Antibody scFv fragments without disulfide bonds made by molecular evolution

Journal of Molecular Biology

Volumn 275, Issue 2, 1998, Pages 245-253

  Proba, Karl ^a   Wörn, Arne ^a   Honegger, Annemarie ^a   Plückthun, Andreas ^a  

^a UNIVERSITY OF ZURICH   (Switzerland)

Author keywords

Antibody engineering; Cytoplasmic expression; Disulfide bond; Intrabodies; scFv fragment

Indexed keywords

ANTIBODY; CYSTEINE; DNA; IMMUNOGLOBULIN FRAGMENT; LEVAN;

ANTIBODY PRODUCTION; ARTICLE; CONTROLLED STUDY; DISULFIDE BOND; ESCHERICHIA COLI; NONHUMAN; PHAGE DISPLAY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DENATURATION; PROTEIN EXPRESSION; THERMODYNAMICS;

ESCHERICHIA COLI;

EID: 0344813702     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1457     Document Type: Article

References (25)

1. Biocca, S. & Cattaneo, A. (1995). Intracellular immunization: antibody targeting to subcellular compartments. Trends Cell Biol. 5, 248-252.
2. Biocca, S., Ruberti, F., Tafani, M., Pierandrei-Amaldi, P. & Cattaneo, A. (1995). Redox state of scFv fragments targeted to the endoplasmic reticulum, cytosol and mitochondria. Biotechnology, 13, 1110-1115.
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, 1027-1033.
4. Freund, C., Ross, A., Guth, B., Plückthun, A. & Holak, T. A. (1993). Characterization of the linker peptide of the single-chain Fv fragment of an antibody by NMR spectroscopy. FEBS Letters, 320, 97-100.
5. Frisch, C., Kolmar, H. & Fritz, H. J. (1994). A soluble immunoglobulin variable domain without a disulfide bridge: construction, accumulation in the cytoplasm of E. coli, purification and physicochemical characterization. Biol. Chem. Hoppe-Seyler, 375, 353-356.
6. Frisch, C., Kolmar, H., Schmidt, A., Kleemann, G., Reinhardt, A., Pohl, E., Usón, I., Schneider, T. R. & Fritz, H. J. (1996). Contribution of the intramolecular disulfide bridge to the folding stability of REI(v), the variable domain of a human immunoglobulin kappa light chain. Fold. Des. 1, 431-440.
7. Glockshuber, R., Schmidt, T. & 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.
8. Goto, Y. & Hamaguchi, K. (1979). The role of the intra-chain disulfide bond in the conformation and stability of the constant fragment of the immunoglobulin light chain. J. Biochem. 86, 1433-1441.
9. Holliger, P., Prospero, T. & Winter, G. (1993). "Diabodies": small bivalent and bispecific antibody fragments. Proc. Natl Acad. Sci. USA, 90, 6444-6448.
10. Inoue, H., Nojima, H. & Okayama, H. (1990). High efficiency transformation of Escherichia coli with plasmids. Gene, 96, 23-28.
11. Kabat, E. A., Wu, T. T., Perry, H M., Gottesman, K. S. & Foeller, C. (1991). Variable region heavy chain sequences. In Sequences of Proteins of Immunological Interest. NIH Publication No. 91-3242, National Technical Information Service (NTIS).
12. Krebber, A., Bornhauser, S., Burmester, J., Honegger, A., Willuda, J., Bosshard, H. R. & Plückthun, A. (1997). Reliable cloning of functional antibody variable domains from hybridomas and spleen repertoires employing a reengineered phage display system. J. Immun. Methods, 201, 35-55.
13. Liu, Y., Breslauer, K. & Anderson, S. (1997). "Designing out" disulfide bonds: thermodynamic properties of 30-51 cystine substitution mutants of bovine pancreatic trypsin inhibitor. Biochemistry, 36, 5323-5335.
14. Munro, S. & 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.
15. Pace, C. N. (1990). Measuring and increasing protein stability. Trends Biotechnol. 8, 93-98.
16. H: consequences for thermodynamic stability and folding. J. Mol. Biol. 265, 161-172.
17. Richardson, J. H. & Marasco, W. A. (1995). Intracellular antibodies: development and therapeutic potential. Trends Biotechnol. 13, 306-310.
18. Rudikoff, S. & Pumphrey, J. G. (1986). Functional antibody lacking a variable-region disulfide bridge. Proc. Natl Acad. Sci. USA, 83, 7875-7878.
19. Saul, F. A. & Poljak, R. J. (1992). Crystal structure of human immunoglobulin fragment Fab New refined at 2.0 Å resolution. Proteins: Struct. Funct. Genet. 14, 363-371.
20. Schier, R., Bye, J., Apell, G., McCall, A., Adams, G. P., Malmqvist, M., Weiner, L. M. & Marks, J. D. (1996). Isolation of high-affinity monomeric human anti-c-erbB-2 single chain Fv using affinity-driven selection. J. Mol. Biol. 255, 28-43.
21. Stemmer, W. P. C. (1994). Rapid evolution of a protein in vitro by DNA shuffling. Nature, 370, 389-391.
22. Strong, R. K., Campbell, R., Rose, D. R., Petsko, G. A., Sharon, J. & Margolies, M. N. (1991). Three-dimensional structure of murine anti-p-azophenylarsonate Fab 36-71. 1. X-ray crystallography, site-directed mutagenesis, and modeling of the complex with hapten. Biochemistry, 30, 3739-3748.
23. Studier, F. W. & Moffatt, B. A. (1986). Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189, 113-130.
24. Tang, Y., Jiang, N., Parakh, C. & Hilvert, D. (1996). Selection of linkers for a catalytic single-chain antibody using phage display technology. J. Biol. Chem. 271, 15682-15686.
25. Whitlow, M., Filpula, D., Rollence, M. L., Feng, S. L. & Wood, J. F. (1994). Multivalent Fvs: characterization of single-chain Fv oligomers and preparation of a bispecific Fv. Protein Eng. 7, 1017-1026.