Cation exchange versus multimodal cation exchange resins for antibody capture from CHO supernatants: Identification of contaminating Host Cell Proteins by mass spectrometry

Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences

Volumn 942-943, Issue , 2013, Pages 126-133

  Joucla, G ^a   Le Senechal C ^a   Begorre M ^a   Garbay, B ^a   Santarelli, X ^a   Cabanne, C ^a  

^a UNIVERSITÉ DE BORDEAUX   (France)

Author keywords

Antibody; Cation exchange chromatography; Host cell proteins; Mass spectrometry; Mixed mode chromatography

Indexed keywords

CELL CULTURE; CHROMATOGRAPHY; ION EXCHANGE RESINS; MASS SPECTROMETRY; POSITIVE IONS;

CATION EXCHANGE CHROMATOGRAPHY; CATION EXCHANGE RESINS; CHINESE HAMSTER OVARY CELLS; CULTURE SUPERNATANT; HOST CELL PROTEIN; HYDROPHOBIC MOIETIES; MIXED-MODE CHROMATOGRAPHY; RECOMBINANT ANTIBODY;

ANTIBODIES;

CATION EXCHANGE RESIN; CELL PROTEIN; IMMUNOGLOBULIN G; RECOMBINANT ANTIBODY;

ANIMAL CELL; ANIMAL CELL CULTURE; ANTIBODY DETECTION; ANTIBODY PRODUCTION; ANTIGEN BINDING; ARTICLE; CATION EXCHANGE; CELL PH; CHO CELL; CONDUCTANCE; CONTROLLED STUDY; DIAFILTRATION; ELUTION; ENZYME LINKED IMMUNOSORBENT ASSAY; FEMALE; HOST CELL; HYDROGEN BOND; INTERMETHOD COMPARISON; ION EXCHANGE CHROMATOGRAPHY; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PURIFICATION; STEADY STATE; ULTRA PERFORMANCE LIQUID CHROMATOGRAPHY; ULTRAFILTRATION; VACUUM ASPIRATION;

CRICETULUS GRISEUS;

ANTIBODY; CATION EXCHANGE CHROMATOGRAPHY; HOST CELL PROTEINS; MASS SPECTROMETRY; MIXED-MODE CHROMATOGRAPHY;

ANIMALS; ANTIBODIES, MONOCLONAL; CATION EXCHANGE RESINS; CHO CELLS; CHROMATOGRAPHY, ION EXCHANGE; CRICETINAE; CRICETULUS; MASS SPECTROMETRY; PROTEINS; REPRODUCIBILITY OF RESULTS;

EID: 84887934788     PISSN: 15700232     EISSN: 1873376X     Source Type: Journal    
DOI: 10.1016/j.jchromb.2013.10.033     Document Type: Article

References (30)

1. Shukla A.A., Thommes J. Recent advances in large-scale production of monoclonal antibodies and related proteins. Trends Biotechnol. 2010, 28:253-261.
2. Rai M., Padh H. Expression systems for production of heterologous proteins (Review). Current Science 2001, 80(9):1121-1128.
3. E.S. Langer, BioPlan Associates, Inc., Pharmaceutical Manufacturing (April 2009).
4. Schwartz W., Judd D., Wysocki M., Guerrier L., Birck-Wilson E., Boschetti E. Comparison of hydrophobic charge induction chromatography with affinity chromatography on protein A for harvest and purification of antibodies. J. Chromatogr. A 2001, 908(1-2):251-263.
5. Follman D.K., Farner R.L. Factorial screening of antibody purification processes using three chromatography steps without protein A. J. Chromatogr. A 2004, 1024(1-2):79-85.
6. Ng P.K., Snyder M.A. pH-based cation exchange chromatography in the capture and elution of monoclonal antibodies. J. Sep. Sci. 2012, 35:29-35.
7. Guerrier L., Flayeux I., Boschetti E. A dual-mode approach to the selective separation of antibodies and their fragments. J. Chromatogr. B 2001, 755:37-46.
8. Boschetti E. Antibody separation by hydrophobic charge induction chromatography. Trends Biotechnol. 2002, 20:333-337.
9. Mowry M.C., Meagher M., Smith L., Marks J., Subramanian A. Production and purification of a chimeric monoclonal antibody against botulinum neurotoxin serotype A. Protein Expres. Purif. 2004, 37:399-408.
10. Ghose S., Hubbard B., Cramer S.M. Evaluation and comparison of alternatives to protein A chromatography mimetic and hydrophobic charge induction chromatographic stationary phases. J. Chromatogr. A 2006, 1122:144-152.
11. Bak H., Thomas O.R.T. Evaluation of commercial chromatographic adsorbents for the direct capture of polyclonal rabbit antibodies from clarified antiserum. J. Chromatogr. B 2007, 848:116-130.
12. Chen J., Tetrault J., Zhang Y., Wasserman A., Conley G., DiLeo M., Haimes E., Nixon A.E., Ley A. The distinctive separation attributes of mixed-mode resins and their application in monoclonal antibody downstream purification process. J. Chromatogr. A 2010, 1217:216-224.
13. Shukla A.A., Hinckley P. Host cell protein clearance during protein A chromatography: development of an improved column wash step. Biotechnol. Prog. 2008, 24(5):1115-1121.
14. Grzeskowiak J.K., Tscheliessnig A., Wu M.W., Toh P.C., Chusainow J., Lee Y.Y., Wong N., Jungbauer A. Two-dimensional difference fluorescence gel electrophoresis to verify the scale-up of a non-affinity-based downstream process for isolation of a therapeutic recombinant antibody. Electrophoresis 2010, 31:1862-1872.
15. Jin M., Szapiel N., Zhang J., Hickey J., Ghose S. Profiling of host cell proteins by two-dimensional difference gel electrophoresis (2D-DIGE): implications for downstream process development. Biotechnol. Bioeng. 2010, 105(2):306-316.
16. Tait A.S., Hogwood C.E., Smales C.M., Bracewell D.G. Host cell protein dynamics in the supernatant of a mAb producing CHO cell line. Biotechnol. Bioeng. 2012, 109(4):971-982.
17. Tarrant R.D., Velez-Suberbie M.L., Tait A.S., Smales C.M., Bracewell D.G. Host cell protein adsorption characteristics during protein A chromatography. Biotechnol. Prog. 2012, 28(4):1037-1044.
18. Hogwood C.E., Tait A.S., Koloteva-Levine N., Bracewell D.G., Smales C.M. The dynamics of the CHO host cell protein profile during clarification and protein A capture in a platform antibody purification process. Biotechnol. Bioeng. 2013, 110(1):240-251.
19. Doneanu C.E., Xenopoulos A., Fadgen K., Murphy J., Skilton St.J., Prentice H., Stapels M., Chen W. Analysis of host-cell proteins in biotherapeutic proteins by comprehensive online two-dimensional liquid chromatography/mass spectrometry. MAbs 2012, 4(1):24-44.
20. Pezzini J., Joucla G., Gantier R., Toueille M., Lomenech A.M., Le Sénéchal C., Garbay B., Santarelli X., Cabanne C. Antibody capture by mixed-mode chromatography: a comprehensive study from determination of optimal purification conditions to identification of contaminating host cell proteins. J. Chromatogr. A 2011, 1218:8197-8208.
21. T.N. Gonzalez, S.R., Leong, L.G. Presta, (2000) (Genentech). Nucleic acids encoding humanized anti-IL-8 monoclonal antibodies. US 6025158.
22. Reeb B.A. Dye exclusion test for bone marrow viability. Bone Marrow and Stem Cell Processing: A Manual of Current Techniques 1992, 403-404. F.A. Davis Company, New York. E.M. Areman, H.J. Deeg, R.A. Sacher (Eds.).
23. Kim W.D., Tokunaga M., Ozaki H., Ishibashi T., Honda K., Kajiura H., Fujiyama K., Asano R., Kumagai I., Omasa T., Ohtake H. Glycosylation pattern of humanized IgG-like bispecific antibody produced by recombinant CHO cells. Appl. Microbiol. Biotechnol. 2010, 85(3):535-542.
24. Melander W.R., Rassi Z.E., Horvath C.S. Interplay of hydrophobic and electrostatic interactions in biopolymer chromatography: effect of salts on the retention of proteins. J. Chromatogr. 1989, 469:3-27.
25. Mattock K.L., Gough P.J., Humphries J., Burnand K., Patel L., Suckling K.E., Cuello F., Watts C., Gautel M., Avkiran M., Smith A. Legumain and cathepsin-L expression in human unstable carotid plaque. Atherosclerosis 2010, 208:83-89.
26. Robert F., Bierau H., Rossi M., Agugiaro D., Soranzo T., Broly H., Mitchell-Logean C. Degradation of an Fc-fusion recombinant protein by host cell proteases: identification of a CHO cathepsin D protease. Biotechnol. Bioeng. 2009, 104(6):1132-1141.
27. Ibrahim-Granet O., Bertrand O. Separation of proteases: old and new approaches. J. Chromatogr. B 1996, 684(1-2):239-263.
28. Hendershot L.M., Valentine V.A., Lee A.S., Morris S.W., Shapiro D.N. Localization of the gene encoding human BiP/GRP78, the endoplasmic reticulum cognate of the HSP70 family, to chromosome 9q34. Genomics 1994, 20(2):281-284.
29. Kober L., Zehe C., Bode J. Development of a novel ER stress based selection system for the isolation of highly productive clones. Biotechnol. Bioeng. 2012, 109(10):2599-2611.
30. Lee Y.K., Brewer J.W., Hellman R., Hendershot L.M. BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly. Mol. Biol. Cell 1999, 10(7):2209-2219.