Development of purification processes for fully human bispecific antibodies based upon modification of protein A binding avidity

mAbs

Volumn 8, Issue 4, 2016, Pages 828-838

  Tustian, Andrew D ^a   Endicott, Christine ^a   Adams, Benjamin ^a   Mattila, John ^a   Bak, Hanne ^a  

^a REGENERON PHARMACEUTICALS INC   (United States)

Author keywords

Affinity chromatography; Bispecific antibody; Downstream process; Elution pH; Heterodimeric antibody; Protein A chromatography; Protein purification

Indexed keywords

MONOCLONAL ANTIBODY; PROTEIN A; BISPECIFIC ANTIBODY; STAPHYLOCOCCUS PROTEIN A;

AFFINITY CHROMATOGRAPHY; ANIMAL CELL; ARTICLE; BINDING AFFINITY; ENZYME LINKED IMMUNOSORBENT ASSAY; HEAVY CHAIN; IMMUNOGENICITY; LIGHT CHAIN; NONHUMAN; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTON NUCLEAR MAGNETIC RESONANCE; ANTIBODY AFFINITY; BIOSYNTHESIS; HUMAN; IMMUNOLOGY; PROCEDURES; PROTEIN ENGINEERING;

ANTIBODIES, BISPECIFIC; ANTIBODIES, MONOCLONAL; ANTIBODY AFFINITY; CHROMATOGRAPHY, AFFINITY; HUMANS; PROTEIN ENGINEERING; STAPHYLOCOCCAL PROTEIN A;

EID: 84963542602     PISSN: 19420862     EISSN: 19420870     Source Type: Journal    
DOI: 10.1080/19420862.2016.1160192     Document Type: Article

References (38)

1. H.Byrne, P.J.Conroy, J.C.Whisstock, R.J.O'Kennedy. A tale of two specificities: bispecific antibodies for therapeutic and diagnostic applications. Trends Biotechnol 2013; 31:621-32; PMID:24094861; http://dx.doi.org/10.1016/j.tibtech.2013.08.007
2. C.May, P.Sapra, H.P.Gerber. Advances in bispecific biotherapeutics for the treatment of cancer. Biochem Pharmacol 2012; 84:1105-12; PMID:22858161; http://dx.doi.org/10.1016/j.bcp.2012.07.011
3. R.Kontermann. Dual targeting strategies with bispecific antibodies. mAbs 2012; 4; PMID:22453100; http://dx.doi.org/10.4161/mabs.4.2.19000
4. S.J.Demarest, K.Hariharan, J.Dong. Emerging antibody combinations in oncology. mAbs 2011; 3:338-51; PMID:21697653; http://dx.doi.org/10.4161/mabs.3.4.16615
5. D.Muller, R.E.Kontermann. Bispecific antibodies for cancer immunotherapy: current perspectives. BioDrugs: Clin Immunotherap, Biopharmac Gene Ther 2010; 24:89-98; PMID:20199124; http://dx.doi.org/10.2165/11530960-000000000-00000
6. D.Holmes. Buy buy bispecific antibodies. Nat Rev Drug Disc 2011; 10:798-800; PMID:22037028; http://dx.doi.org/10.1038/nrd3581
7. R.Linke, A.Klein, D.Seimetz. Catumaxomab: clinical development and future directions. mAbs 2010; 2:129-36; PMID:20190561; http://dx.doi.org/10.4161/mabs.2.2.11221
8. E.Wolf, R.Hofmeister, P.Kufer, B.Schlereth, P.A.Baeuerle. BiTEs: bispecific antibody constructs with unique anti-tumor activity. Drug Disc Today 2005; 10:1237-44; PMID:16213416; http://dx.doi.org/10.1016/S1359-6446(05)03554-3
9. H.Lindhofer, R.Mocikat, B.Steipe, S.Thierfelder. Preferential species-restricted heavy/light chain pairing in rat/mouse quadromas. Implications for a single-step purification of bispecific antibodies. J Immunol 1995; 155:219-25; PMID:7602098
10. A.M.Merchant, Z.Zhu, J.Q.Yuan, A.Goddard, C.W.Adams, L.G.Presta, P.Carter. An efficient route to human bispecific IgG. Nat Biotechnol 1998; 16:677-81; PMID:9661204; http://dx.doi.org/10.1038/nbt0798-677
11. J.Jackman, Y.Chen, A.Huang, B.Moffat, J.M.Scheer, S.R.Leong, W.P.Lee, J.Zhang, N.Sharma, Y.Lu, et al. Development of a two-part strategy to identify a therapeutic human bispecific antibody that inhibits IgE receptor signaling. J Biol Chem 2010; 285:20850-9; PMID:20444694; http://dx.doi.org/10.1074/jbc.M110.113910
12. C.Spiess, J.Bevers, 3rd, J.Jackman, N.Chiang, G.Nakamura, M.Dillon, H.Liu, P.Molina, J.M.Elliott, W.Shatz, et al. Development of a human IgG4 bispecific antibody for dual targeting of interleukin-4 (IL-4) and interleukin-13 (IL-13) cytokines. J Biol Chem 2013; 288:26583-93; PMID:23880771; http://dx.doi.org/10.1074/jbc.M113.480483
13. E.J.Smith, K.Olson, L.J.Haber, B.Varghese, P.Duramad, A.D.Tustian, A.Oyejide, J.R.Kirshner, L.Canova, J.Menon, et al. A novel, native-format bispecific antibody triggering T-cell killing of B-cells is robustly active in mouse tumor models and cynomolgus monkeys. Sci Rep 2015; 5:17943; PMID:26659273; http://dx.doi.org/10.1038/srep17943
14. 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 1981; 20:2361-70; PMID:7236608; http://dx.doi.org/10.1021/bi00512a001
15. J.Deisenhofer, T.A.Jones, R.Huber, J.Sjodahl, J.Sjoquist. Crystallization, crystal structure analysis and atomic model of the complex formed by a human Fc fragment and fragment B of protein A from Staphylococcus aureus. Hoppe-Seyler's Zeitschrift fur Physiologische Chemie 1978; 359:975-85; PMID:711157; http://dx.doi.org/10.1515/bchm2.1978.359.2.975
16. B.Akerstrom, B.H.Nilson, H.R.Hoogenboom, L.Bjorck. On the interaction between single chain Fv antibodies and bacterial immunoglobulin-binding proteins. J Immunol Methods 1994; 177:151-63; PMID:7822821; http://dx.doi.org/10.1016/0022-1759(94)90152-X
17. M.Inganas. Comparison of mechanisms of interaction between protein A from Staphylococcus aureus and human monoclonal IgG, IgA and IgM in relation to the classical FC gamma and the alternative F(ab')2 epsilon protein A interactions. Scandinavian J Immunol 1981; 13:343-52; PMID:7302528; http://dx.doi.org/10.1111/j.1365-3083.1981.tb00143.x
18. M.A.Starovasnik, M.P.O'Connell, W.J.Fairbrother, R.F.Kelley. Antibody variable region binding by Staphylococcal protein A: thermodynamic analysis and location of the Fv binding site on E-domain. Protein Sci: A Pub Protein Society 1999; 8:1423-31; PMID:10422830; http://dx.doi.org/10.1110/ps.8.7.1423
19. M.A.Vidal, F.P.Conde. Alternative mechanism of protein A-immunoglobulin interaction the VH-associated reactivity of a monoclonal human IgM. J Immunol 1985; 135:1232-8; PMID:3925002
20. K.N.Potter, Y.Li, R.A.Mageed, R.Jefferis, J.D.Capra. Anti-idiotypic antibody D12 and superantigen SPA both interact with human VH3-encoded antibodies on the external face of the heavy chain involving FR1, CDR2 and FR3. Molecular Immunol 1998; 35:1179-87; PMID:10199392; http://dx.doi.org/10.1016/S0161-5890(98)00103-5
21. E.H.Sasso, G.J.Silverman, M.Mannik. Human IgM molecules that bind staphylococcal protein A contain VHIII H chains. J Immunol 1989; 142:2778-83; PMID:2495325
22. E.H.Sasso, G.J.Silverman, M.Mannik. Human IgA and IgG F(ab')2 that bind to staphylococcal protein A belong to the VHIII subgroup. J Immunol 1991; 147:1877-83; PMID:1909733
23. H.W.SchroederJr, J.L.Hillson, R.M.Perlmutter. Structure and evolution of mammalian VH families. Int Immunol 1990; 2:41-50; PMID:2128464; http://dx.doi.org/10.1093/intimm/2.1.41
24. M.A.Walter, D.W.Cox. Analysis of genetic variation reveals human immunoglobulin VH-region gene organization. Am J Hum Genet 1988; 42:446-51; PMID:2894757
25. U.K.Ljungberg, B.Jansson, U.Niss, R.Nilsson, B.E.Sandberg, B.Nilsson. The interaction between different domains of staphylococcal protein A and human polyclonal IgG, IgA, IgM and F(ab')2: separation of affinity from specificity. Mol Immunol 1993; 30:1279-85; PMID:8413328; http://dx.doi.org/10.1016/0161-5890(93)90044-C
26. P.W.Roben, A.N.Salem, G.J.Silverman. VH3 family antibodies bind domain D of staphylococcal protein A. J Immunol 1995; 154:6437-45; PMID:7759880
27. L.Cedergren, R.Andersson, B.Jansson, M.Uhlen, B.Nilsson. Mutational analysis of the interaction between staphylococcal protein A and human IgG1. Protein Eng 1993; 6:441-8; PMID:8332602; http://dx.doi.org/10.1093/protein/6.4.441
28. S.Ghose, M.Allen, B.Hubbard, C.Brooks, S.M.Cramer. Antibody variable region interactions with Protein A: implications for the development of generic purification processes. Biotechnol Bioeng 2005; 92:665-73; PMID:16206278; http://dx.doi.org/10.1002/bit.20729
29. N.B.Afeyan, N.F.Gordon, I.Mazsaroff, L.Varady, S.P.Fulton, Y.B.Yang, F.E.Regnier. Flow-through particles for the high-performance liquid chromatographic separation of biomolecules: perfusion chromatography. J Chromatograp 1990; 519:1-29; PMID:2077042; http://dx.doi.org/10.1016/0021-9673(90)85132-F
30. D.Whitney, M.McCoy, N.Gordon, N.Afeyan. Characterization of large-pore polymeric supports for use in perfusion biochromatography. J Chromatograp A 1998; 807:165-84; PMID:9646494; http://dx.doi.org/10.1016/S0021-9673(98)00068-5
31. I.Arora. Chromatographic methods for the purification of monoclonal antibodies and their alternatives: a review.
32. G.Zhao, X.-Y.Dong, Y.Sun. Ligands for mixed-mode protein chromatography: Principles, characteristics and design. J Biotechnol 2009; 144:3-11; PMID:19409941; http://dx.doi.org/10.1016/j.jbiotec.2009.04.009
33. J.Chen, J.Tetrault, Y.Zhang, A.Wasserman, G.Conley, M.Dileo, E.Haimes, A.E.Nixon, A.Ley. The distinctive separation attributes of mixed-mode resins and their application in monoclonal antibody downstream purification process. J Chromatograp A 2010; 1217:216-24; PMID:19819462; http://dx.doi.org/10.1016/j.chroma.2009.09.047
34. P.Gagnon. Purification Tools for Monoclonal Antibodies, Validated Biosystems. Inc, Tucson 1996.
35. A.A.Shukla, P.Hinckley. Host cell protein clearance during protein A chromatography: development of an improved column wash step. Biotechnol Progress 2008; 24:1115-21; PMID:19194921; http://dx.doi.org/10.1002/btpr.50
36. G.R.Bolton, K.R.Selvitelli, I.Iliescu, D.J.Cecchini. Inactivation of viruses using novel protein A wash buffers. Biotechnology progress 2015; 31:406-13; PMID:25482293; http://dx.doi.org/10.1002/btpr.2024
37. S.Ghose, B.Hubbard, S.M.Cramer. Binding capacity differences for antibodies and Fc-fusion proteins on protein A chromatographic materials. Biotechnology and bioengineering 2007; 96:768-79; PMID:16817242; http://dx.doi.org/10.1002/bit.21044
38. D.K.Follman, R.L.Fahrner. Factorial screening of antibody purification processes using three chromatography steps without protein A. Journal of chromatography A 2004; 1024:79-85; PMID:14753709; http://dx.doi.org/10.1016/j.chroma.2003.10.060