Selection for improved protein stability by phage display

Journal of Molecular Biology

Volumn 294, Issue 1, 1999, Pages 163-180

  Jung, Sabine ^a   Honegger, Annemarie ^a   Plückthun, Andreas ^a  

^a UNIVERSITY OF ZURICH   (Switzerland)

Author keywords

Antibody engineering; Chemical and thermal denaturation; DNA shuffling; Phage display; Protein stability

Indexed keywords

GUANIDINE; MUTANT PROTEIN; OLIGONUCLEOTIDE;

ANTIGEN BINDING; ARTICLE; CONTROLLED STUDY; DENATURATION; ENZYME LINKED IMMUNOSORBENT ASSAY; ESCHERICHIA COLI; GENETIC ENGINEERING; MOLECULAR MODEL; MUTAGENESIS; NONHUMAN; PHAGE DISPLAY; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN STABILITY; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY;

ESCHERICHIA COLI; TRIXIS;

EID: 0033584889     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3196     Document Type: Article

References (48)

1. Bass S., Gu Q., Christen A. Multicopy suppressors of prc mutant Escherichia coli include two HtrA (DegP) protease homologs (HhoAB), DksA, and a truncated R1pA. J. Bacteriol. 178:1996;1154-1161.
2. Bedzyk W. D., Swindlehurst C. A., Voss E. W. Jr. Relative binding properties of fluorescein and 9-hydroxyphenylfluoron (HPF) with murine monoclonal anti-fluorescein antibodies. Biochim. Biophys. Acta. 1119:1992;27-34.
3. Braisted A. C., Wells J. A. Minimizing a binding domain from protein A. Proc. Natl Acad. Sci. USA. 93:1996;5688-5692.
4. Carter P., Presta L., Gorman C. M., Ridgway J. B., Henner D., Wong W. L., Rowland A. M., Kotts C., Carver M. E., Shepard H. M. Humanization of an anti-p185HER2 antibody for human cancer therapy. Proc. Natl Acad. Sci. USA. 89:1992;4285-4289.
5. de Haard H. J., Kazemier B., van der Bent A., Oudshoorn P., Boender P., van Gemen B., Arends J. W., Hoogenboom H. R. Absolute conservation of residue 6 of immunoglobulin heavy chain variable regions of class IIA is required for correct folding. Protein Eng. 11:1998;1267-1276.
6. Deng S. J., MacKenzie C. R., Sadowska J., Michniewicz J., Young N. M., Bundle D. R., Narang S. A. Selection of antibody single-chain variable fragments with improved carbohydrate binding by phage display. J. Biol. Chem. 269:1994;9533-9538.
7. Eigenbrot C., Randal M., Presta L., Carter P., Kossiakoff A. A. X-ray structures of the antigen-binding domains from three variants of humanized anti-p185HER2 antibody 4D5 and comparison with molecular modeling. J. Mol. Biol. 229:1993;969-995.
8. Figini M., Marks J. D., Winter G., Griffiths A. D. In vitro assembly of repertoires of antibody chains on the surface of phage by renaturation. J. Mol. Biol. 239:1994;68-78.
9. Forsberg G., Forsgren M., Jaki M., Norin M., Sterky C., Enhörning Å., Larsson K., Ericsson M., Björk P. Identification of framework residues in a secreted recombinant antibody fragment that control production level and localization in Escherichia coli. J. Biol. Chem. 272:1997;12430-12436.
10. Ge, L., Knappik, A., Pack, P., Freund, C. & Plückthun, A.1995. Expressing antibodies in Escherichia coli. In Antibody Engineering (Borrebaeck, C. A. K., ed.), 2nd edit., pp. 229-266, Oxford University Press, Oxford.
11. Gill S. C., von Hippel P. H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:1989;319-326.
12. Griffiths A. D., Duncan A. R. Strategies for selection of antibodies by phage display. Curr. Opin. Biotechnol. 9:1998;102-108.
13. Gu H., Yi Q., Bray S. T., Riddle D. S., Shiau A. K., Baker D. A phage display system for studying the sequence determinants of protein folding. Protein Sci. 4:1995;1108-1117.
14. Gupta K., Lee Y., Yin J. Extremo-phage: in vitro selection of tolerance to a hostile environment. J. Mol. Evol. 41:1995;113-114.
15. Herron J. N., Terry A. H., Johnston S., He X. M., Guddat L. W., Voss E. W. Jr, Edmundson A. B. High resolution structures of the 4-4-20 Fab-fluorescein complex in two solvent systems: effects of solvent on structure and antigen-binding affinity. Biophys. J. 67:1994;2167-2183.
16. Hoogenboom H. R., de Bruine A. P., Hufton S. E., Hoet R. M., Arends J. W., Roovers R. C. Antibody phage display technology and its applications. Immunotechnology. 4:1998;1-20.
17. Jackson J. R., Sathe G., Rosenberg M., Sweet R. In vitro antibody maturation. Improvement of a high affinity, neutralizing antibody against IL-1 beta. J. Immunol. 154:1995;3310-3319.
18. Jelesarov I., Bosshard H. R. Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition. J. Mol. Recogn. 12:1999;3-18.
19. Jung S., Plückthun A. Improving in vivo folding and stability of a single-chain Fv antibody fragment by loop grafting. Protein Eng. 10:1997;959-966.
20. Kipriyanov S. M., Moldenhauer G., Martin A. C., Kupriyanova O. A., Little M. Two amino acid mutations in an anti-human CD3 single chain Fv antibody fragment that affect the yield on bacterial secretion but not the affinity. Protein Eng. 10:1997;445-453.
21. Knappik A., Plückthun A. Engineered turns of a recombinant antibody improve its in vivo folding. Protein Eng. 8:1995;81-89.
22. Krebber A., Bornhauser S., Burmester J., Honegger A., Willuda J., Bosshard H. R., Plückthun A. Reliable cloning of functional antibody variable domains from hybridomas and spleen cell repertoires employing a reengineered phage display system. J. Immunol. Methods. 201:1997;35-55.
23. Kristensen P., Winter G. Proteolytic selection for protein folding using filamentous bacteriophages. Fold. Des. 3:1998;321-328.
24. Langedijk A. C., Honegger A., Maat J., Planta R. J., van Schaik R. C., Plückthun A. The nature of antibody heavy chain residue H6 strongly influences the stability of a VH domain lacking the disulfide bridge. J. Mol. Biol. 283:1998;95-110.
25. Lindner P., Bauer K., Krebber A., Nieba L., Kremmer E., Krebber C., Honegger A., Klinger B., Mocikat R., Plückthun A. Specific detection of his-tagged proteins with recombinant anti-His tag scFv-phosphatase or scFv-phage fusions. Biotechniques. 22:1997;140-149.
26. Nieba L., Honegger A., Krebber C., Plückthun A. Disrupting the hydrophobic patches at the antibody variable/constant domain interface: improved in vivo folding and physical characterization of an engineered scFv fragment. Protein Eng. 10:1997;435-444.
27. Ohage E. C., Graml W., Walter M. M., Steinbacher S., Steipe B. Beta-turn propensities as paradigms for the analysis of structural motifs to engineer protein stability. Protein Sci. 6:1997;233-241.
28. Pace C. N. Measuring and increasing protein stability. Trends Biotechnol. 8:1990;93-98.
29. Pedrazzi G., Schwesinger F., Honegger A., Krebber C., Plückthun A. Affinity and folding properties both influence the selection of antibodies with the selectively infective phage (SIP) methodology. FEBS Letters. 415:1997;289-293.
30. Plotnikov V. V., Brandts J. M., Lin L. N., Brandts J. F. A new ultrasensitive scanning calorimeter. Anal. Biochem. 250:1997;237-244.
31. Plückthun A., Krebber A., Krebber C., Horn U., Knüpfer U., Wenderoth R., Nieba L., Proba K., Riesenberg D. Producing antibodies in Escherichia coli: from PCR to fermentation. McCafferty J., Hoogenboom H. R., Chiswell D. J. Antibody Engineering. 1996;203-252 IRL Press, Oxford.
32. Proba K., Wörn A., Honegger A., Plückthun A. Antibody scFv fragments without disulfide bonds made by molecular evolution. J. Mol. Biol. 275:1998;245-253.
33. 2 fragment for improved binding to T cells. Int. J. Cancer Suppl. 7:1992;45-50.
34. Ruan B., Hoskins J., Wang L., Bryan P. N. Stabilizing the subtilisin BPN' pro-domain by phage display selection: how restrictive is the amino acid code for maximum protein stability? Protein Sci. 7:1998;2345-2353.
35. Saul F. A., Poljak R. J. Structural patterns at residue positions 9, 18, 67 and 82 in the VH framework regions of human and murine immunoglobulins. J. Mol. Biol. 230:1993;15-20.
36. Sieber V., Plückthun A., Schmid F. X. Selecting proteins with improved stability by a phage-based method. Nature Biotechnol. 16:1998;955-960.
37. Starovasnik M. A., Braisted A. C., Wells J. A. Structural mimicry of a native protein by a minimized binding domain. Proc. Natl Acad. Sci. USA. 94:1997;10080-10085.
38. Stemmer W. P. DNA shuffling by random fragmentation and reassembly: in vitro recombination for molecular evolution. Proc. Natl Acad. Sci. USA. 91:1994a;10747-10751.
39. Stemmer W. P. Rapid evolution of a protein in vitro by DNA shuffling. Nature. 370:1994b;389-391.
40. Tang Y., Jiang N., Parakh C., Hilvert D. Selection of linkers for a catalytic single-chain antibody using phage display technology. J. Biol. Chem. 271:1996;15682-15686.
41. Vaughan T. J., Osbourn J. K., Tempest P. R. Human antibodies by design. Nature Biotechnol. 16:1998;535-539.
42. Weber-Bornhauser S., Eggenberger J., Jelesarov I., Bernard A., Berger C., Bosshard H. R. Thermodynamics and kinetics of the reaction of a single-chain antibody fragment (scFv) with the leucine zipper domain of transcription factor GCN4. Biochemistry. 37:1998;13011-13020.
43. Whitlow M., Howard A. J., Wood J. F., Voss E. W. Jr, Hardman K. D. 1.85 Å structure of anti-fluorescein 4-4-20 Fab. Protein Eng. 8:1995;749-761.
44. Willuda J., Honegger A., Waibel R., Schubiger P. A., Stahel R., Zangemeister-Wittke U., Plückthun A. High thermal stability is essential for tumor targeting of antibody fragments: engineering of a humanized anti-EGP-2 (Ep-CAM) scFv fragment. Cancer Res. 1999.
45. Winter G., Griffiths A. D., Hawkins R. E., Hoogenboom H. R. Making antibodies by phage display technology. Annu. Rev. Immunol. 12:1994;433-455.
46. Wörn A., Plückthun A. Mutual stabilization of VL and VH in single-chain antibody fragments, investigated with mutants engineered for stability. Biochemistry. 37:1998;13120-13127.
47. Wörn A., Plückthun A. Different equilibrium stability behavior of scFv fragments: identification, classification and improvement by protein engineering. Biochemistry. 38:1999;8739-8750.
48. Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene. 33:1985;103-119.