Improved expression characteristics of single-chain Fv fragments when fused downstream of the Escherichia coli maltose-binding protein or upstream of a single immunoglobulin-constant domain

Protein Expression and Purification

Volumn 18, Issue 1, 2000, Pages 1-10

  Hayhurst, Andrew ^a  

^a UNIVERSITY OF ABERDEEN   (United Kingdom)

Author keywords

Atrazine; Maltose binding protein; Protein solubility; Single chain antibody fragment; Translocation

Indexed keywords

ANTIBODY SPECIFICITY; CELL FRACTIONATION; CELL GROWTH; CYTOPLASM; ENZYME LINKED IMMUNOSORBENT ASSAY; ESCHERICHIA; GENE FUSION; MALTOSE BINDING PROTEIN; PROTEIN EXPRESSION; SINGLE CHAIN ANTIBODY FRAGMENT; SOLUBILITY;

ESCHERICHIA COLI;

EID: 0034142296     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1999.1164     Document Type: Article

References (51)

1. Knappik A., Krebber C., Plückthun A. The effect of folding catalysts on the in vivo folding process of different antibody fragments expressed in Escherichia coli. Biotechnology. 11:1993;77-83.
2. Nieba L., Honeggar A., Krebber C., Plückthun A. Disrupting the hydrophobic patches at the antibody variable/constant domain interface improves in vivo folding and physical characterization of an engineered scFv fragment. Protein Eng. 10:1997;435-444.
3. Somerville J. E. Jr., Goshorn S. C., Fell H. P., Darveau R. P. Bacterial aspects associated with the expression of single-chain antibody fragments in Escherichia coli. Appl. Microbiol. Biotechnol. 42:1994;595-603.
4. Plückthun A., Krebber A., Krebber C., Horn U., Knupfer U., Wenderoth R., Nieba L., Proba K., Riesenberg D. McCafferty J. Antibody Engineering: A Practical Approach. 1996;203-252 IRL Press, Oxford.
5. Kipriyanov S. M., Moldenhauer G., Little M. High level production of soluble single chain antibodies in small scale Escherichia coli cultures. J. Immunol. Methods. 200:1997;69-77.
6. Knappik A., Plückthun A. Engineering turns of a recombinant antibody improves its in vivo folding. Protein Eng. 8:1995;81-89.
7. 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.
8. Kipriyanov S. M., Moldenhauer G., Martin A. C. R., Kipriyanov 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.
9. 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.
10. Graham B., Porter A. J., Harris W. J. Cloning, expression and characterization of a single-chain antibody fragment to the herbicide paraquat. J. Chem. Technol. Biotechnol. 63:1995;279-289.
11. Byrne F. R., Grant S. D., Porter A. J., Harris W. J. Cloning expression and characterization of a single chain antibody specific for the herbicide atrazine. Food Agric. Immunol. 8:1996;19-29.
12. Learmonth D. Cloning and Expression of Herbicide-Specific Single-Chain Antibody Fragments in Escherichia coli and Nicotiana tabacum. 1997;Univ. Aberdeen, Scotland.
13. Grant S. D. Construction and Expression in Escherichia coli of Novel Single Chain Antibody Fragments against the Herbicide Atrazine. 1997;Univ. Aberdeen, Scotland.
14. Bothmann H., Plückthun A. Selection for a periplasmic factor improving phage display and functional periplasmic expression. Nature Biotechnol. 16:1998;376-380.
15. Hayhurst A., Harris W. J. Escherichia coli Skp chaperone coexpression improves solubility and phage display of single chain antibody fragments. Protein Expression Purif. 14:1999;336-343.
16. Tudyka T., Skerra A. Glutathione-S transferase can be used as a C-terminal, enzymatically active dimerization module for a recombinant protease inhibitor, and functionally secreted into the periplasm of Escherichia coli. Protein Sci. 6:1997;2180-2187.
17. Guan C., Li P., Riggs P. D., Inouye H. Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose binding protein. Gene. 67:1998;21-30.
18. Wang C., Castro F. A., Wilkes D. M., Altenberg G. A. Expression and purification of the first nucleotide-binding domain and linker region of human multidrug resistance gene product: Comparison of fusions to glutathione S-transferase, thioredoxin and maltose-binding protein. Biochem. J. 338:1999;77-81.
19. Kapust R. B., Waugh D. S. Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci. 8:1999;1668-1674.
20. Malinowski D. P., Gourley M., Edelstein S., Pearson R. E. Expression of a Chlamydia anticarbohydrate single-chain antibody as a maltose binding fusion protein. Cell Biophys. 21:1992;1-12.
21. Brégégère F., Schwartz J., Bedouelle H. Bifunctional hybrids between the variable domains of an immunoglobulin and the maltose binding protein of Escherichia coli: Production, purification and antigen binding. Protein Eng. 7:1994;271-280.
22. Chames P., Fieschi J., Baty D. Production of a soluble and active MBP-scFv fusion: Favourable effect of the leaky tolR strain. FEBS Lett. 405:1997;224-228.
23. McGregor D. P., Molloy P. E., Cunningham C., Harris W. J. Spontaneous assembly of bivalent single chain antibody fragments in Escherichia coli. Mol. Immunol. 31:1994;219-226.
24. Grant S. D., Cupit P. M., Learmonth D., Byrne F. R., Graham B. M., Porter A. J., Harris W. J. Expression of monovalent and bivalent antibody fragments in Escherichia coli. J. Hematother. 4:1995;383-388.
25. Struhl K. A rapid method for creating recombinant DNA molecules. Biotechniques. 3:1985;452-543.
26. Sambrook J., Fritsch E. F., Maniatis T. Transfer of proteins from SDS-polyacrylamide gels to solid supports. Molecular Cloning: A Laboratory Manual. 1989;Cold Spring Harbor Laboratory Press, Cold Spring Harbor. p. 18.60-18.75.
27. Neu H. C., Heppel L. A. The release of enzymes from Escherichia coli by osmotic shock and during formation of sphaeroplasts. J. Biol. Chem. 240:1965;3685-3692.
28. Pages A-M., Anba J., Bernadac A., Shinagawa H., Nakata A., Lazdunski C. Normal precursors of periplasmic proteins accumulated in the cytoplasm are not exported post-translationally in Escherichia coli. Eur. J. Biochem. 143:1984;499-505.
29. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
30. Sachdev D., Chirgwin J. M. Order of fusions between bacterial and mammalian proteins can determine solubility in Escherichia coli. Biochem. Biophys. Res. Commun. 244:1998;933-937.
31. Richarme G., Caldas T. D. Chaperone properties of the bacterial periplasmic substrate-binding proteins. J. Biol. Chem. 272:1997;15607-15612.
32. Danese P. N., Silhavy T. J. Targeting and assembly of periplasmic and outer-membrane proteins in Escherichia coli. Annu. Rev. Genet. 32:1998;59-94.
33. Randall L. L., Hardy S. J. Correlation of competence for export with lack of tertiary structure of the mature species: a study in vivo of maltose binding protein of E. coli. Cell. 46:1986;921-928.
34. Randall L. L. Translocation of domains of nascent periplasmic proteins across the cytoplasmic membrane is independent of elongation. Cell. 33:1983;231-240.
35. Duplay P., Hoffnung M. Two regions of mature periplasmic maltose binding protein of Escherichia coli involved in secretion. Bacteriology. 170:1988;4445-4450.
36. Hardy S. J., Randall L. L. A kinetic partitioning model of selective binding of non-native proteins by the bacterial chaperone secB. Science. 251:1991;439-443.
37. Barkocy-Gallagher G. A., Cannon J. G., Bassford P. J. Jr. Thirty three amino acids of the mature moiety of an unprocessed maltose binding protein are sufficient for export in Escherichia coli. J. Bacteriol. 176:1994;3397-3399.
38. Kim J., Kendall D. A. Identification of a sequence motif that confers SecB dependence on a Sec-B independent secretory protein in vivo. J. Bacteriol. 180:1998;1396-1401.
39. Weiss J. B., Ray P. H., Bassford P. J. Jr. Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose binding protein in vitro. Proc. Natl. Acad. Sci. USA. 85:1988;8978-8982.
40. Collier D. N., Bankaitis V. A., Weiss J. B., Bassford P. J. Jr. The antifolding activity of secB promotes the export of the E. coli maltose binding protein. Cell. 22:1988;273-283.
41. Murén E. M., Suciu D., Topping T. B., Kumamoto C. A., Randall L. L. Mutational alterations in the homotetrameric chaperone secB that implicate the structure as dimer of dimers. J. Biol. Chem. 274:1999;19397-19402.
42. Lecker S. H., Driessen A. J. M., Wickner W. ProOmpA contains secondary and tertiary structure prior to translocation and is shielded from aggregation by association with secB protein. EMBO J. 9:1990;2309-2314.
43. MacKenzie R., To R. The role of valency in the selection of anti-carbohydrate single-chain Fvs from phage display libraries. J. Immunol. Methods. 220:1998;39-49.
44. Fekkes P., de Wit J. G., van der Wolk J. P., Kimsey H. H., Kumamoto C. A., Driessen A. J. Preprotein transfer to the Escherichia coli translocase requires the co-operative binding of SecB and the signal sequence to SecA. Mol. Microbiol. 29:1998;1179-1190.
45. Simmons L. C., Yansura D. G. Translational level is a critical factor for the secretion of heterologous proteins in Escherichia coli. Nature Biotechnol. 14:1996;629-634.
46. Nilsson B., Berman-Marks C., Kuntz I. D., Anderson S. Secretion incompetence of bovine pancreatic trypsin inhibitor expressed in Escherichia coli. J. Biol. Chem. 266:1991;2970-2977.
47. Chea K-C., Harrison S., King R., Crocker L., Wells J. R. E., Robins A. Secretion of eukaryotic growth hormones in Escherichia coli is influenced by the sequence of the mature proteins. Gene. 138:1994;9-15.
48. Monsalve R. I., Lu G., King T. P. Expressions of recombinant venom allergen, antigen 5 of yellowjacket (Vespula vulgaris) and paper wasp (Polistes annularis), in bacteria or yeast. Protein Expression Purif. 16:1999;410-416.
49. Hardesty B., Tsalkova T., Kramer G. Co-translational folding. Curr. Opin. Struct. Biol. 9:1999;111-114.
50. Wall J. G., Plückthun A. The hierarchy of mutations influencing the folding of antibody domains in Escherichia coli. Protein Eng. 12:1999;605-611.
51. Harris W. J. Exploiting antibody-based technologies to manage environmental pollution. Trends Biotechnol. 17:1999;290-296.