Metabolic biotinylation of recombinant antibody by biotin ligase retained in the endoplasmic reticulum

Biomolecular Engineering

Volumn 24, Issue 3, 2007, Pages 283-291

  Barat, Bhaswati ^a   Wu, Anna M ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Biotin ligase; Biotinylation; BirA; Carcinoembryonic antigen; Diabody; Engineered antibodies

Indexed keywords

CELLS; DRUG INTERACTIONS; ESCHERICHIA COLI; MEDICAL APPLICATIONS; METABOLISM;

BIOTIN LIGASE; BIOTINYLATION; CARCINOEMBRYONIC ANTIGEN; ENDOPLASMIC RETICULUM; ENGINEERED ANTIBODIES; EUKARYOTIC CELLS;

ANTIBODIES;

AMINO ACID DERIVATIVE; BIOTIN; CARCINOEMBRYONIC ANTIBODY; CARCINOEMBRYONIC ANTIGEN; HYBRID PROTEIN; LIGASE; RECOMBINANT ANTIBODY; SECRETORY PROTEIN;

ANIMAL CELL; ARTICLE; BIOTINYLATION; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; ENZYME ENGINEERING; ENZYME RELEASE; ESCHERICHIA COLI; EUKARYOTIC CELL; NONHUMAN; PRIORITY JOURNAL; PROPIONIBACTERIUM FREUDENREICHII SHERMANII; PROTEIN EXPRESSION; PURIFICATION;

ANTIBODIES, MONOCLONAL; BIOTINYLATION; CARBON-NITROGEN LIGASES; ENDOPLASMIC RETICULUM; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; PROTEIN ENGINEERING; RECOMBINANT FUSION PROTEINS; REPRESSOR PROTEINS; TRANSCRIPTION FACTORS;

ESCHERICHIA COLI; EUKARYOTA; PROPIONIBACTERIUM FREUDENREICHII SUBSP. SHERMANII;

EID: 34548485309     PISSN: 13890344     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bioeng.2007.02.003     Document Type: Article

References (50)

1. Altman J.D., Moss P.A., Goulder P.J., Barouch D.H., McHeyzer-Williams M.G., Bell J.I., McMichael A.J., and Davis M.M. Phenotypic analysis of antigen-specific T lymphocytes. Science 274 (1996) 94-96
2. Arnold G.S., Sasser A.K., Stachler M.D., and Bartlett J.S. Metabolic biotinylation provides a unique platform for the purification and targeting of multiple AAV vector serotypes. Mol. Ther. 14 (2006) 97-106
3. Asai T., Trinh R., Ng P.P., Penichet M.L., Wims L.A., and Morrison S.L. A human biotin acceptor domain allows site-specific conjugation of an enzyme to an antibody-avidin fusion protein for targeted drug delivery. Biomol. Eng. 21 (2005) 145-155
4. Bayer E.A., and Wilchek M. Protein biotinylation. Methods Enzymol. 184 (1990) 138-160
5. Bebbington C.R., Renner G., Thomson S., King D., Abrams D., and Yarranton G.T. High-level expression of a recombinant antibody from myeloma cells using a glutamine synthetase gene as an amplifiable selectable marker. Biotechnology (NY) 10 (1992) 169-175
6. Beckett D., Kovaleva E., and Schatz P.J. A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation. Protein Sci. 8 (1999) 921-929
7. Beerli R.R., Wels W., and Hynes N.E. Autocrine inhibition of the epidermal growth factor receptor by intracellular expression of a single-chain antibody. Biochem. Biophys. Res. Commun. 204 (1994) 666-672
8. Beerli R.R., Wels W., and Hynes N.E. Intracellular expression of single chain antibodies reverts ErbB-2 transformation. J. Biol. Chem. 269 (1994) 23931-23936
9. Campos S.K., and Barry M.A. Rapid construction of capsid-modified adenoviral vectors through bacteriophage lambda Red recombination. Hum. Gene Ther. 15 (2004) 1125-1130
10. Carmichael J.A., Power B.E., Garrett T.P., Yazaki P.J., Shively J.E., Raubischek A.A., Wu A.M., and Hudson P.J. The crystal structure of an anti-CEA scFv diabody assembled from T84.66 scFvs in V(L)-to-V(H) orientation: implications for diabody flexibility. J. Mol. Biol. 326 (2003) 341-351
11. Chapman-Smith A., and Cronan Jr. J.E. In vivo enzymatic protein biotinylation. Biomol. Eng. 16 (1999) 119-125
12. Cronan Jr. J.E. Biotination of proteins in vivo. A post-translational modification to label, purify, and study proteins. J. Biol. Chem. 265 (1990) 10327-10333
13. Cull M.G., and Schatz P.J. Biotinylation of proteins in vivo and in vitro using small peptide tags. Methods Enzymol. 326 (2000) 430-440
14. de Boer E., Rodriguez P., Bonte E., Krijgsveld J., Katsantoni E., Heck A., Grosveld F., and Strouboulis J. Efficient biotinylation and single-step purification of tagged transcription factors in mammalian cells and transgenic mice. Proc. Natl. Acad. Sci. U.S.A. 100 (2003) 7480-7485
15. Diamandis E.P., and Christopoulos T.K. The biotin-(strept)avidin system: principles and applications in biotechnology. Clin. Chem. 37 (1991) 625-636
16. Galfre G., and Milstein C. Preparation of monoclonal antibodies: strategies and procedures. Methods Enzymol. 73 (1981) 3-46
17. Holliger P., Prospero T., and Winter G. "Diabodies": small bivalent and bispecific antibody fragments. Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 6444-6448
18. Hu S., Shively L., Raubitschek A., Sherman M., Williams L.E., Wong J.Y., Shively J.E., and Wu A.M. Minibody: a novel engineered anti-carcinoembryonic antigen antibody fragment (single-chain Fv-CH3) which exhibits rapid, high-level targeting of xenografts. Cancer Res. 56 (1996) 3055-3061
19. Kenanova V., Olafsen T., Crow D.M., Sundaresan G., Subbarayan M., Carter N.H., Ikle D.N., Yazaki P.J., Chatziioannou A.F., Gambhir S.S., et al. Tailoring the pharmacokinetics and positron emission tomography imaging properties of anti-carcinoembryonic antigen single-chain Fv-Fc antibody fragments. Cancer Res. 65 (2005) 622-631
20. Kojima N., Matsuo T., and Sakai Y. Rapid hepatic cell attachment onto biodegradable polymer surfaces without toxicity using an avidin-biotin binding system. Biomaterials 27 (2006) 4904-4910
21. Krepkiy D., Wong K., Gawrisch K., and Yeliseev A. Bacterial expression of functional, biotinylated peripheral cannabinoid receptor CB2. Protein Expres. Purif. 49 (2006) 60-70
22. Kumar A., and Snyder M. Protein complexes take the bait. Nature 415 (2002) 123-124
23. Munro S., and Pelham H.R. A C-terminal signal prevents secretion of luminal ER proteins. Cell 48 (1987) 899-907
24. Nesbeth D., Williams S.L., Chan L., Brain T., Slater N.K., Farzaneh F., and Darling D. Metabolic biotinylation of lentiviral pseudotypes for scalable paramagnetic microparticle-dependent manipulation. Mol. Ther. 13 (2006) 814-822
25. Neumaier M., Shively L., Chen F.S., Gaida F.J., Ilgen C., Paxton R.J., Shively J.E., and Riggs A.D. Cloning of the genes for T84.66, an antibody that has a high specificity and affinity for carcinoembryonic antigen, and expression of chimeric human/mouse T84.66 genes in myeloma and Chinese hamster ovary cells. Cancer Res. 50 (1990) 2128-2134
26. Ohno K., Levin B., and Meruelo D. Cell-specific, multidrug delivery system using streptavidin-protein. A fusion protein. Biochem. Mol. Med. 58 (1996) 227-233
27. Olafsen T., Cheung C.W., Yazaki P.J., Li L., Sundaresan G., Gambhir S.S., Sherman M.A., Williams L.E., Shively J.E., Raubitschek A.A., et al. Covalent disulfide-linked anti-CEA diabody allows site-specific conjugation and radiolabeling for tumor targeting applications. Protein Eng. Des. Sel. 17 (2004) 21-27
28. Parrott M.B., and Barry M.A. Metabolic biotinylation of recombinant proteins in mammalian cells and in mice. Mol. Ther. 1 (2000) 96-104
29. Parrott M.B., and Barry M.A. Metabolic biotinylation of secreted and cell surface proteins from mammalian cells. Biochem. Biophys. Res. Commun. 281 (2001) 993-1000
30. Parrott M.B., Adams K.E., Mercier G.T., Mok H., Campos S.K., and Barry M.A. Metabolically biotinylated adenovirus for cell targeting, ligand screening, and vector purification. Mol. Ther. 8 (2003) 688-700
31. Parthasarathy R., Bajaj J., and Boder E.T. An immobilized biotin ligase: surface display of Escherichia coli BirA on Saccharomyces cerevisiae. Biotechnol. Prog. 21 (2005) 1627-1631
32. Reddy D.V., Rothemund S., Shenoy B.C., Carey P.R., and Sonnichsen F.D. Structural characterization of the entire 1.3S subunit of transcarboxylase from Propionibacterium shermanii. Protein Sci. 7 (1998) 2156-2163
33. Saviranta P., Haavisto T., Rappu P., Karp M., and Lovgren T. In vitro enzymatic biotinylation of recombinant fab fragments through a peptide acceptor tail. Bioconjug. Chem. 9 (1998) 725-735
34. Schatz P.J. Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: a 13 residue consensus peptide specifies biotinylation in Escherichia coli. Biotechnology (NY) 11 (1993) 1138-1143
35. Smith P.A., Tripp B.C., DiBlasio-Smith E.A., Lu Z., LaVallie E.R., and McCoy J.M. A plasmid expression system for quantitative in vivo biotinylation of thioredoxin fusion proteins in Escherichia coli. Nucleic Acids Res. 26 (1998) 1414-1420
36. Smith J.S., Keller J.R., Lohrey N.C., McCauslin C.S., Ortiz M., Cowan K., and Spence S.E. Redirected infection of directly biotinylated recombinant adenovirus vectors through cell surface receptors and antigens. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 8855-8860
37. Tannous B.A., Grimm J., Perry K.F., Chen J.W., Weissleder R., and Breakefield X.O. Metabolic biotinylation of cell surface receptors for in vivo imaging. Nat. Methods 3 (2006) 391-396
38. Tatsumi H., Fukuda S., Kikuchi M., and Koyama Y. Construction of biotinylated firefly luciferases using biotin acceptor peptides. Anal. Biochem. 243 (1996) 176-180
39. Tirat A., Freuler F., Stettler T., Mayr L.M., and Leder L. Evaluation of two novel tag-based labelling technologies for site-specific modification of proteins. Int. J. Biol. Macromol. 39 (2006) 66-76
40. Tsao K.L., DeBarbieri B., Michel H., and Waugh D.S. A versatile plasmid expression vector for the production of biotinylated proteins by site-specific, enzymatic modification in Escherichia coli. Gene 169 (1996) 59-64
41. Verhaegen M., and Christopoulos T.K. Bacterial expression of in vivo-biotinylated aequorin for direct application to bioluminometric hybridization assays. Anal. Biochem. 306 (2002) 314-322
42. Verhaegent M., and Christopoulos T.K. Recombinant Gaussia luciferase. Overexpression, purification, and analytical application of a bioluminescent reporter for DNA hybridisation. Anal. Chem. 74 (2002) 4378-4385
43. Viens A., Mechold U., Lehrmann H., Harel-Bellan A., and Ogryzko V. Use of protein biotinylation in vivo for chromatin immunoprecipitation. Anal. Biochem. 325 (2004) 68-76
44. Warren D.J., Bjerner J., Paus E., Bormer O.P., and Nustad K. Use of an in vivo biotinylated single-chain antibody as capture reagent in an immunometric assay to decrease the incidence of interference from heterophilic antibodies. Clin. Chem. 51 (2005) 830-838
45. Wood H.G., and Barden R.E. Biotin enzymes. Annu. Rev. Biochem. Allied Res. India 46 (1997) 385-413
46. Wu A.M., Williams L.E., Zieran L., Padma A., Sherman M., Bebb G.G., Odom-Maryon T., Wang J.Y.C., Shively J.E., and Raubitschek A.A. Anti-carcinoembryonic antigen (CEA) diabody for rapid tumor targeting and imaging. Tumor Target. 4 (1999) 47-58
47. Wu S.C., Yeung J.C., Hwang P.M., and Wong S.L. Design, production, and characterization of an engineered biotin ligase (BirA) and its application for affinity purification of staphylokinase produced from Bacillus subtilis via secretion. Protein Expres. Purif. 24 (2002) 357-365
48. Yang J., Jaramillo A., Shi R., Kwok W.W., and Mohanakumar T. In vivo biotinylation of the major histocompatibility complex (MHC) class II/peptide complex by coexpression of BirA enzyme for the generation of MHC class II/tetramers. Hum. Immunol. 65 (2004) 692-699
49. Yazaki P.J., and Wu A.M. Construction and characterization of minibodies for imaging and therapy of colorectal carcinomas. Methods Mol. Biol. 207 (2003) 351-364
50. Yazaki P.J., Shively L., Clark C., Cheung C.W., Le W., Szpikowska B., Shively J.E., Raubitschek A.A., and Wu A.M. Mammalian expression and hollow fiber bioreactor production of recombinant anti-CEA diabody and minibody for clinical applications. J. Immunol. Methods 253 (2001) 195-208