A new tool for monoclonal antibody analysis

References

• Reichert JM. Marketed therapeutic antibodies compendium. MAbs 2012; 4:413 - 5; http://dx.doi.org/10.4161/mabs.19931; PMID: 22531442
   PubMed Web of Science ®Google Scholar
• Salfeld JG. Isotype selection in antibody engineering. Nat Biotechnol 2007; 25:1369 - 72; http://dx.doi.org/10.1038/nbt1207-1369; PMID: 18066027
   PubMed Web of Science ®Google Scholar
• Jiang X-R, Song A, Bergelson S, Arroll T, Parekh B, May K, Chung S, Strouse R, Mire-Sluis A, Schenerman M. Advances in the assessment and control of the effector functions of therapeutic antibodies. Nat Rev Drug Discov 2011; 10:101 - 11; http://dx.doi.org/10.1038/nrd3365; PMID: 21283105
   PubMed Web of Science ®Google Scholar
• Liu H, Gaza-Bulseco G, Faldu D, Chumsae C, Sun J. Heterogeneity of monoclonal antibodies. J Pharm Sci 2008; 97:2426 - 47; http://dx.doi.org/10.1002/jps.21180; PMID: 17828757
   PubMed Web of Science ®Google Scholar
• Beck A, Wagner-Rousset E, Ayoub D, Van Dorsselaer A, Sanglier-Cianférani S. Characterization of therapeutic antibodies and related products. Anal Chem 2013; 85:715 - 36; http://dx.doi.org/10.1021/ac3032355; PMID: 23134362
   PubMed Web of Science ®Google Scholar
• Jefferis R. Glycosylation of recombinant antibody therapeutics. Biotechnol Prog 2005; 21:11 - 6; http://dx.doi.org/10.1021/bp040016j; PMID: 15903235
   PubMed Web of Science ®Google Scholar
• Dick LW Jr., Mahon D, Qiu D, Cheng K-C. Peptide mapping of therapeutic monoclonal antibodies: improvements for increased speed and fewer artifacts. J Chromatogr B Analyt Technol Biomed Life Sci 2009; 877:230 - 6; http://dx.doi.org/10.1016/j.jchromb.2008.12.009; PMID: 19112052
   PubMed Web of Science ®Google Scholar
• Lippincott J, Apostol I. Carbamylation of cysteine: a potential artifact in peptide mapping of hemoglobins in the presence of urea. Anal Biochem 1999; 267:57 - 64; http://dx.doi.org/10.1006/abio.1998.2970; PMID: 9918655
   PubMed Web of Science ®Google Scholar
• Xiao G, Bondarenko PV, Jacob J, Chu GC, Chelius D. 18O labeling method for identification and quantification of succinimide in proteins. Anal Chem 2007; 79:2714 - 21; http://dx.doi.org/10.1021/ac0617870; PMID: 17313184
   PubMed Web of Science ®Google Scholar
• Fodor S, Zhang Z. Rearrangement of terminal amino acid residues in peptides by protease-catalyzed intramolecular transpeptidation. Anal Biochem 2006; 356:282 - 90; http://dx.doi.org/10.1016/j.ab.2006.06.023; PMID: 16859627
   PubMed Web of Science ®Google Scholar
• Zang L, Carlage T, Murphy D, Frenkel R, Bryngelson P, Madsen M, Lyubarskaya Y. Residual metals cause variability in methionine oxidation measurements in protein pharmaceuticals using LC-UV/MS peptide mapping. J Chromatogr B Analyt Technol Biomed Life Sci 2012; 895-896:71 - 6; http://dx.doi.org/10.1016/j.jchromb.2012.03.016; PMID: 22483985
   PubMed Web of Science ®Google Scholar
• Yan B, Valliere-Douglass J, Brady L, Steen S, Han M, Pace D, Elliott S, Yates Z, Han Y, Balland A, et al. Analysis of post-translational modifications in recombinant monoclonal antibody IgG1 by reversed-phase liquid chromatography/mass spectrometry. J Chromatogr A 2007; 1164:153 - 61; http://dx.doi.org/10.1016/j.chroma.2007.06.063; PMID: 17640657
   PubMed Web of Science ®Google Scholar
• Gadgil HS, Bondarenko PV, Pipes GD, Dillon TM, Banks D, Abel J, Kleemann GR, Treuheit MJ. Identification of cysteinylation of a free cysteine in the Fab region of a recombinant monoclonal IgG1 antibody using Lys-C limited proteolysis coupled with LC/MS analysis. Anal Biochem 2006; 355:165 - 74; http://dx.doi.org/10.1016/j.ab.2006.05.037; PMID: 16828048
   PubMed Web of Science ®Google Scholar
• Adamczyk M, Gebler JC, Wu J. Papain digestion of different mouse IgG subclasses as studied by electrospray mass spectrometry. J Immunol Methods 2000; 237:95 - 104; http://dx.doi.org/10.1016/S0022-1759(00)00135-6; PMID: 10725455
   PubMed Web of Science ®Google Scholar
• Yan B, Eris T, Yates Z, Hong RW, Steen S, Kleemann G, Wang W, Liu JL. Analysis of human antibody IgG2 domains by reversed-phase liquid chromatography and mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci 2009; 877:1613 - 20; http://dx.doi.org/10.1016/j.jchromb.2009.03.043; PMID: 19411197
   PubMed Web of Science ®Google Scholar
• Chen S, Lau H, Brodsky Y, Kleemann GR, Latypov RF. The use of native cation-exchange chromatography to study aggregation and phase separation of monoclonal antibodies. Protein Sci 2010; 19:1191 - 204; http://dx.doi.org/10.1002/pro.396; PMID: 20512972
   PubMed Web of Science ®Google Scholar
• von Pawel-Rammingen U, Johansson BP, Björck L. IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G. EMBO J 2002; 21:1607 - 15; http://dx.doi.org/10.1093/emboj/21.7.1607; PMID: 11927545
   PubMed Web of Science ®Google Scholar
• Vincents B, von Pawel-Rammingen U, Björck L, Abrahamson M. Enzymatic characterization of the streptococcal endopeptidase, IdeS, reveals that it is a cysteine protease with strict specificity for IgG cleavage due to exosite binding. Biochemistry 2004; 43:15540 - 9; http://dx.doi.org/10.1021/bi048284d; PMID: 15581366
   PubMed Web of Science ®Google Scholar
• Wenig K, Chatwell L, von Pawel-Rammingen U, Björck L, Huber R, Sondermann P. Structure of the streptococcal endopeptidase IdeS, a cysteine proteinase with strict specificity for IgG. Proc Natl Acad Sci U S A 2004; 101:17371 - 6; http://dx.doi.org/10.1073/pnas.0407965101; PMID: 15574492
   PubMed Web of Science ®Google Scholar
• Chevreux G, Tilly N, Bihoreau N. Fast analysis of recombinant monoclonal antibodies using IdeS proteolytic digestion and electrospray mass spectrometry. Anal Biochem 2011; 415:212 - 4; http://dx.doi.org/10.1016/j.ab.2011.04.030; PMID: 21596014
   PubMed Web of Science ®Google Scholar
• Goetze AM, Zhang Z, Liu L, Jacobsen FW, Flynn GC. Rapid LC-MS screening for IgG Fc modifications and allelic variants in blood. Mol Immunol 2011; 49:338 - 52; http://dx.doi.org/10.1016/j.molimm.2011.09.002; PMID: 21945018
   PubMed Web of Science ®Google Scholar
• Jäger C, Ferrara C, Umaña P, Zeck A, Regula JT, Koll H. Determination of antibody glycosylation by mass spectrometry. Methods Mol Biol 2012; 901:195 - 208; http://dx.doi.org/10.1007/978-1-61779-931-0_13; PMID: 22723103
   PubMedGoogle Scholar
• Wang B, Gucinski AC, Keire DA, Buhse LF, Boyne MT 2nd. Structural comparison of two anti-CD20 monoclonal antibody drug products using middle-down mass spectrometry. Analyst 2013; 138:3058 - 65; http://dx.doi.org/10.1039/c3an36524g; PMID: 23579346
   PubMed Web of Science ®Google Scholar
• Ayoub D, Jabs W, Resemann A, Evers W, Evans C, Main L, Baessmann C, Wagner-Rousset E, Suckau D, Beck A. Correct primary structure assessment and extensive glyco-profiling of cetuximab by a combination of intact, middle-up, middle-down and bottom-up ESI and MALDI mass spectrometry techniques. MAbs 2013; 5:699 - 710; http://dx.doi.org/10.4161/mabs.25423; PMID: 23924801
   PubMed Web of Science ®Google Scholar
• Wagner-Rousset E, Janin-Bussat M-C, Colas O, Excoffier M, Ayoub D, Haeuw J-F, Rilatt I, Perez M. Corvaȉa N, Beck A. Antibody-drug conjugate model fast characterization by LC-MS following IdeS proteolytic digestion. MAbs 2014; 6:1 - 12; http://dx.doi.org/10.4161/mabs.26773
   PubMed Web of Science ®Google Scholar
• Goetze AM, Liu YD, Arroll T, Chu L, Flynn GC. Rates and impact of human antibody glycation in vivo. Glycobiology 2012; 22:221 - 34; http://dx.doi.org/10.1093/glycob/cwr141; PMID: 21930650
   PubMed Web of Science ®Google Scholar
• Zhou S, Mozziconacci O, Kerwin BA, Schöneich C. Fluorogenic tagging methodology applied to characterize oxidized tyrosine and phenylalanine in an immunoglobulin monoclonal antibody. Pharm Res 2013; 30:1311 - 27; http://dx.doi.org/10.1007/s11095-012-0970-7; PMID: 23412915
   PubMed Web of Science ®Google Scholar
• Woodard J, Lau H, Latypov RF. Nondenaturing size-exclusion chromatography-mass spectrometry to measure stress-induced aggregation in a complex mixture of monoclonal antibodies. Anal Chem 2013; 85:6429 - 36; http://dx.doi.org/10.1021/ac401455f; PMID: 23742703
   PubMed Web of Science ®Google Scholar
• Strand J, Huang C-T, Xu J. Characterization of Fc-fusion protein aggregates derived from extracellular domain disulfide bond rearrangements. J Pharm Sci 2013; 102:441 - 53; http://dx.doi.org/10.1002/jps.23421; PMID: 23242781
   PubMed Web of Science ®Google Scholar
• Lynaugh H, Li H, Gong B. Rapid Fc glycosylation analysis of Fc fusions with IdeS and liquid chromatography mass spectrometry. MAbs 2013; 5:641 - 5; http://dx.doi.org/10.4161/mabs.25302; PMID: 23839239
   PubMed Web of Science ®Google Scholar
• Zhang Z, Pan H, Chen X. Mass spectrometry for structural characterization of therapeutic antibodies. Mass Spectrom Rev 2009; 28:147 - 76; http://dx.doi.org/10.1002/mas.20190; PMID: 18720354
   PubMed Web of Science ®Google Scholar
• Fornelli L, Ayoub D, Aizikov K, Beck A, Tsybin YO. Middle-down analysis of monoclonal antibodies with electron transfer dissociation orbitrap fourier transform mass spectrometry. Anal Chem 2014; 86:3005 - 12; http://dx.doi.org/10.1021/ac4036857; PMID: 24588056
   PubMed Web of Science ®Google Scholar
• Bondt A, Rombouts Y, Hazes JMW, Wuhrer M, Dolhain RJEM. European Workshop for Rheumatology Research, 20–22 February 2014, Lisbon, Portugal. Abstracts. Ann Rheum Dis 2014; 73:Suppl 1 A1; http://dx.doi.org/10.1136/annrheumdis-2013-205124.2; PMID: 24489135
   PubMedGoogle Scholar
• Anumula KR. Quantitative glycan profiling of normal human plasma derived immunoglobulin and its fragments Fab and Fc. J Immunol Methods 2012; 382:167 - 76; http://dx.doi.org/10.1016/j.jim.2012.05.022; PMID: 22683540
   PubMed Web of Science ®Google Scholar
• Angal S, King DJ, Bodmer MW, Turner A, Lawson ADG, Roberts G, Pedley B, Adair JR. A single amino acid substitution abolishes the heterogeneity of chimeric mouse/human (IgG4) antibody. Mol Immunol 1993; 30:105 - 8; http://dx.doi.org/10.1016/0161-5890(93)90432-B; PMID: 8417368
   PubMed Web of Science ®Google Scholar
• Labrijn AF, Buijsse AO, van den Bremer ETJ, Verwilligen AYW, Bleeker WK, Thorpe SJ, Killestein J, Polman CH, Aalberse RC, Schuurman J, et al. Therapeutic IgG4 antibodies engage in Fab-arm exchange with endogenous human IgG4 in vivo. Nat Biotechnol 2009; 27:767 - 71; http://dx.doi.org/10.1038/nbt.1553; PMID: 19620983
   PubMed Web of Science ®Google Scholar
• Shen FJ, Kwong MY, Keck RG, Harris RJ. The application of tert-butylhydroperoxide oxidation to study sites of potential methionine oxidation in a recombinant antibody. Techniques in Protein Chemistry 1996; VII:275 - 84; http://dx.doi.org/10.1016/S1080-8914(96)80031-7
   Google Scholar
• Keck RG. The use of t-butyl hydroperoxide as a probe for methionine oxidation in proteins. Anal Biochem 1996; 236:56 - 62; http://dx.doi.org/10.1006/abio.1996.0131; PMID: 8619496
   PubMed Web of Science ®Google Scholar
• Ji JA, Zhang B, Cheng W, Wang YJ. Methionine, tryptophan, and histidine oxidation in a model protein, PTH: mechanisms and stabilization. J Pharm Sci 2009; 98:4485 - 500; http://dx.doi.org/10.1002/jps.21746; PMID: 19455640
   PubMed Web of Science ®Google Scholar
• Edelman GM, Cunningham BA, Gall WE, Gottlieb PD, Rutishauser U, Waxdal MJ. The covalent structure of an entire gammaG immunoglobulin molecule. Proc Natl Acad Sci U S A 1969; 63:78 - 85; http://dx.doi.org/10.1073/pnas.63.1.78; PMID: 5257969
   PubMed Web of Science ®Google Scholar
• Pan H, Chen K, Chu L, Kinderman F, Apostol I, Huang G. Methionine oxidation in human IgG2 Fc decreases binding affinities to protein A and FcRn. Protein Sci 2009; 18:424 - 33; http://dx.doi.org/10.1002/pro.45; PMID: 19165723
   PubMed Web of Science ®Google Scholar
• Liu H, Gaza-Bulseco G, Zhou L. Mass spectrometry analysis of photo-induced methionine oxidation of a recombinant human monoclonal antibody. J Am Soc Mass Spectrom 2009; 20:525 - 8; http://dx.doi.org/10.1016/j.jasms.2008.11.011; PMID: 19103498
   PubMed Web of Science ®Google Scholar
• Liu H, Chumsae C, Gaza-Bulseco G, Hurkmans K, Radziejewski CH. Ranking the susceptibility of disulfide bonds in human IgG1 antibodies by reduction, differential alkylation, and LC-MS analysis. Anal Chem 2010; 82:5219 - 26; http://dx.doi.org/10.1021/ac100575n; PMID: 20491447
   PubMed Web of Science ®Google Scholar
• Harris RJ, Kabakoff B, Macchi FD, Shen FJ, Kwong M, Andya JD, Shire SJ, Bjork N, Totpal K, Chen AB. Identification of multiple sources of charge heterogeneity in a recombinant antibody. J Chromatogr B Biomed Sci Appl 2001; 752:233 - 45; http://dx.doi.org/10.1016/S0378-4347(00)00548-X; PMID: 11270864
   PubMed Web of Science ®Google Scholar
• Ryan MH, Petrone D, Nemeth JF, Barnathan E, Björck L, Jordan RE. Proteolysis of purified IgGs by human and bacterial enzymes in vitro and the detection of specific proteolytic fragments of endogenous IgG in rheumatoid synovial fluid. Mol Immunol 2008; 45:1837 - 46; http://dx.doi.org/10.1016/j.molimm.2007.10.043; PMID: 18157932
   PubMed Web of Science ®Google Scholar
• Liu D, Ren D, Huang H, Dankberg J, Rosenfeld R, Cocco MJ, Li L, Brems DN, Remmele RL Jr.. Structure and stability changes of human IgG1 Fc as a consequence of methionine oxidation. Biochemistry 2008; 47:5088 - 100; http://dx.doi.org/10.1021/bi702238b; PMID: 18407665
   PubMed Web of Science ®Google Scholar
• Gaza-Bulseco G, Faldu S, Hurkmans K, Chumsae C, Liu H. Effect of methionine oxidation of a recombinant monoclonal antibody on the binding affinity to protein A and protein G. J Chromatogr B Analyt Technol Biomed Life Sci 2008; 870:55 - 62; http://dx.doi.org/10.1016/j.jchromb.2008.05.045; PMID: 18567545
   PubMed Web of Science ®Google Scholar
• Bertolotti-Ciarlet A, Wang W, Lownes R, Pristatsky P, Fang Y, McKelvey T, Li Y, Li Y, Drummond J, Prueksaritanont T, et al. Impact of methionine oxidation on the binding of human IgG1 to Fc Rn and Fc γ receptors. Mol Immunol 2009; 46:1878 - 82; http://dx.doi.org/10.1016/j.molimm.2009.02.002; PMID: 19269032
   PubMed Web of Science ®Google Scholar
• Wang W, Vlasak J, Li Y, Pristatsky P, Fang Y, Pittman T, Roman J, Wang Y, Prueksaritanont T, Ionescu R. Impact of methionine oxidation in human IgG1 Fc on serum half-life of monoclonal antibodies. Mol Immunol 2011; 48:860 - 6; http://dx.doi.org/10.1016/j.molimm.2010.12.009; PMID: 21256596
   PubMed Web of Science ®Google Scholar
• Chumsae C, Gaza-Bulseco G, Sun J, Liu H. 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; 850:285 - 94; http://dx.doi.org/10.1016/j.jchromb.2006.11.050; PMID: 17182291
   PubMed Web of Science ®Google Scholar
• Kerwin BA, Remmele RL Jr.. Protect from light: photodegradation and protein biologics. J Pharm Sci 2007; 96:1468 - 79; http://dx.doi.org/10.1002/jps.20815; PMID: 17230445
   PubMed Web of Science ®Google Scholar
• Lam XM, Yang JY, Cleland JL. Antioxidants for prevention of methionine oxidation in recombinant monoclonal antibody HER2. J Pharm Sci 1997; 86:1250 - 5; http://dx.doi.org/10.1021/js970143s; PMID: 9383735
   PubMed Web of Science ®Google Scholar
• Li S, Schöneich C, Borchardt RT. Chemical instability of protein pharmaceuticals: Mechanisms of oxidation and strategies for stabilization. Biotechnol Bioeng 1995; 48:490 - 500; http://dx.doi.org/10.1002/bit.260480511; PMID: 18623513
   PubMed Web of Science ®Google Scholar
• Chu J-W, Yin J, Brooks BR, Wang DIC, Ricci MS, Brems DN, Trout BL. A comprehensive picture of non-site specific oxidation of methionine residues by peroxides in protein pharmaceuticals. J Pharm Sci 2004; 93:3096 - 102; http://dx.doi.org/10.1002/jps.20207; PMID: 15514984
   PubMed Web of Science ®Google Scholar
• Vlasak J, Ionescu R. Heterogeneity of monoclonal antibodies revealed by charge-sensitive methods. Curr Pharm Biotechnol 2008; 9:468 - 81; http://dx.doi.org/10.2174/138920108786786402; PMID: 19075686
   PubMed Web of Science ®Google Scholar
• Du Y, Walsh A, Ehrick R, Xu W, May K, Liu H. Chromatographic analysis of the acidic and basic species of recombinant monoclonal antibodies. MAbs 2012; 4:578 - 85; http://dx.doi.org/10.4161/mabs.21328; PMID: 22820257
   PubMed Web of Science ®Google Scholar
• Moorhouse KG, Nashabeh W, Deveney J, Bjork NS, Mulkerrin MG, Ryskamp T. Validation of an HPLC method for the analysis of the charge heterogeneity of the recombinant monoclonal antibody IDEC-C2B8 after papain digestion. J Pharm Biomed Anal 1997; 16:593 - 603; http://dx.doi.org/10.1016/S0731-7085(97)00178-7; PMID: 9502155
   PubMed Web of Science ®Google Scholar
• Vlasak J, Bussat MC, Wang S, Wagner-Rousset E, Schaefer M, Klinguer-Hamour C, Kirchmeier M, Corvaïa N, Ionescu R, Beck A. Identification and characterization of asparagine deamidation in the light chain CDR1 of a humanized IgG1 antibody. Anal Biochem 2009; 392:145 - 54; http://dx.doi.org/10.1016/j.ab.2009.05.043; PMID: 19497295
   PubMed Web of Science ®Google Scholar
• Lau H, Pace D, Yan B, McGrath T, Smallwood S, Patel K, Park J, Park SS, Latypov RF. Investigation of degradation processes in IgG1 monoclonal antibodies by limited proteolysis coupled with weak cation-exchange HPLC. J Chromatogr B Analyt Technol Biomed Life Sci 2010; 878:868 - 76; http://dx.doi.org/10.1016/j.jchromb.2010.02.003; PMID: 20206584
   PubMed Web of Science ®Google Scholar
• Kim J, Jones L, Taylor L, Kannan G, Jackson F, Lau H, Latypov RF, Bailey B. Characterization of a unique IgG1 mAb CEX profile by limited Lys-C proteolysis/CEX separation coupled with mass spectrometry and structural analysis. J Chromatogr B Analyt Technol Biomed Life Sci 2010; 878:1973 - 81; http://dx.doi.org/10.1016/j.jchromb.2010.05.032; PMID: 20554483
   PubMed Web of Science ®Google Scholar
• Pace AL, Wong RL, Zhang YT, Kao Y-H, Wang YJ. Asparagine deamidation dependence on buffer type, pH, and temperature. J Pharm Sci 2013; 102:1712 - 23; http://dx.doi.org/10.1002/jps.23529; PMID: 23568760
   PubMed Web of Science ®Google Scholar
• Huang L, Lu J, Wroblewski VJ, Beals JM, Riggin RM. In vivo deamidation characterization of monoclonal antibody by LC/MS/MS. Anal Chem 2005; 77:1432 - 9; http://dx.doi.org/10.1021/ac0494174; PMID: 15732928
   PubMed Web of Science ®Google Scholar
• Janin-Bussat M-C, Tonini L, Huillet C, Colas O, Klinguer-Hamour C, Corvaïa N, Beck A. Cetuximab Fab and Fc N-glycan fast characterization using IdeS digestion and liquid chromatography coupled to electrospray ionization mass spectrometry. Methods Mol Biol 2013; 988:93 - 113; http://dx.doi.org/10.1007/978-1-62703-327-5_7; PMID: 23475716
   PubMedGoogle Scholar
• Beck A, Diemer H, Ayoub D, Debaene F, Wagner-Rousset E, Carapito C, Van Dorsselaer A, Sanglier-Cianférani S. Analytical characterization of biosimilar antibodies and Fc-fusion proteins. Trends Analyt Chem 2013; 48:81 - 95; http://dx.doi.org/10.1016/j.trac.2013.02.014
   Web of Science ®Google Scholar