In vitro enzymatic biotinylation of recombinant Fab fragments through a peptide acceptor tail

Bioconjugate Chemistry

Volumn 9, Issue 6, 1998, Pages 725-735

  Saviranta, Petri ^a   Haavisto, Tapio ^a   Rappu, Pekka ^a   Karp, Matti ^a   Lövgren, Timo ^a  

^a UNIVERSITY OF TURKU   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO TERMINAL SEQUENCE; BIOTIN LIGASE; BIOTINYLATION; CARBOXY TERMINAL SEQUENCE; CHROMATOGRAPHY; ENZYME ACTIVITY; ESCHERICHIA COLI; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; RECOMBINANT PROTEIN;

AMINO ACIDS; ANTIGENS; BINDING ENERGY; ESCHERICHIA COLI; IMMUNOLOGY; PEPTIDES; PURIFICATION;

AMINO-ACIDS; BIOTINYLATIONS; C-TERMINUS; FAB' FRAGMENT; FUSION PROTEINS; GLUTATHIONE S-TRANSFERASES; IN-VITRO; LIGASES; PEPTIDE FUSION; SITE-SPECIFIC;

COENZYMES;

EID: 0032212036     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc9800217     Document Type: Article

References (36)

1. Athappilly, F. K., and Hendrickson, W. A. (1995) Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing. Structure 3, 1407-1419.
2. Barbas, C. F., III, Kang, A. S., Lerner, R. A., and Benkovic, S. J. (1991) Assembly of combinatorial antibody libraries on phage surfaces: the gene III site. Proc. Natl. Acad. Sci. U.S.A. 88, 7978-82.
3. Barker, D. F., and Campbell, A. M. (1981) Genetic and biochemical characterization of the birA gene and its product: evidence for a direct role of biotin holoenzyme synthetase in repression of the biotin operon in Escherichia coli. J. Mol. Biol. 146, 469-492.
4. Bayer, E. A., and Wilchek, M. (1990) Protein biotinylation. Methods Enzymol. 184, 138-166.
5. Benhar, I., Brinkmann, U., Webber, K. O., and Pastan, I. (1994) Mutations of two lysine residues in the CDR loops of a recombinant immunotoxin that reduce its sensitivity to chemical derivatization. Bioconjugate Chem. 4, 321-326.
6. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
7. Buoncristiani, M. R., and Otsuka, A. J. (1988) Overproduction and rapid purification of the biotin operon repressor from Escherichia coli. J. Biol. Chem. 263, 1013-1016.
8. Buoncristiani, M. R., Howard, P. K., and Otsuka, A. J. (1986) DNA-binding and enzymatic domains of the bifunctional biotin operon repressor (BirA) of Escherichia coli. Gene 44, 255-261.
9. Casadaban, M. J., and Cohen, S. N. (1980) Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J. Mol. Biol. 138, 179-207.
10. Chapman-Smith, A., Turner, D. L., Cronan, J. E., Jr., Morris, T. W., and Wallace, J. C. (1994) Expression, biotinylation and purification of a biotin-domain peptide from the biotin carboxy carrier protein of Escherichia coli acetyl-CoA carboxylase. Biochem. J. 302, 881-887.
11. Cronan, J. E., Jr. (1989) The E. coli bio operon: transcriptional repression by an essential protein modification enzyme. Cell 58, 427-429.
12. Cronan, J. E., Jr. (1990) Biotination of proteins in vivo. A posttranslational modification to label, purify and study proteins. J. Biol. Chem. 265, 10327-10333.
13. Diamandis, E. P., and Christopoulos, T. K. (1991) The Biotin-(strept)avidin system: principles and applications in biotechnology. Clin. Chem. 37, 625-636.
14. Hayden, M. S., Gilliland, L. K., and Ledbetter J. A. (1997) Antibody engineering. Curr. Opin. Immunol. 9, 201-212.
15. Hermanson, G. T. (1996) Bioconjugate techniques, Academic Press, Inc., San Diego, CA.
16. Jander, G., Cronan, J. E., and Beckwith, J. (1996) Biotinylation in vivo as a sensitive indicator of protein secretion and membrane protein insertion. J. Bacteriol. 178, 3049-3058.
17. Knappik, A., and Plückthun, A. (1995) Engineered turns of a recombinant antibody improve its in vivo folding. Protein Eng. 8, 81-89.
18. Li, S. J., and Cronan, J. E., Jr. (1992) The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase. J. Biol. Chem. 267, 855-863.
19. Lövgren, T., Heinonen, P., Lehtinen, P., Hakala, H., Heinola, J., Harju, R., Takalo, H., Mukkala, V. M., Schmid, R., Lönnberg, H., Pettersson, K., and Iitiä, A. (1997) Sensitive bioaffinity assays with individual microparticles and time-resolved fluorometry. Clin. Chem. 43, 1937-1943.
20. Mukkala, V.-M., Hänninen, E., and Hemmilä, I. (1993) Synthesis of two biotin isothiocyanate derivatives. Proceedings of 8th European Symposium on Organic Chemistry, p 422, Sitges, Spain.
21. Pajunen, M., Saviranta, P., Jauria, P., Karp, M., Pettersson, K., Mäntsalä, P., and Lövgren, T. (1997) Cloning, sequencing, expression, and characterization of three anti-estradiol-17β Fab fragments. Biochim. Biophys. Acta 1351, 192-202.
22. Plückthun, A., and Skerra, A. (1989) Expression of functional antibody Fv and Fab fragments in Escherichia coli. Methods Enzymol. 178, 497-515.
23. Rapley R. (1995) The biotechnology and applications of antibody engineering. Mol. Biotechnol. 3, 139-154.
24. Reed, K. E., and Cronan, J. E., Jr. (1991) Escherichia coli exports previously folded and biotinated protein domains. J. Biol. Chem. 266, 11425-11428.
25. Saviranta, P., Pajunen, M., Jauria, P., Karp, M., Pettersson, K., Mäntsalä, P., and Lövgren, T. (1998) Engineering the steroid-specificity of an anti-17β-estradiol Fab by random mutagenesis and competitive phage panning. Protein Eng. 11, 143-152.
26. Schatz, P. J. (1993) Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: A 13 amino acids concensus peptide specifies biotinylation in Escherichia coli. BioTechnology 11, 1138-1143.
27. Shenoy, B. C., and Wood, H. G. (1988) Purification and properties of the synthetase catalyzing the biotination of the aposubunit of transcarboxylase from Propionibacterium shermanii. FASEB J. 12, 2396-2401.
28. Smith, D. B., and Johnson, K. S. (1988) Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67, 31-40.
29. Tsao, K.-L., DeBarbieri, B., Michel, H., and Waugh, D. S. (1996) A versatile plasmid expression vector for the production of biotinylated proteins by site-specific, enzymatic modification in Escherichia coli. Gene 169, 59-64.
30. Vincent, P., and Samuel, D. (1993) A comparison of the binding of biotin and biotinylated macromolecular ligands to an anti-biotin monoclonal antibody and to streptavidin. J. Immunol. Methods 165, 177-182.
31. Weiss, E., Chatellier, J., and Orfanoudakis, G. (1994) In vivo biotinylated recombinant antibodies: Construction, characterization, and application of a bifunctional Fab-BCCP fusion protein produced in Escherichia coli. Protein Expression Purif. 5, 509-517.
32. Wilchek, M., and Bayer, E. A. (1990a) Introduction to avidin-biotin technology. Methods. Enzymol. 184, 5-13.
33. Wilchek, M., and Bayer, E. A. (1990b) Biotin-containing reagents. Methods Enzymol. 184, 123-138.
34. Wilson, K. P., Shewchuk, L. M., Brennan, R. G., Otsuka, A. J., and Matthews, B. W. (1992) Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. Proc. Natl. Acad. Sci. U.S.A. 89, 9257-9261.
35. Wood, H. G., Barden, R. E. (1977) Biotin enzymes. Annu. Rev. Biochem. 46, 385-413.
36. Xu, Y. And Beckett, D. (1996) Evidence for interdomain interaction in the Escherichia coli repressor of the biotin biosynthesis from studies of an N-terminal domain deletion mutant. Biochemistry 35, 1783-1792.