Scalable high throughput selection from phage-displayed synthetic antibody libraries

Journal of Visualized Experiments

Volumn , Issue 95, 2015, Pages

  Miersch, Shane ^a,b   Li, Zhijian ^a,b   Hanna, Rachel ^a,b   McLaughlin, Megan E ^a,b   Hornsby, Michael ^a,c   Matsuguchi, Tet ^a,c   Paduch, Marcin ^a,d   Sääf, Annika ^a,d   Wells, Jim ^a,c   Koide, Shohei ^a,d   Kossiakoff, Anthony ^a,d   Sidhu, Sachdev S ^a,b  

^a The Recombinant Antibody Network   (United States)

^b UNIVERSITY OF TORONTO   (Canada)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d UNIVERSITY OF CHICAGO   (United States)

Author keywords

Amino Acids; And Nucleosides; And Proteins; Antibody selection; Bacteria; High throughput; Immunology; Issue 95; Life Sciences (General); Nucleic Acids; Nucleotides; Peptides; Phage display; Scalable methodology; Synthetic antibodies; Viruses

Indexed keywords

ANTIBODY; ANTIGEN; EPITOPE; PEPTIDE LIBRARY;

ANTIGEN ANTIBODY REACTION; ENZYME LINKED IMMUNOSORBENT ASSAY; HIGH THROUGHPUT SCREENING; HUMAN; IMMUNOASSAY; IMMUNOLOGY; PEPTIDE LIBRARY; PROCEDURES;

ANTIBODIES; ANTIGEN-ANTIBODY REACTIONS; ANTIGENS; ENZYME-LINKED IMMUNOSORBENT ASSAY; EPITOPES; HIGH-THROUGHPUT SCREENING ASSAYS; HUMANS; IMMUNOASSAY; PEPTIDE LIBRARY;

EID: 84921688431     PISSN: 1940087X     EISSN: None     Source Type: Journal    
DOI: 10.3791/51492     Document Type: Article

References (25)

1. Winter, G., Milstein, C. Man-made antibodies. Nature. 349, 293-299 (1991).
2. Miersch, S., Sidhu, S. S. Synthetic antibodies: concepts, potential and practical considerations. Methods.57, 486-498 (2012).
3. Schofield, D. J., et al. Application of phage display to high throughput antibody generation and characterization. Genome Biol. 8, R254(2007).
4. Hust, M., et al. A human scFv antibody generation pipeline for proteome research. J. Biotechnol. 152, 159-170 (2011).
5. Colwill, K., Graslund, S. A roadmap to generate renewable protein binders to the human proteome. Nat. Methods. 8, 551-558 (2011).
6. Mersmann, M., et al. Towards proteome scale antibody selections using phage display. Nat. Biotechnol.27, 118-128 (2010).
7. Pershad, K., et al. Generating a panel of highly specific antibodies to 20 human SH2 domains by phage display. Protein Eng. Des. Sel. 23, 279-288 (2010).
8. Turunen, L., Takkinen, K., Soderlund, H., Pulli, T. Automated panning and screening procedure on microplates for antibody generation from phage display libraries. J Biomol. Screen. 14, 282-293 (2009).
9. Hughes, R. A., Miklos, A. E., Ellington, A. D. Gene synthesis: methods and applications. Methods Enzymol.498, 277-309 (2011).
10. Boersma, Y. L., Pluckthun, A. DARPins and other repeat protein scaffolds: advances in engineering and applications. 22, 849-857 (2011).
11. Terpe, K. Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems. Appl. Microbiol. Biotechnol. 60, 523-533 (2003).
12. Lichty, J. J., Malecki, J. L., Agnew, H. D., Michelson-Horowitz, D. J., Tan, S. Comparison of affinity tags for protein purification. Protein Expr. Purif. 41, 98-105 (2005).
13. Fellouse, F. A., et al. High-throughput generation of synthetic antibodies from highly functional minimalist phage-displayed libraries. J. Mol. Biol. 373, 924-940 (2007).
14. Paduch, M., et al. Generating conformation-specific synthetic antibodies to trap proteins in selected functional states. Methods. 60, 3-14 (2013).
15. Studier, F. W. Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif.41, 207-234 (2005).
16. Huang, H., Sidhu, S. S. Studying binding specificities of peptide recognition modules by high-throughput phage display selections. Methods Mol. Biol. 781, 87-97 (2011).
17. McLaughlin, M. E., Sidhu, S. S. Engineering and analysis of peptide-recognition domain specificities by phage display and deep Sequencing. Methods Enzymol. 523, 327-349 (2013).
18. Bradford, M. M. 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 (1976).
19. den Engelsman, J., et al. Strategies for the assessment of protein aggregates in pharmaceutical biotech product development. Pharm. Res. 28, 920-933 (2011).
20. Lavinder, J. J., Hari, S. B., Sullivan, B. J., Magliery, T. J. High-throughput thermal scanning: a general, rapid dye-binding thermal shift screen for protein engineering. J. Am. Chem. Soc. 131, 3794-3795 (2009).
21. Fellouse, F. A., Sidhu, S. S. Making antibodies in bacteria. in Making and Using Antibodies: A Practical Handbook. Howard, G. C., MR, K. aser 151-172 CRC Press Boca Raton, Florida (2013).
22. Acton, T. B., et al. Preparation of protein samples for NMR structure, function, and small-molecule screening studies. Methods in Enzymology. 483, 23-47 (2011).
23. Mahon, C. M., et al. Comprehensive interrogation of a minimalist synthetic CDR-H3 library and its ability to generate antibodies with therapeutic potential. J. Mol. Biol. 425, 1712-1730 (2013).
24. Persson, H., et al. CDR-H3 diversity is not required for antigen recognition by synthetic antibodies. J. Mol. Biol. 425, 803-811 (2013).
25. Bradbury, A. R., Sidhu, S., Dubel, S., McCafferty, J. Beyond natural antibodies: the power of in vitro display technologies. Nat. Biotechnol. 29, 245-254 (2011).