Physicochemical and functional comparability between the proposed biosimilar rituximab GP2013 and originator rituximab

BioDrugs

Volumn 27, Issue 5, 2013, Pages 495-507

  Visser, Jan ^a   Feuerstein, Isabel ^b   Stangler, Thomas ^b   Schmiederer, Timo ^b   Fritsch, Cornelius ^b   Schiestl, Martin ^b  

^a Sandoz Biopharmaceuticals   (Germany)

^b NOVARTIS PHARMA AG   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

2 AMINOBENZAMIDE; AMINO ACID; BIOSIMILAR AGENT; DODECYL SULFATE SODIUM; FC RECEPTOR; GLYCAN DERIVATIVE; GP 2013; LYSINE; RITUXIMAB; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANTIBODY DEPENDENT CELLULAR CYTOTOXICITY; APOPTOSIS; ARTICLE; ASYMMETRIC FLOW FIELD FLOW FRACTIONATION; BIOASSAY; CAPILLARY ELECTROPHORESIS; CIRCULAR DICHROISM; COMPLEMENT DEPENDENT CYTOTOXICITY; DEUTERIUM HYDROGEN EXCHANGE; DIFFERENTIAL SCANNING CALORIMETRY; DRUG RECEPTOR BINDING; ELECTROSPRAY MASS SPECTROMETRY; FLUORESCENCE; FRACTIONATION; GEL PERMEATION CHROMATOGRAPHY; GLYCATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; INFRARED SPECTROSCOPY; ION EXCHANGE CHROMATOGRAPHY; MASS SPECTROMETRY; MOLECULAR WEIGHT; PEPTIDE MAPPING; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; SURFACE PLASMON RESONANCE; ULTRAVIOLET SPECTROPHOTOMETRY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ANTIBODIES, MONOCLONAL, MURINE-DERIVED; BIOSIMILAR PHARMACEUTICALS; CELL LINE; HUMANS; KILLER CELLS, NATURAL; PEPTIDE MAPPING; POLYSACCHARIDES;

EID: 84883879484     PISSN: 11738804     EISSN: 1179190X     Source Type: Journal    
DOI: 10.1007/s40259-013-0036-3     Document Type: Article

References (33)

1. European Medicines Agency, Committee for Medicinal Products for Human Use (CHMP). Guideline on similar biological medicinal products containing monoclonal antibodies - non-clinical and clinical issues. London: European Medicines Agency; 2012. http://www.ema.europa.eu/docs/en-GB/document-library/ Scientific-guideline/2012/06/WC500128686.pdf.
2. Food and Drug Administration, Center for Drug Evaluation and Research (CDER). Guidance for Industry. Scientific considerations in demonstrating biosimilarity to a reference product. Rockville: Food and Drug Administration; 2012. http://www.fda.gov/downloads/Drugs/ GuidanceComplianceRegulatoryInformation/Guidances/UCM291128.pdf.
3. Schiestl M, Stangler T, Torella C, et al. Acceptable changes in quality attributes of glycosylated biopharmaceuticals. Nat Biotechnol. 2011;29(4):310-2.
4. McCamish M, Woollett G. The state of the art in the development of biosimilars. Clin Pharmacol Ther. 2012;91(3):405-17.
5. Cornes P. The economic pressures for biosimilar drug use in cancer medicine. Target Oncol. 2012;7(Suppl 1):S57-67.
6. Engen JR. Analysis of protein confirmation and dynamics by hydrogen/deuterium exchange MS. Anal Chem. 2009;81(19):7870-5.
7. Houde D, Berkowitz SA, Engen JR. The utility of hydrogen deuterium exchange mass spectrometry in biopharmaceutical comparability studies. J Pharm Sci. 2011;100(6):2071-86.
8. Van Holde KE, Curtis Johnson W, Shing Ho P. Thermodynamics and biochemistry. In: Principles of physical biochemistry. 2nd ed. Upper Saddle River: Pearson Prentice Hall; 2006. p. 72-105.
9. Andersen CB, Manno M, Rischel C, Thórólfsson M, Martorana V. Aggregation of a multidomain protein: a coagulation mechanism governs aggregation of a model IgG1 antibody under weak thermal stress. Prot Sci. 2010;19:279-90.
10. Du Y, Walsh A, Ehrick R, et al. Chromatographic analysis of the acidic and basic species of recombinant monoclonal antibodies. MAbs. 2012;4(5):578-85.
11. Khawli LA, Goswami S, Hutchinson R, et al. Charge variants in IgG1: isolation, characterization, in vitro binding properties and pharmacokinetics in rats. MAbs. 2010;2(6):613-24.
12. Chelius D, Rehder DS, Bondarenko PV. Identification and characterization of deamidation sites in the conserved regions of human immunoglobulin gamma antibodies. Anal Chem. 2005;77(18):6004-11.
13. Chumsae C, Gaza-Bulseco G, Sun J, et al. Comparison of methionine oxidation in thermal stability and chemically stressed samples of a fully human monoclonal antibody. J Chromatogr B Analyt Technol Biomed Life Sci. 2007;850(1-2):285-94.
14. Johnson KA, Paisley-Flango K, Tangarone BS, et al. Cation exchange-HPLC and mass spectrometry reveal C-terminal amidation of an IgG1 heavy chain. Anal Biochem. 2007;360(1):75-83.
15. Zhang B, Yang Y, Yuk I, et al. Unveiling a glycation hot spot in a recombinant humanized monoclonal antibody. Anal Chem. 2008;80(7):2379-90.
16. Hossler P, Khattak SF, Li ZJ. Optimal and consistent protein glycosylation in mammalian cell culture. Glycobiology. 2009;19(9):936-49.
17. Beck A, Wagner-Rousset E, Bussat MC, et al. Trends in glycosylation, glycoanalysis and glycoengineering of therapeutic antibodies and Fc-fusion proteins. Curr Pharm Biotechnol. 2008;9(6):482-501.
18. Ghaderi D, Taylor RE, Padler-Karavani V, et al. Implications of the presence of N-glycolylneuraminic acid in recombinant therapeutic glycoproteins. Nat Biotechnol. 2010;28(8):863-7.
19. Macher BA, Galili U. The Galalpha1,3Galbeta1,4GlcNAc-R (alpha-Gal) epitope: a carbohydrate of unique evolution and clinical relevance. Biochim Biophys Acta. 2008;1780(2):75-88.
20. Chung CH, Mirakhur B, Chan E, et al. Cetuximab-induced anaphylaxis and IgE specific for galactose-α-1,3-galactose. N Engl J Med. 2008;358(11):1109-17.
21. Shields RL, Lai J, Keck R, et al. Lack of fucose on human IgG1N-linked oligosaccharides improves binding to human Fcgamma RIII and antibody-dependent cytotoxicity. J Biol Chem. 2002;277(30):26733-40.
22. Niwa R, Natsume A, Uehara A, et al. IgG subclass-independent improvement of antibody-dependent cellular cytotoxicity by fucose removal from Asn297-linked oligosaccharides. J Immunol Methods. 2005;306(1-2):151-60.
23. Chung S, Quarmby V, Gao X, et al. Quantitative evaluation of fucose reducing effects in a humanized antibody on Fc receptor binding and antibody-dependent cell-mediated cytotoxicity activities. MAbs. 2012;4(3):326-40.
24. Rosenberg AS. Effects of protein aggregates: an immunologic perspective. AAPS J. 2006;8(3):E501-7.
25. den Engelsman J, Garidel P, Smulders R, et al. Strategies for the assessment of protein aggregates in pharmaceutical biotech product development. Pharm Res. 2011;28(4):920-33.
26. Weiner GJ. Rituximab: mechanism of action. Semin Hematol. 2010;47(2):115-23.
27. Roopenian DC, Akilesh S. FcRn: the neonatal Fc receptor comes of age. Nat Rev Immunol. 2007;7(9):715-25.
28. Jiang XR, Song A, Bergelson S, et al. Advances in the assessment and control of the effector functions of therapeutic antibodies. Nat Rev Drug Discov. 2011;10(2):101-11.
29. Nimmerjahn F, Ravetch JV. Anti-inflammatory actions of intravenous immunoglobulin. Annu Rev Immunol. 2008;26:513-33.
30. Cartron G, Dacheux L, Salles G, et al. Therapeutic activity of humanized anti-CD20 monoclonal antibody and polymorphism in IgG Fc receptor FcgammaRIIIa gene. Blood. 2002;99(3):754-8.
31. γRIIb binding. J Biol Chem. 2001;276(49):45539-47.
32. Masuda K, Kubota T, Kaneko E, et al. Enhanced binding affinity for FcγRIIIa of fucose-negative antibody is sufficient to induce maximal antibody-dependent cellular cytotoxicity. Mol Immunol. 2007;44(12):3122-31.
33. Lee CH, Choi DK, Choi HJ, et al. Expression of soluble and functional human neonatal Fc receptor in Pichia pastoris. Prot Expr Purif. 2010;71(1):42-8.