Bibliography

Biosimilarity: The FDA Perspective

24 • Higher eukaryotes like mammalian cells or insect or plant cells provide much lower yields and are harder to manage.

Mammalian cells such as ovarian cells of CHO are commonly used to produce complex glycoproteins. • Plant and transgenic animals produce therapeutic proteins in a tissue (in the case of plants) or in a uid (most often milk for transgenic animals) in large quantities that are highly practical sources of future biological products.

Given that living entities are involved in the expression of proteins, it is easy to see how a change in bioprocessing conditions can readily alter the structure of proteins. Harder to manage are the variance in the glycan patterns, the antibody-dependent cell-mediated cytotoxicity, and other similar variations that might not necessarily be clinically meaningful, yet to prove it otherwise may be impossible, resulting in a biosimilar product developer modifying the bioprocessing to assure that the structure of protein expressed is as close as possible to the originator molecule.

Anderson, C. L. (2012 June) Applications of imaged capillary isoelectric focussing technique in development of biopharmaceutical glycoprotein-based products. Electrophoresis 33 (11): 1538–1544. Bártová, E., Krejcí, J., Harnicarová, A., Galiová, G., and Kozubek, S. (2008) Histone modi cations and nuclear architecture: A review. J Histochem Cytochem 56 (8): 711–721. Beck, A., Sanglier-Cianférani, S., and Van Dorsselaer, A. (2012 June 5) Biosimilar, biobetter, and next generation antibody characterization by mass spectrometry. Anal Chem 84 (11): 4637–4646. Beck, A., Wurch, T., and Reichert, J. M. (2011 March–April 3) Sixth annual european antibody congress 2010: November 29–December 1, 2010, Geneva, Switzerland. MAbs 3 (2): 111–132. Boubeva, R., Reichert, C., Handrick, R., Müller, C., Hannemann, J., and Borcharda, G. (2012) New expression method and characterization of recombinant human granulocyte colonystimulating factor in a stable protein formulation. Chimia (Aarau) 66 (5): 281–285. Brennan, D. F. and Barford, D. (2009) Eliminylation: A post-translational modi cation catalyzed by phosphothreonine lyases. Trends Biochem Sci 34 (3): 108–114. Cantor, C. R. and Schimmel, P. R., Biophysical Chemistry Part 1: The Conformation of Biological Macromolecules. New York: W. H. Freeman and Co.; 1980. Cao, J., Sun, W., Gong, F., and Liu, W. (2014 May) Charge pro ling and stability testing of biosimilar by capillary isoelectric focusing. Electrophoresis 35 (10): 1461–1468. Chen, S. L., Wu, S. L., Huang, L. J., Huang, J. B., and Chen, S. H. (2013 June) A global comparability approach for biosimilar monoclonal antibodies using LC-tandem MS based proteomics. J Pharm Biomed Anal 80: 126–135. Creighton, T. E., Protein Structures and Molecular Properties. Second ed., New York: W. H. Freeman and Co.; 1993. Creighton, T. E., The Biophysical Chemistry of Nucleic Acids and Proteins. London: Helvetian Press; 2010.

Understanding proteins

Debaene, F., Wagner-Rousset, E., Colas, O., Ayoub, D., Corvaïa, N., Van Dorsselaer, A., Beck, A., and Cianférani, S. (2013 October 15) Time resolved native ionmobility mass spectrometry tomonitor dynamics of IgG4 Fab arm exchange and “bispeci c” monoclonal antibody formation. Anal Chem 85 (20): 9785–9792. Declerck, P. J. (2013 February) Biosimilar monoclonal antibodies: A science-based regulatory challenge. Expert Opin Biol Ther 13 (2): 153–156. Dorvignit, D., Palacios, J. L., Merino, M., Hernández, T., Sosa, K., Casaco, A., López-Requena, A., and Mateo de Acosta, C. (2012 July–August) Expression and biological characterization of an anti-CD20 biosimilar candidate antibody: A case study. MAbs 4 (4): 488–496. Eddé, B., Rossier, J., Le Caer, J. P., Desbruyères, E., Gros, F., and Denoulet, P. (1990) Posttranslational glutamylation of alpha-tubulin. Science 247 (4938): 83–85. Eichbaum, C. and Haefeli, W. E. (2011 November) Biologics—Nomenclature and classi cation. Ther Umsch 68 (11): 593–601. Gadermaier, G. (2014) Non-speci c lipid transfer proteins: A protein family in search of an allergenic pattern. Int Arch Allergy Immunol 164 (3): 169–170. Gadermaier, G., Eichhorn, S., Vejvar, E., Weilnböck, L., Lang, R., Briza, P., Huber, C. G., Ferreira, F., and Hawranek, T. (2014 August) Plantago lanceolata: An important trigger of summerpollinosis with limited IgE cross-reactivity. J Allergy Clin Immunol 134 (2): 472–475. Glozak, M. A., Sengupta, N., Zhang, X., and Seto, E. (2005) Acetylation and deacetylation of non-histone proteins. Gene 363: 15–23. Guo, Q., Guo, H., Liu, T., Zheng, Y., Gu, P., Chen, X., Wang, H., Hou, S., and Guo, Y. (2014 November 2) Versatile characterization of glycosylation modi cation in CTLA4-Ig fusion proteins by liquid chromatography-mass spectrometry. MAbs 6 (6): 1474–1485. Haselberg, R., de Jong, G. J., and Somsen, G. W. (2013 February 19) Low- ow sheathless capillary electrophoresis-mass spectrometry for sensitive glycoform pro ling of intact pharmaceutical proteins. Anal Chem 85 (4): 2289–2296. Hashii, N., Harazono, A., Kuribayashi, R., Takakura, D., and Kawasaki, N. (2014 April 30) Characterization of N-glycan heterogeneities of erythropoietin products by liquid chromatography/mass spectrometry and multivariate analysis. Rapid Commun Mass Spectrom 28 (8): 921–932. Hassett, B., McMillen, S., and Fitzpatrick, B. (2013 September–October) Characterization and comparison of commercially available TNF receptor 2-Fc fusion protein products: Letter to the editor. MAbs 5 (5): 624–625. Heringa, J. and Taylor, W. R., Computational Protein Science: Methods in Structural Bioinformatics. Hoboken, NJ: J. Wiley & Sons; 2016. Jiang, H., Wu, S. L., Karger, B. L., and Hancock, W. S. (2010 July 15) Characterization of the glycosylation occupancy and the active site in the follow-on protein therapeutic: TNK-tissue plasminogen activator. Anal Chem 82 (14): 6154–6162. Kessel, A. and Nir Ben-Tal, A., Introduction to Proteins: Structure, Function, and Motion. Boca Raton, FL: Chapman & Hall/CRC Mathematical and Computational Biology; 2010. Khoury, G. A., Baliban, R. C., and Floudas, C. A. (2011) Proteome-wide posttranslational modi cation statistics: Frequency analysis and curation of the swiss-prot database. Sci Rep 1 (90): 90. Li, C., Rossomando, A., Wu, S. L., and Karger, B. L. (2013 July–August) Comparability analysis of anti-CD20 commercial (rituximab) and RNAi-mediated fucosylated antibodies by two LC-MS approaches. MAbs 5 (4): 565–575. Lipiäinen, T., Peltoniemi, M., Sarkhel, S., Yrjönen, T., Vuorela, H., Urtti, A., and Juppo, A. (2015 February) Formulation and stability of cytokine therapeutics. J Pharm Sci 104 (2): 307–326. Malakhova, O. A., Yan, M., Malakhov, M. P., Yuan, Y., Ritchie, K. J., Kim, K. I., Peterson, L. F., Shuai, K., and Zhang, D.-E. (2003) Protein ISGylation modulates the JAK-STAT signaling pathway. Genes Dev 17 (4): 455–460. 25

Biosimilarity: The FDA Perspective

26

Mueller, D. A., Heinig, L., Ramljak, S., Krueger, A., Schulte, R., Wrede, A., Stuke, A. W. (2010 December) Conditional expression of full-length humanized antiprion protein antibodies in Chinese hamster ovary cells. Hybridoma (Larchmt) 29 (6): 463–472. Mydel, P. et al. (2010) Carbamylation-dependent activation of T cells: A novel mechanism in the pathogenesis of autoimmune arthritis. J Immunol 184 (12): 6882–6890. Novo, J. B., Oliveira, M. L., Magalhães, G. S., Morganti, L., Raw, I., and Ho, P. L. (2010 November) Generation of polyclonal antibodies against recombinant human glucocerebrosidase produced in Escherichia coli. Mol Biotechnol 46 (3): 279–286. Oh, M. J., Hua, S., Kim, B. J., Jeong, H. N., Jeong, S. H., Grimm, R., Yoo, J. S., and An, H. J. (2013 March) Analytical platform for glycomic characterization of recombinant erythropoietin biotherapeutics and biosimilars by MS. Bioanalysis 5 (5): 545–559. Pan, J. and Borchers, C. H. (2014 May) Top–down mass spectrometry and hydrogen/ deuterium exchange for comprehensive structural characterization of interferons: Implications for biosimilars. Proteomics 14 (10): 1249–1258. Parnham, M. J., Schindler-Horvat, J., and Kozlović, M. (2007 February) Non-clinical safety studies on biosimilar recombinant human erythropoietin. Basic Clin Pharmacol Toxicol 100 (2): 73–83. Review. PubMed PMID: 17244255. Polevoda, B. and Sherman, F. (2003) N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins. J Mol Biol 325 (4): 595–622. Schellekens, H. (2004 August) When biotech proteins go off-patent. Trends Biotechnol 22 (8): 406–410. Review. PubMed PMID: 15283985. Skrlin, A., Radic, I., Vuletic, M., Schwinke, D., Runac, D., Kusalic, T., Paskvan, I., Krsic, M., Bratos, M., and Marinc, S. (2010 September) Comparison of the physicochemical properties of a biosimilar lgrastim with those of reference lgrastim. Biologicals 38 (5): 557–566. Sörgel, F., Lerch, H., and Lauber, T. (2010 December 1) Physicochemical and biologic comparability of a biosimilar granulocyte colony-stimulating factor with its reference product. BioDrugs 24 (6): 347–357. Su, J., Mazzeo, J., Subbarao, N., and Jin, T. (2011 July) Pharmaceutical development of biologics: Fundamentals, challenges and recent advances. Ther Deliv 2 (7): 865–871. PubMed PMID: 22833901. Tan, Q., Guo, Q., Fang, C., Wang, C., Li, B., Wang, H., Li, J., and Guo, Y. (2012 November–December) Characterization and comparison of commercially available TNF receptor 2-Fc fusion protein products. MAbs 4 (6): 761–774. Thelwell, C. (2014 March) Biological standards for potency assignment to brinolytic agents used in thrombolytic therapy. Semin Thromb Hemost 40 (2): 205–213. Toyama, A., Nakagawa, H., Matsuda, K., Sato, T. A., Nakamura, Y., and Ueda, K. (2012 November 20) Quantitative structural characterization of local N-glycan microheterogeneity in therapeutic antibodies by energy-resolved oxonium ion monitoring. Anal Chem 84 (22): 9655–9662. Visser, J., Feuerstein, I., Stangler, T., Schmiederer, T., Fritsch, C., and Schiestl, M. (2013 October) Physicochemical and functional comparability between the proposed biosimilar rituximab GP2013 and originator rituximab. BioDrugs 27 (5): 495–507. Walsh, G., Post-Translational Modification of Protein Biopharmaceuticals. Hoboken, NJ: Wiley-Blackwell; 2009. Whiteheart, S. W. et al. (1989) Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally modi ed by novel amide-linked ethanolamine-phosphoglycerol moieties: Addition of ethanolamine-phosphoglycerol to speci c glutamic acid residues on EF-1 alpha. J Biol Chem 264 (24): 14334–14341.

Understanding proteins

Wilson, V. G. (Ed.), Sumoylation: Molecular Biology and Biochemistry. Oxford, UK: Horizon Bioscience; 2004. ISBN 0-9545232-8-8. Xie, H., Chakraborty, A., Ahn, J., Yu, Y. Q., Dakshinamoorthy, D. P., Gilar, M., Chen, W., Skilton, S. J., and Mazzeo, J. R. (2010 July–August) Rapid comparison of a candidate biosimilar to an innovator monoclonal antibody with advanced liquid chromatography and mass spectrometry technologies. MAbs 2 (4): 379–394. Yang, X. J. and Seto, E. (2008) Lysine acetylation: Codi ed crosstalk with other posttranslational modi cations. Mol Cell 31 (4): 449–461.

27

http://taylorandfrancis.com