An automated robotic platform for rapid profiling oligosaccharide analysis of monoclonal antibodies directly from cell culture

Analytical Biochemistry

Volumn 442, Issue 1, 2013, Pages 10-18

  Doherty, Margaret ^a   Bones, Jonathan ^a   McLoughlin, Niaobh ^a   Telford, Jayne E ^a   Harmon, Bryan ^b   DeFelippis, Michael R ^b   Rudd, Pauline M ^a  

^a NATIONAL INSTITUTE FOR BIOPROCESSING RESEARCH AND TRAINING   (Ireland)

^b ELI LILLY AND COMPANY   (United States)

Author keywords

Automation; Cell culture media; Glycomics; Monoclonal antibodies; Oligosaccharides; Ultra performance liquid chromatography

Indexed keywords

AUTOMATION; CAPILLARY ELECTROPHORESIS; CELL CULTURE; LIQUID CHROMATOGRAPHY; LIQUIDS; MASS SPECTROMETRY; MONOCLONAL ANTIBODIES; OLIGOSACCHARIDES; POLYSACCHARIDES; PURIFICATION; ROBOTICS;

BIOPROCESS DEVELOPMENT; CELL CULTURE MEDIA; GLYCOMICS; INNATE IMMUNE SYSTEMS; MONOCLONAL ANTIBODIES (MAB); PROCESS ANALYTICAL TECHNOLOGY; THERAPEUTIC ANTIBODIES; ULTRA PERFORMANCE LIQUID CHROMATOGRAPHY;

QUALITY CONTROL;

FC RECEPTOR; FLUORESCENT DYE; GLYCAN; MONOCLONAL ANTIBODY; OLIGOSACCHARIDE; CULTURE MEDIUM;

ALKYLATION; ANIMAL CELL; ARTICLE; AUTOMATION; BIOREACTOR; CAPILLARY ELECTROPHORESIS; CELL CULTURE; DEGLYCOSYLATION; INNATE IMMUNITY; LABORATORY AUTOMATION; LIQUID; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PURIFICATION; ROBOTICS; TECHNOLOGY; ULTRA PERFORMANCE LIQUID CHROMATOGRAPHY; CHEMICAL STRUCTURE; CHEMISTRY; CULTURE MEDIUM; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HIGH THROUGHPUT SCREENING; HUMAN;

ANTIBODIES, MONOCLONAL; AUTOMATION; CELLS, CULTURED; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CULTURE MEDIA; HIGH-THROUGHPUT SCREENING ASSAYS; HUMANS; MODELS, MOLECULAR; OLIGOSACCHARIDES; ROBOTICS;

EID: 84885636807     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2013.07.005     Document Type: Article

References (37)

1. R.O. Duthaler, B. Ernst, R. Fischer, A.G. Katopodis, W. Kinzy, W. Marterer, R. Oehrlein, M.B. Streiff, G. Thoma, In vivo neutralization of naturally existing antibodies against linear a(1,3)-galactosidic carbohydrate epitopes by multivalent antigen presentation: a solution for the first hurdle of pig-Tohuman xenotransplantation, Chimia (Aarau) 64 (2010) 23-28.
2. R.R. Porter, The structure of antibodies: the basic pattern of the principal class of molecules that neutralize antigens (foreign substances in the body) is four cross-linked chains: this pattern is modified so that antibodies can fit different antigens, Sci. Am. 217 (1967) 81-87. passim.
3. J.J. van Bueren, T. Rispens, S. Verploegen, T. van der Palen-Merkus, S. Stapel, L.J. Workman, H. James, P.H. van Berkel, J.G. van de Winkel, T.A. Platts-Mills, P.W. Parren, Anti-galactose-A-1,3-galactose IgE from allergic patients does not bind a-galactosylated glycans on intact therapeutic antibody Fc domains, Nat. Biotechnol. 29 (2011) 574-576.
4. R. Jefferis, Antibody therapeutics: isotype and glycoform selection, Expert Opin. Biol. Ther. 7 (2007) 1401-1413. (Pubitemid 47475656)
5. R. Jefferis, Recombinant antibody therapeutics: the impact of glycosylation on mechanisms of action, Trends Pharmacol. Sci. 30 (2009) 356-362.
6. C.H. Chung, B. Mirakhur, E. Chan, Q.T. Le, J. Berlin, M. Morse, B.A. Murphy, S.M. Satinover, J. Hosen, D. Mauro, R.J. Slebos, Q. Zhou, D. Gold, T. Hatley, D.J. Hicklin, T.A. Platts-Mills, Cetuximab-induced anaphylaxis and IgE specific for galactose-A-1,3-galactose, N. Engl. J. Med. 358 (2008) 1109-1117. (Pubitemid 351398485)
7. V. Restelli, M.D. Wang, N. Huzel, M. Ethier, H. Perreault, M. Butler, The effect of dissolved oxygen on the production and the glycosylation profile of recombinant human erythropoietin produced from CHO cells, Biotechnol. Bioeng. 94 (2006) 481-494.
8. E. Trummer, K. Fauland, S. Seidinger, K. Schriebl, C. Lattenmayer, R. Kunert, K. Vorauer-Uhl, R. Weik, N. Borth, H. Katinger, D. Muller, Process parameter shifting: I. Effect of DOT, pH, and temperature on the performance of Epo-Fc expressing CHO cells cultivated in controlled batch bioreactors, Biotechnol. Bioeng. 94 (2006) 1033-1044. (Pubitemid 44221048)
9. N.S. Wong, L. Wati, P.M. Nissom, H.T. Feng, M.M. Lee, M.G. Yap, An investigation of intracellular glycosylation activities in CHO cells: effects of nucleotide sugar precursor feeding, Biotechnol. Bioeng. 107 (2010) 321-336.
10. J. Rodriguez, M. Spearman, T. Tharmalingam, K. Sunley, C. Lodewyks, N. Huzel, M. Butler, High productivity of human recombinant b-interferon from a lowtemperature perfusion culture, J. Biotechnol. 150 (2010) 509-518.
11. E. Trummer, K. Fauland, S. Seidinger, K. Schriebl, C. Lattenmayer, R. Kunert, K. Vorauer-Uhl, R. Weik, N. Borth, H. Katinger, D. Muller, Process parameter shifting: II. Biphasic cultivation-A tool for enhancing the volumetric productivity of batch processes using Epo-Fc expressing CHO cells, Biotechnol. Bioeng. 94 (2006) 1045-1052. (Pubitemid 44221049)
12. G. Walsh, R. Jefferis, Post-Translational modifications in the context of therapeutic proteins, Nat. Biotechnol. 24 (2006) 1241-1252. (Pubitemid 44564769)
13. B.R. Hirsch, G.H. Lyman, Biosimilars: are they ready for primetime in the United States?, J Natl. Compr. Cancer Network 9 (2011) 934-943.
14. H.I. Miller, Why an abbreviated FDA pathway for biosimilars is overhyped, Nat. Biotechnol. 29 (2011) 794-795.
15. G. Dranitsaris, E. Amir, K. Dorward, Biosimilars of biological drug therapies: regulatory, clinical, and commercial considerations, Drugs 71 (2011) 1527-1536.
16. M.A. Bynum, H. Yin, K. Felts, Y.M. Lee, C.R. Monell, K. Killeen, Characterization of IgG N-glycans employing a microfluidic chip that integrates glycan cleavage, sample purification, LC separation, and MS detection, Anal. Chem. 81 (2009) 8818-8825.
17. L.R. Ruhaak, R. Hennig, C. Huhn, M. Borowiak, R.J. Dolhain, A.M. Deelder, E. Rapp, M. Wuhrer, Optimized workflow for preparation of APTS-labeled Nglycans allowing high-Throughput analysis of human plasma glycomes using 48-channel multiplexed CGE-LIF, J. Proteome Res. 9 (2010) 6655-6664.
18. Z. Szabo, A. Guttman, T. Rejtar, B.L. Karger, Improved sample preparation method for glycan analysis of glycoproteins by CE-LIF and CE-MS, Electrophoresis 31 (2010) 1389-1395.
19. D. Reusch, M. Haberger, M.H. Selman, P. Bulau, A.M. Deelder, M. Wuhrer, N. Engler, High-Throughput work flow for IgG Fc-glycosylation analysis of biotechnological samples, Anal. Biochem. 432 (2013) 82-89.
20. L. Royle, M.P. Campbell, C.M. Radcliffe, D.M. White, D.J. Harvey, J.L. Abrahams, Y.-G. Kim, G.W. Henry, N.A. Shadick, M.E. Weinblatt, D.M. Lee, P.M. Rudd, R.A. Dwek, HPLC-based analysis of serum N-glycans on a 96-well plate platform with dedicated database software, Anal. Biochem. 376 (2008) 1-12.
21. L. Royle, C.M. Radcliffe, R.A. Dwek, P.M. Rudd, Detailed structural analysis of Nglycans released from glycoproteins in SDS-PAGE gel bands using HPLC combined with exoglycosidase array digestions, Methods Mol. Biol. 347 (2006) 125-143.
22. M.P. Campbell, L. Royle, C.M. Radcliffe, R.A. Dwek, P.M. Rudd, GlycoBase and autoGU: tools for HPLC-based glycan analysis, Bioinformatics 24 (2008) 1214-1216. (Pubitemid 351594175)
23. D.J. Harvey, A.H. Merry, L. Royle, M.P. Campbell, R.A. Dwek, P.M. Rudd, Proposal for a standard system for drawing structural diagrams of N-And O-linked carbohydrates and related compounds, Proteomics 9 (2009) 3796-3801.
24. M.E. Dilorenzo, C. Timoney, R.A. Felder, Technological advancements in liquid handling robotics, J. Lab. Autom. 6 (2001) 36-40.
25. R. Jefferis, Glycosylation of recombinant antibody therapeutics, Biotechnol. Prog. 21 (2005) 11-16. (Pubitemid 40218466)
26. B. Huang, F.F. Liu, X.Y. Dong, Y. Sun, Molecular mechanism of the affinity interactions between protein A and human immunoglobulin G1 revealed by molecular simulations, J. Phys. Chem. B 115 (2011) 4168-4176.
27. A.K. Palm, M.V. Novotny, A monolithic PNGase F enzyme microreactor enabling glycan mass mapping of glycoproteins by mass spectrometry, Rapid Commun. Mass Spectrom. 19 (2005) 1730-1738. (Pubitemid 40831956)
28. J. Krenkova, N.A. Lacher, F. Svec, Multidimensional system enabling deglycosylation of proteins using a capillary reactor with peptide-Nglycosidase F immobilized on a porous polymer monolith and hydrophilic interaction liquid chromatography-mass spectrometry of glycans, J. Chromatogr. A 1216 (2009) 3252-3259.
29. W.N. Sandoval, V. Pham, E.S. Ingle, P.S. Liu, J.R. Lill, Applications of microwaveassisted proteomics in biotechnology, Comb. Chem. High Throughput Screening 10 (2007) 751-765.
30. L.R. Ruhaak, C. Huhn, W.J. Waterreus, A.R. de Boer, C. Neususs, C.H. Hokke, A.M. Deelder, M. Wuhrer, Hydrophilic interaction chromatography-based highthroughput sample preparation method for N-glycan analysis from total human plasma glycoproteins, Anal. Chem. 80 (2008) 6119-6126.
31. M.H. Selman, M. Hemayatkar, A.M. Deelder, M. Wuhrer, Cotton HILIC SPE microtips for microscale purification and enrichment of glycans and glycopeptides, Anal. Chem. 83 (2011) 2492-2499.
32. J.C. Bigge, T.P. Patel, J.A. Bruce, P.N. Goulding, S.M. Charles, R.B. Parekh, Nonselective and efficient fluorescent labeling of glycans using 2-Amino benzamide and anthranilic acid, Anal. Biochem. 230 (1995) 229-238.
33. M. Olajos, P. Hajos, G.K. Bonn, A. Guttman, Sample preparation for the analysis of complex carbohydrates by multicapillary gel electrophoresis with lightemitting diode induced fluorescence detection, Anal. Chem. 80 (2008) 4241-4246. (Pubitemid 351812782)
34. L. Novakova, L. Matysova, P. Solich, Advantages of application of UPLC in pharmaceutical analysis, Talanta 68 (2006) 908-918. (Pubitemid 43052506)
35. J. Bones, S. Mittermayr, N. O'Donoghue, A. Guttman, P.M. Rudd, Ultra performance liquid chromatographic profiling of serum N-glycans for fast and efficient identification of cancer associated alterations in glycosylation, Anal. Chem. 82 (2010) 10208-10215.
36. S. Mittermayr, J. Bones, M. Doherty, A. Guttman, P.M. Rudd, Multiplexed analytical glycomics: rapid and confident IgG N-glycan structural elucidation, J. Proteome Res. 10 (2011) 3820-3829.
37. J. Deisenhofer, Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9-And 2.8-A resolution, Biochemistry 20 (1981) 2361-2370. (Pubitemid 11089772)