High-throughput analysis of intraclonal variability of glycoprotein sialylation

Biotechnology Progress

Volumn 28, Issue 2, 2012, Pages 591-594

  Markely, Lam Raga A ^a,b   Wang, Daniel I C ^b  

^a BIOGEN   (United States)

^b MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

Cell culture; Glycosylation; High throughput; Sialic acid

Indexed keywords

CELL CLONES; CELL LINES; CHINESE HAMSTER OVARY CELLS; CHO CELL; CONVENTIONAL METHODS; EXPERIMENTAL STUDIES; HIGH THROUGHPUT; HIGH-THROUGHPUT ANALYSIS; HIGH-THROUGHPUT METHOD; PROTEIN PURIFICATION; SIALIC ACIDS; SIALYLATION; SUBCLONES; THERAPEUTIC PROTEIN; TOTAL PROTEIN; TOTAL PROTEIN CONCENTRATION;

CARBOXYLIC ACIDS; CELL CULTURE; GLYCOSYLATION;

RECOMBINANT PROTEINS;

GLYCOPROTEIN; N ACETYLNEURAMINIC ACID; RECOMBINANT PROTEIN;

ANIMAL; ARTICLE; CHO CELL; EVALUATION; GENETICS; HAMSTER; HIGH THROUGHPUT SCREENING; METABOLISM; METHODOLOGY;

ANIMALS; CHO CELLS; CRICETINAE; GLYCOPROTEINS; HIGH-THROUGHPUT SCREENING ASSAYS; N-ACETYLNEURAMINIC ACID; RECOMBINANT PROTEINS;

CRICETULUS GRISEUS;

EID: 84859632710     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.738     Document Type: Article

References (37)

1. Jayapal KR, Wlaschin KF, Hu WS, Yap MGS. Recombinant protein therapeutics from CHO cells-20 years and counting. Chem Eng Prog. 2007; 103: 40-47.
2. Aggarwal S. What's fueling the biotech engine-2009-2010. Nat Biotechnol. 2010; 28: 1165-1171.
3. Walsh G. Biopharmaceutical benchmarks 2010. Nat Biotechnol. 2010; 28: 917-924.
4. Walsh G, Jefferis R. Post-translational modifications in the context of therapeutic proteins. Nat Biotechnol. 2006; 24: 1241-1252.
5. Butler M. Animal cell cultures: recent achievements and perspectives in the production of biopharmaceuticals. Appl Microbiol Biotechnol. 2005; 68: 283-291.
6. Seth G, Charaniya S, Wiaschin KF, Hu WS. In pursuit of a super producer-alternative paths to high producing recombinant mammalian cells. Curr Opin Biotechnol. 2007; 18: 557-564.
7. Pilbrough W, Munro TP, Gray P. Intraclonal protein expression heterogeneity in recombinant CHO cells. PLoS One. 2009; 4: e8432.
8. Kim NS, Kim SJ, Lee GM. Clonal variability within dihydrofolate reductase-mediated gene amplified Chinese hamster ovary cells: stability in the absence of selective pressure. Biotechnol Bioeng. 1998; 60: 679-688.
9. Park S, Kim W, Kim Y, Son YD, Lee SC, Kim E, Kim SH, Kim JH, Kim HS. Array-based analysis of secreted glycoproteins for rapid selection of a single cell producing a glycoprotein with desired glycosylation. Anal Chem. 2010; 82: 5830-5837.
10. Love JC, Ronan JL, Grotenbreg GM, van der Veen AG, Ploegh HL. A microengraving method for rapid selection of single cells producing antigen-specific antibodies. Nat Biotechnol. 2006; 24: 703-707.
11. Love KR, Panagiotou V, Jiang B, Stadheim TA, Love JC. Integrated single-cell analysis shows pichia pastoris secretes protein stochastically. Biotechnol Bioeng. 2010; 106: 319-325.
12. Panagiotou V, Love KR., Jiang B, Nett J, Stadheim T, Love JC. Generation and screening of Pichia pastoris Strains with enhanced protein production by use of microengraving. Appl Environ Microbiol. 2011; 77: 3154-3156.
13. Davis JM, Pennington JE, Kubler AM, Conscience JF. A simple, single-step technique for selecting and cloning hybridomas for the production of monoclonal-antibodies. J Immunol Methods. 1982; 50: 161-171.
14. Rueda AZ, Coll JM. Cloning of myelomas and hybridomas in fibrin clots. J Immunol Methods. 1988; 114: 213-217.
15. Herzenberg LA, Parks D, Sahaf B, Perez O, Roederer M, Herzenberg LA. The history and future of the fluorescence activated cell sorter and flow cytometry: a view from Stanford. Clin Chem. 2002; 48: 1819-1827.
16. Ngantung FA, Miller PG, Brushett FR, Tang GL, Wang DIC. RNA interference of sialidase improves glycoprotein sialic acid content consistency. Biotechnol Bioeng. 2006; 95: 106-119.
17. Kaneko Y, Nimmerjahn F, Ravetch EV. Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation. Science. 2006; 313: 670-673.
18. Sinclair AM, Elliott S. Glycoengineering: the effect of glycosylation on the properties of therapeutic proteins. J Pharm Sci. 2005; 94: 1626-1635.
19. Goldwasser E, Kung CKH, Eliason J. Mechanism of erythropoietin-induced differentiation .13. Role of sialic-acid in erythropoietin action. J Biol Chem. 1974; 249: 4202-4206.
20. Tsuda E, Kawanishi G, Ueda M, Masuda S, Sasaki R. The role of carbohydrate in recombinant human erythropoietin. Eur J Biochem. 1990; 188: 405-411.
21. Gopaul KP, Crook MA. Sialic acid: a novel marker of cardiovascular disease? Clin Biochem. 2006; 39: 667-681.
22. Markely LRA, Ong BT, Hoi KM, Teo G, Lu MY, Wang DIC. A high-throughput method for quantification of glycoprotein sialylation. Anal Biochem. 2010; 407: 128-133.
23. Ng SK, Wang DIC, Yap MGS. Application of destabilizing sequences on selection marker for improved recombinant protein productivity in CHO-DG44. Metabol Eng. 2007; 9: 304-316.
24. Wong NSC, Wati L, Nissom PM, Feng HT, Lee MM, Yap MGS. An investigation of intracellular glycosylation activities in CHO cells: effects of nucleotide sugar precursor feeding. Biotechnol Bioeng. 2010; 107: 321-336.
25. Wong DCF, Wong NSC, Goh JSY, May LM, Yap MGS. Profiling of N-glycosylation gene expression in CHO cell fed-batch cultures. Biotechnol Bioeng. 2010; 107: 516-528.
26. Wong NSC, Yap MGS, Wang DIC. Enhancing recombinant glycoprotein sialylation through CMP-sialic acid transporter over expression in chinese hamster ovary cells. Biotechnol Bioeng. 2006; 93: 1005-1016.
27. Clark KJR, Griffiths J, Bailey KM, Harcum SW. Gene-expression profiles for five key glycosylation genes for galactose-fed CHO cells expressing recombinant IL-4/13 cytokine trap. Biotechnol Bioeng. 2005; 90: 568-577.
28. Hossler P, Mulukutla BC, Hu W-S. Systems analysis of N-glycan processing in mammalian cells. PLoS One. 2007; 2: e713.
29. Umana P, Bailey JE. A mathematical model of N-linked glycoform biosynthesis. Biotechnol Bioeng. 1997; 55: 890-908.
30. Krambeck FJ, Betenbaugh MJ. A mathematical model of N-linked glycosylation. Biotechnol Bioeng. 2005; 92: 711-728.
31. Santell L, Ryll T, Etcheverry T, Santoris M, Dutina G, Wang A, Gunson J, Warner TG. Aberrant metabolic sialylation of recombinant proteins expressed in Chinese hamster ovary cells in high productivity cultures. Biochem Biophys Res Commun. 1999; 258: 132-137.
32. Sung YH, Song YJ, Lim SW, Chung JY, Lee GM. Effect of sodium butyrate on the production, heterogeneity and biological activity of human thrombopoietin by recombinant Chinese hamster ovary cells. J Biotechnol. 2004; 112: 323-335.
33. Joosten CE, Shuler ML. Effect of culture conditions on the degree of sialylation of a recombinant glycoprotein expressed in insect cells. Biotechnol Prog. 2003; 19: 739-749.
34. Chitlaru T, Kronman C, Zeevi M, Kam M, Harel A, Ordentlich A, Velan B, Shafferman A. Modulation of circulatory residence of recombinant acetylcholinesterase through biochemical or genetic manipulation of sialylation levels. Biochem J. 1998; 336: 647-658.
35. Gawlitzek M, Valley U, Wagner R. Ammonium ion and glucosamine dependent increases of oligosaccharide complexity in recombinant glycoproteins secreted from cultivated BHK-21 cells. Biotechnol Bioeng. 1998; 57: 518-528.
36. Gawlitzek M, Papac DI, Sliwkowski MB, Ryll T. Incorporation of N-15 from ammonium into the N-linked oligosaccharides of an immunoadhesin glycoprotein expressed in Chinese hamster ovary cells. Glycobiology. 1999; 9: 125-131.
37. Gawlitzek M, Ryll T, Lofgren J, Sliwkowski MB. Ammonium alters N-glycan structures of recombinant TNFR-IgG: degradative versus biosynthetic mechanisms. Biotechnol Bioeng. 2000; 68: 637-646.