden, G. A., and G. Georgiou. 1990. Folding and aggregation of β-lactamase in the periplasmic space of E. coli. J. Biol. Chem. 265:16760-16766.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16760-16766
    • Bowden, G.A.1    Georgiou, G.2
  • 2
    • 0343035661 scopus 로고    scopus 로고
    • A TNF receptor antagonist scFv, which is not secreted in mammalian cells, is expressed as a soluble mono- and bivalent scFv derivative in insect cells
    • Amsterdam
    • Brocks, B., H.-J. Rode, M. Klein, E. Gerlach, S. Dübel, M. Little, K. Pfizenmaier, and D. Moosmayer. 1997. A TNF receptor antagonist scFv, which is not secreted in mammalian cells, is expressed as a soluble mono- and bivalent scFv derivative in insect cells. Immunotechnology (Amsterdam) 4:173-184.
    • (1997) Immunotechnology , vol.4 , pp. 173-184
    • Brocks, B.1    Rode, H.-J.2    Klein, M.3    Gerlach, E.4    Dübel, S.5    Little, M.6    Pfizenmaier, K.7    Moosmayer, D.8
  • 3
    • 0027457077 scopus 로고
    • A signal sequence is not required for protein export in prlA mutants of E. coli
    • Derman, A. I., J. W. Puziss, P. J. Bassford, and J. Beckwith. 1993. A signal sequence is not required for protein export in prlA mutants of E. coli. EMBO J. 12:879-888.
    • (1993) EMBO J. , vol.12 , pp. 879-888
    • Derman, A.I.1    Puziss, J.W.2    Bassford, P.J.3    Beckwith, J.4
  • 4
    • 0027967844 scopus 로고
    • How proteins cross the bacterial cytoplasmic membrane
    • Driessen, A. J. M. 1994. How proteins cross the bacterial cytoplasmic membrane. J. Membr. Biol. 142:145-159.
    • (1994) J. Membr. Biol. , vol.142 , pp. 145-159
    • Driessen, A.J.M.1
  • 5
    • 0026900343 scopus 로고
    • Regulated secretion and purification of recombinant antibodies in E. coli
    • Dübel, S., F. Breitling, I. Klewinghaus, and M. Little. 1992. Regulated secretion and purification of recombinant antibodies in E. coli. Cell Biophys. 21:69-79.
    • (1992) Cell Biophys. , vol.21 , pp. 69-79
    • Dübel, S.1    Breitling, F.2    Klewinghaus, I.3    Little, M.4
  • 7
    • 0030912095 scopus 로고    scopus 로고
    • Identification of framework residues in a secreted recombinant antibody fragment that control production level and localisation in E. coli
    • Forstberg, G., M. Forsgren, M. Jaki, M. Norin, C. Sterky, A. Enhörning, K. Larsson, M. Ericsson, and P. Björk. 1997. Identification of framework residues in a secreted recombinant antibody fragment that control production level and localisation in E. coli. J. Biol. Chem. 272:12430-12436.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12430-12436
    • Forstberg, G.1    Forsgren, M.2    Jaki, M.3    Norin, M.4    Sterky, C.5    Enhörning, A.6    Larsson, K.7    Ericsson, M.8    Björk, P.9
  • 8
    • 0030069429 scopus 로고    scopus 로고
    • Advances in immunotoxin biology and therapy: A summary of the Fourth International Symposium on Immunotoxins
    • Frankel, A. E., D. FritzGerald, C. Siegall, and O. W. Press. 1996. Advances in immunotoxin biology and therapy: a summary of the Fourth International Symposium on Immunotoxins. Cancer Res. 56:926-932.
    • (1996) Cancer Res. , vol.56 , pp. 926-932
    • Frankel, A.E.1    Fritzgerald, D.2    Siegall, C.3    Press, O.W.4
  • 9
    • 0025083528 scopus 로고
    • Cell surface glycoprotein of reactive stromal fibroblasts as a potential antibody target in human epithelial cancers
    • Garin-Chesa, P., L. J. Old, and W. J. Rettig. 1990. Cell surface glycoprotein of reactive stromal fibroblasts as a potential antibody target in human epithelial cancers. Proc. Natl. Acad. Sci. USA 87:7235-7239.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7235-7239
    • Garin-Chesa, P.1    Old, L.J.2    Rettig, W.J.3
  • 10
    • 0025162270 scopus 로고
    • A comparison of strategies to stabilise immunoglobulin Fv-fragments
    • Glockshuber, R., M. Malia, I. Pfizinger, and A. Plückthun. 1990. A comparison of strategies to stabilise immunoglobulin Fv-fragments. Biochemistry 29:1362-1367.
    • (1990) Biochemistry , vol.29 , pp. 1362-1367
    • Glockshuber, R.1    Malia, M.2    Pfizinger, I.3    Plückthun, A.4
  • 11
    • 85069112217 scopus 로고    scopus 로고
    • Unpublished data
    • 10a. Gumpert, J. Unpublished data.
    • Gumpert, J.1
  • 12
    • 0029689586 scopus 로고    scopus 로고
    • Synthesis and secretion of recombinant penicillin G acylase in bacterial L-forms
    • Gumpert, J., H. Cron, R. Plapp, H. Niersbach, and C. Hoischen. 1996. Synthesis and secretion of recombinant penicillin G acylase in bacterial L-forms. J. Basic Microbiol. 36:89-98.
    • (1996) J. Basic Microbiol. , vol.36 , pp. 89-98
    • Gumpert, J.1    Cron, H.2    Plapp, R.3    Niersbach, H.4    Hoischen, C.5
  • 13
    • 0021004977 scopus 로고
    • Characteristic properties and biological significance of stable protoplast type L-forms
    • Gumpert, J., and U. Taubeneck. 1983. Characteristic properties and biological significance of stable protoplast type L-forms. Exper. Suppl. 46:227-241.
    • (1983) Exper. Suppl. , vol.46 , pp. 227-241
    • Gumpert, J.1    Taubeneck, U.2
  • 15
    • 0030974363 scopus 로고    scopus 로고
    • Lipid and fatty acid composition of cytoplasmatic membranes from Streptomyces hygroscopicus and its stable protoplast-type L form
    • Hoischen, C., K. Gura, C. Luge, and J. Gumpert. 1997. Lipid and fatty acid composition of cytoplasmatic membranes from Streptomyces hygroscopicus and its stable protoplast-type L form. J. Bacteriol. 179:3430-3436.
    • (1997) J. Bacteriol. , vol.179 , pp. 3430-3436
    • Hoischen, C.1    Gura, K.2    Luge, C.3    Gumpert, J.4
  • 17
    • 0028966985 scopus 로고
    • Engineered turns of a recombinant antibody improve its in vivo folding
    • Knappik, A., and A. Plückthun. 1995. Engineered turns of a recombinant antibody improve its in vivo folding. Protein Eng. 8:81-89.
    • (1995) Protein Eng. , vol.8 , pp. 81-89
    • Knappik, A.1    Plückthun, A.2
  • 18
    • 14744305361 scopus 로고
    • The effect of folding catalysts on the in vivo folding process of different antibody fragments expressed in E. coli
    • Knappik, A., C. Krebber, and A. Plückthun. 1993. The effect of folding catalysts on the in vivo folding process of different antibody fragments expressed in E. coli. Bio/Technology 11:77-83.
    • (1993) Bio/Technology , vol.11 , pp. 77-83
    • Knappik, A.1    Krebber, C.2    Plückthun, A.3
  • 19
    • 0028928021 scopus 로고
    • Molecular chaperones involved in protein degradation in the endoplasmatic reticulum: Quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmatic reticulum
    • Knittler, M. R., S. Dirks, and I. G. Haas. 1995. Molecular chaperones involved in protein degradation in the endoplasmatic reticulum: quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmatic reticulum. Proc. Natl. Acad. Sci. USA 92:1764-1768.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1764-1768
    • Knittler, M.R.1    Dirks, S.2    Haas, I.G.3
  • 20
    • 0030576931 scopus 로고    scopus 로고
    • High-level expression in insect cells and purification of secreted monomeric single-chain Fv antibodies
    • Kretzschmar, T., L. Aoustin, O. Zingel, M. Marangi, B. Vonach, H. Towbin, and M. Geiser. 1996. High-level expression in insect cells and purification of secreted monomeric single-chain Fv antibodies. J. Immunol. Methods 195: 93-101.
    • (1996) J. Immunol. Methods , vol.195 , pp. 93-101
    • Kretzschmar, T.1    Aoustin, L.2    Zingel, O.3    Marangi, M.4    Vonach, B.5    Towbin, H.6    Geiser, M.7
  • 21
    • 0031973556 scopus 로고    scopus 로고
    • Expression and secretion of functional miniantibodies McPC603scFvDhlx in cell wallless L-form strains of Proteus mirabilis and E. coli
    • Kujau, M. J., C. Hoischen, D. Riesenberg, and J. Gumpert. 1998. Expression and secretion of functional miniantibodies McPC603scFvDhlx in cell wallless L-form strains of Proteus mirabilis and E. coli. Appl. Microbiol. Biotechnol. 49:51-58.
    • (1998) Appl. Microbiol. Biotechnol. , vol.49 , pp. 51-58
    • Kujau, M.J.1    Hoischen, C.2    Riesenberg, D.3    Gumpert, J.4
  • 22
    • 27844488066 scopus 로고
    • Novel shuttle vectors for improved streptokinase expression in streptococci and bacterial L-forms
    • Laplace, F., J. Müller, J. Gumpert, and H. Malke. 1989. Novel shuttle vectors for improved streptokinase expression in streptococci and bacterial L-forms. FEMS Microbiol. Lett. 65:89-94.
    • (1989) FEMS Microbiol. Lett. , vol.65 , pp. 89-94
    • Laplace, F.1    Müller, J.2    Gumpert, J.3    Malke, H.4
  • 25
    • 0030893407 scopus 로고    scopus 로고
    • Protein folding in the bacterial periplasm
    • Missiakas, D., and S. Raina. 1997. Protein folding in the bacterial periplasm. J. Bacteriol. 179:2465-2471.
    • (1997) J. Bacteriol. , vol.179 , pp. 2465-2471
    • Missiakas, D.1    Raina, S.2
  • 27
    • 0030965970 scopus 로고    scopus 로고
    • Disrupting the hydrophobic patches at the antibody variable/constant domain interface: Improving in vivo folding and physical characterisation of an engineered scFv fragment
    • Nieba, L., A. Honegger, C. Krebber, and A. Plückthun. 1997. Disrupting the hydrophobic patches at the antibody variable/constant domain interface: improving in vivo folding and physical characterisation of an engineered scFv fragment. Protein Eng. 10:435-444.
    • (1997) Protein Eng. , vol.10 , pp. 435-444
    • Nieba, L.1    Honegger, A.2    Krebber, C.3    Plückthun, A.4
  • 28
    • 0027442660 scopus 로고
    • Improved bivalent miniantibodies, with identical avidity as whole antibodies, produced by high cell density fermentation of E. coli
    • Pack, P., M. Kujau, V. Schroeckh, U. Knüpfer, R. Wenderoth, D. Riesenberg, and A. Plückthun. 1993. Improved bivalent miniantibodies, with identical avidity as whole antibodies, produced by high cell density fermentation of E. coli. Bio/Technology 11:1271-1277.
    • (1993) Bio/Technology , vol.11 , pp. 1271-1277
    • Pack, P.1    Kujau, M.2    Schroeckh, V.3    Knüpfer, U.4    Wenderoth, R.5    Riesenberg, D.6    Plückthun, A.7
  • 29
    • 0031030579 scopus 로고    scopus 로고
    • Assisted protein folding
    • Ruddon, R. W., and E. Bedows. 1997. Assisted protein folding. J. Biol. Chem. 272:3125-3128.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3125-3128
    • Ruddon, R.W.1    Bedows, E.2
  • 30
    • 0030575802 scopus 로고    scopus 로고
    • Isolation of picomolar affinity anti-c-erbB-2 single-chain Fv by molecular evolution of the complementarity determination regions in the centre of the antibody binding site
    • Schier, R., A. McCall, G. P. Adams, K. W. Marshall, H. Merritt, M. Yim, R. S. Crawford, L. M. Weiner, C. Marks, and J. D. Marks. 1996. Isolation of picomolar affinity anti-c-erbB-2 single-chain Fv by molecular evolution of the complementarity determination regions in the centre of the antibody binding site. J. Mol. Biol. 263:551-567.
    • (1996) J. Mol. Biol. , vol.263 , pp. 551-567
    • Schier, R.1    McCall, A.2    Adams, G.P.3    Marshall, K.W.4    Merritt, H.5    Yim, M.6    Crawford, R.S.7    Weiner, L.M.8    Marks, C.9    Marks, J.D.10
  • 32
    • 0028555357 scopus 로고
    • Use of the tetracycline promoter for the tightly regulated production of a murine antibody fragment in E. coli
    • Skerra, A. 1994. Use of the tetracycline promoter for the tightly regulated production of a murine antibody fragment in E. coli. Gene 151:131-135.
    • (1994) Gene , vol.151 , pp. 131-135
    • Skerra, A.1
  • 33
    • 0026350603 scopus 로고
    • ab fragment of the antibody McPC603 in E. coli: Influence of disulphides and cis-prolines
    • ab fragment of the antibody McPC603 in E. coli: influence of disulphides and cis-prolines. Protein Eng. 4:971-979.
    • (1991) Protein Eng. , vol.4 , pp. 971-979
    • Skerra, A.1    Plückthun, A.2
  • 34
    • 0027973672 scopus 로고
    • Bacterial aspects associated with the expression of a single-chain antibody fragment in E. coli
    • Sommerville, J. E., S. C. Goshorn, H. P. Fell, and R. P. Darveau. 1995. Bacterial aspects associated with the expression of a single-chain antibody fragment in E. coli. Appl. Microbiol. Biotechnol. 42:595-603.
    • (1995) Appl. Microbiol. Biotechnol. , vol.42 , pp. 595-603
    • Sommerville, J.E.1    Goshorn, S.C.2    Fell, H.P.3    Darveau, R.P.4
  • 35
    • 0029785453 scopus 로고    scopus 로고
    • Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition
    • Speed, M. A., D. I. C. Wang, and J. King. 1996. Specific aggregation of partially folded polypeptide chains: the molecular basis of inclusion body composition. Nat. Biotechnol. 14:1283-1287.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1283-1287
    • Speed, M.A.1    Wang, D.I.C.2    King, J.3
  • 36
    • 0027997012 scopus 로고
    • Correctly folded T-cell receptor fragments in the periplasm of E. coli
    • Wülfing, C., and A. Plückthun. 1994. Correctly folded T-cell receptor fragments in the periplasm of E. coli. J. Mol. Biol. 242:655-669.
    • (1994) J. Mol. Biol. , vol.242 , pp. 655-669
    • Wülfing, C.1    Plückthun, A.2
  • 37
    • 0028286019 scopus 로고
    • Protein folding in the periplasm of E. coli
    • Wülfing, C., and A. Pl̈ckthun. 1994. Protein folding in the periplasm of E. coli. Mol. Microbiol. 12:685-692.
    • (1994) Mol. Microbiol. , vol.12 , pp. 685-692
    • Wülfing, C.1    Pl̈ckthun, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.