Identification and quantitation of hinge cysteinylation on endogenous IgG2 antibodies from human serum

References

• Smith SL. Ten years of orthoclone OKT3 (Muromonab-CD3): a review. J Transpl Coord. 1996;6(3):109–9. doi:https://doi.org/10.1177/090591999600600304.
   PubMedGoogle Scholar
• Reichert JM, Rosensweig CJ, Faden LB, Dewitz MC. Monoclonal antibody successes in the clinic. Nat Biotechnol. 2005;23(9):1073–78. doi:https://doi.org/10.1038/nbt0905-1073.
   PubMed Web of Science ®Google Scholar
• Newsome BW, Ernstoff MS. The clinical pharmacology of therapeutic monoclonal antibodies in the treatment of malignancy; have the magic bullets arrived? Br J Clin Pharmacol. 2008;66(1):6–19. doi:https://doi.org/10.1111/j.1365-2125.2008.03187.x.
   PubMedGoogle Scholar
• Brekke OH, Sandlie I. Therapeutic antibodies for human diseases at the dawn of the twenty-first century. Nat Rev Drug Discov. 2003;2(1):52–62. doi:https://doi.org/10.1038/nrd984.
   PubMed Web of Science ®Google Scholar
• Vlasak J, Ionescu R. Fragmentation of monoclonal antibodies. mAbs. 2011;3(3):253–63. doi:https://doi.org/10.4161/mabs.3.3.15608.
   PubMed Web of Science ®Google Scholar
• Goswami S, Wang W, Arakawa T, Ohtake S. Developments and challenges for MAb-based therapeutics. Antibodies. 2013;2(4):452–500. doi:https://doi.org/10.3390/antib2030452.
   Google Scholar
• Shire SJ. Stability of monoclonal antibodies (mAbs). Monoclonal Antibodies: meeting the challenges in manufacturing, formulation, delivery and stability of final drug product. Cambridge (UK): Woodhead Publishing; 2015. p. 45–92.
   Google Scholar
• Cromwell MEM, Hilario E, Jacobson F. Protein aggregation and bioprocessing. Aaps J. 2006;8(3):1–8. doi:https://doi.org/10.1208/aapsj080366.
   Google Scholar
• Goulet DR, Atkins WM. Considerations for the design of antibody-based therapeutics. J Pharm Sci. 2019;109(1):74–103.
   PubMed Web of Science ®Google Scholar
• Vázquez-Rey M, Lang DA. Aggregates in monoclonal antibody manufacturing processes. Biotechnol Bioeng. 2011;108(7):1494–508. doi:https://doi.org/10.1002/bit.23155.
   PubMed Web of Science ®Google Scholar
• Jenkins N. Modifications of therapeutic proteins: challenges and prospects. Cytotechnology. 2007;53:121–25.
   PubMed Web of Science ®Google Scholar
• Xu Y, Wang D, Mason B, Rossomando T, Li N, Liu D, Cheung JK, Xu W, Raghava S, Katiyar A, et al. Structure, heterogeneity and developability assessment of therapeutic antibodies. mAbs. 2019;11(2):239–64. doi:https://doi.org/10.1080/19420862.2018.1553476.
   PubMed Web of Science ®Google Scholar
• Liu H, Ponniah G, Zhang HM, Nowak C, Neill A, Gonzalez-Lopez N, Patel R, Cheng G, Kita AZ, Andrien B. In vitro and in vivo modifications of recombinant and human IgG antibodies. mAbs. 2014;6(5):1145–54. doi:https://doi.org/10.4161/mabs.29883.
   PubMed Web of Science ®Google Scholar
• Beck A, Liu H. Macro- and micro-heterogeneity of natural and recombinant IgG antibodies. Antibodies. 2019;8(1):18. doi:https://doi.org/10.3390/antib8010018.
   Web of Science ®Google Scholar
• Kita A, Ponniah G, Nowak C, Liu H. Characterization of cysteinylation and trisulfide bonds in a recombinant monoclonal antibody. Anal Chem. 2016;88(10):5430–37. doi:https://doi.org/10.1021/acs.analchem.6b00822.
   PubMed Web of Science ®Google Scholar
• Neill A, Nowak C, Patel R, Ponniah G, Gonzalez N, Miano D, Liu H. Characterization of recombinant monoclonal antibody charge variants using OFFGEL fractionation, weak anion exchange chromatography, and mass spectrometry. Anal Chem. 2015;87(12):6204–11. doi:https://doi.org/10.1021/acs.analchem.5b01452.
   PubMed Web of Science ®Google Scholar
• Wypych J, Li M, Guo A, Zhang Z, Martinez T, Allen MJ, Fodor S, Kelner DN, Flynn GC, Liu YD, et al. Human IgG2 antibodies display disulfide-mediated structural isoforms. J Biol Chem. 2008;283(23):16194–205. doi:https://doi.org/10.1074/jbc.M709987200.
   PubMed Web of Science ®Google Scholar
• Dillon TM, Ricci MS, Vezina C, Flynn GC, Liu YD, Rehder DS, Plant M, Henkle B, Li Y, Deechongkit S, et al. Structural and functional characterization of disulfide isoforms of the human IgG2 subclass. J Biol Chem. 2008;283(23):16206–15. doi:https://doi.org/10.1074/jbc.M709988200.
   PubMed Web of Science ®Google Scholar
• Liu YD, Chen X, Van Enk JZ, Plant M, Dillon TM, Flynn GC. Human IgG2 antibody disulfide rearrangement in vivo. J Biol Chem. 2008;283(43):29266–72. doi:https://doi.org/10.1074/jbc.M804787200.
   PubMed Web of Science ®Google Scholar
• Zhang Q, Schenauer MR, McCarter JD, Flynn GC. IgG1 thioether bond formation in vivo. J Biol Chem. 2013;288(23):16371–82. doi:https://doi.org/10.1074/jbc.M113.468397.
   PubMed Web of Science ®Google Scholar
• Zhang Q, Flynn GC. Cysteine racemization on igg heavy and light chains. J Biol Chem. 2013;288(48):34325–35. doi:https://doi.org/10.1074/jbc.M113.506915.
   PubMed Web of Science ®Google Scholar
• Gu S, Wen D, Weinreb PH, Sun Y, Zhang L, Foley SF, Kshirsagar R, Evans D, Mi S, Meier W, et al. Characterization of trisulfide modification in antibodies. Anal Biochem. 2010;400(1):89–98. doi:https://doi.org/10.1016/j.ab.2010.01.019.
   PubMed Web of Science ®Google Scholar
• Huh JH, White AJ, Brych SR, Franey H, Matsumura M. The identification of free cysteine residues within antibodies and a potential role for free cysteine residues in covalent aggregation because of agitation stress. J Pharm Sci. 2013;102(6):1701–11. doi:https://doi.org/10.1002/jps.23505.
   PubMed Web of Science ®Google Scholar
• Schmid I, Bonnington L, Gerl M, Bomans K, Thaller AL, Wagner K, Schlothauer T, Falkenstein R, Zimmermann B, Kopitz J, et al. Assessment of susceptible chemical modification sites of trastuzumab and endogenous human immunoglobulins at physiological conditions. Commun Biol. 2018;1(1). doi:https://doi.org/10.1038/s42003-018-0032-8.
   Google Scholar
• Schroeder HW, Cavacini L. Structure and function of immunoglobulins. J Allergy Clin Immunol. 2010;125(3):197–218. doi:https://doi.org/10.1016/j.jaci.2009.09.046.
   Google Scholar
• Di Giuseppe D, Frosali S, Priora R, Di Simplicio FC, Buonocore G, Cellesi C, Capecchi PL, Pasini FL, Lazzerini PE, Jakubowski H, et al. The effects of age and hyperhomocysteinemia on the redox forms of plasma thiols. J Lab Clin Med. 2004;144(5):235–45. doi:https://doi.org/10.1016/j.lab.2004.06.006.
   PubMedGoogle Scholar
• Rossi R, Giustarini D, Milzani A, Dalle-Donne I. Cysteinylation and homocysteinylation of plasma protein thiols during ageing of healthy human beings. J Cell Mol Med. 2009;13:3131–40.
   PubMed Web of Science ®Google Scholar
• Carballal S, Radi R, Kirk MC, Barnes S, Freeman BA, Alvarez B. Sulfenic acid formation in human serum albumin by hydrogen peroxide and peroxynitrite. Biochemistry. 2003;42(33):9906–14. doi:https://doi.org/10.1021/bi027434m.
   PubMed Web of Science ®Google Scholar
• Nakashima F, Shibata T, Kamiya K, Yoshitake J, Kikuchi R, Matsushita T, Ishii I, Giménez-Bastida JA, Schneider C, Uchida K. Structural and functional insights into S-thiolation of human serum albumins. Sci Rep. 2018;8(1):1–12. doi:https://doi.org/10.1038/s41598-018-19610-9.
   PubMedGoogle Scholar
• Sotgia S, Carru C, Pinna GA, Deiana L, Zinellu A. D-penicillamine Interferes with S-homocysteinylation and S-cysteinylation of LDL apolipoprotein B. J Clin Pharmacol. 2011;51(12):1728–32. doi:https://doi.org/10.1177/0091270010385933.
   PubMedGoogle Scholar
• Gonzalez-Quintela A, Alende R, Gude F, Campos J, Rey J, Meijide LM, Fernandez-Merino C, Vidal C. Serum levels of immunoglobulins (IgG, IgA, IgM) in a general adult population and their relationship with alcohol consumption, smoking and common metabolic abnormalities. Clin Exp Immunol. 2008;151(1):42–50. doi:https://doi.org/10.1111/j.1365-2249.2007.03545.x.
   PubMed Web of Science ®Google Scholar