References
- Gokbuget N, Dombret H, Bonifacio M, Reichle A, Graux C, Faul C, Diedrich H, Topp MS, Bruggemann M, Horst HA, et al. Blinatumomab for minimal residual disease in adults with B-precursor acute lymphoblastic leukemia. Blood. 2018;131(14):1522–10. doi:https://doi.org/10.1182/blood-2017-08-798322.
- Kantarjian H, Stein A, Gokbuget N, Fielding AK, Schuh AC, Ribera JM, Wei A, Dombret H, Foa R, Bassan R, et al. Blinatumomab versus chemotherapy for advanced acute lymphoblastic leukemia. N Engl J Med. 2017;376(9):836–47. doi:https://doi.org/10.1056/NEJMoa1609783.
- Oldenburg J, Mahlangu JN, Kim B, Schmitt C, Callaghan MU, Young G, Santagostino E, Kruse-Jarres R, Negrier C, Kessler C, et al. Emicizumab prophylaxis in hemophilia A with inhibitors. N Engl J Med. 2017;377(9):809–18. doi:https://doi.org/10.1056/NEJMoa1703068.
- Labrijn AF, Janmaat ML, Reichert JM, Parren PWHI. Bispecific antibodies: a mechanistic review of the pipeline. Nat Rev Drug Discov. 2019;18(8):585–608. doi:https://doi.org/10.1038/s41573-019-0028-1.
- Kontermann RE. Dual targeting strategies with bispecific antibodies. MAbs. 2012;4(2):182–97. doi:https://doi.org/10.4161/mabs.4.2.19000.
- Brinkmann U, Kontermann RE. The making of bispecific antibodies. MAbs. 2017;9(2):182–212. doi:https://doi.org/10.1080/19420862.2016.1268307.
- Chames P, Baty D. Bispecific antibodies for cancer therapy: the light at the end of the tunnel? MAbs. 2009;1(6):539–47. doi:https://doi.org/10.4161/mabs.1.6.10015.
- Kontermann RE. Recombinant bispecific antibodies for cancer therapy. Acta Pharmacol Sin. 2005;26(1):1–9. doi:https://doi.org/10.1111/aphs.2005.26.issue-1.
- Baeuerle PA, Reinhardt C. Bispecific T-cell engaging antibodies for cancer therapy. Cancer Res. 2009;69(12):4941–44. doi:https://doi.org/10.1158/0008-5472.CAN-09-0547.
- Sasso EH, Silverman GJ, Mannik M. Human IgA and IgG F(ab’)2 that bind to staphylococcal protein A belong to the VHIII subgroup. J Immunol. 1991;147:1877–83.
- Garber K. Bispecific antibodies rise again. Nat Rev Drug Discov. 2014;13(11):799–801. doi:https://doi.org/10.1038/nrd4478.
- Taki S, Kamada H, Inoue M, Nagano K, Mukai Y, Higashisaka K, Yoshioka Y, Tsutsumi Y, Tsunoda S. A novel bispecific antibody against human CD3 and ephrin receptor A10 for breast cancer therapy. PLoS One. 2015;10(12):e0144712. doi:https://doi.org/10.1371/journal.pone.0144712.
- Dorken B, Riethmuller G, Kufer P, Lutterbuse R, Bargou R, Loffler A. CD19XCD3 specific polypeptides and uses thereof. United States patent US 7,575,923 B2. 2009.
- Mack M, Riethmuller G, Kufer P. A small bispecific antibody construct expressed as a functional single-chain molecule with high tumor cell cytotoxicity. Proc Natl Acad Sci USA. 1995;92(15):7021–25. doi:https://doi.org/10.1073/pnas.92.15.7021.
- Loffler A, Kufer P, Lutterbuse R, Zettl F, Daniel PT, Schwenkenbecher JM, Riethmuller G, Dorken B, Bargou RC. A recombinant bispecific single-chain antibody, CD19 X CD3, induces rapid and high lymphoma-directed cytotoxicity by unstimulated T lymphocytes. Blood. 2000;95(6):2098–103. doi:https://doi.org/10.1182/blood.V95.6.2098.
- Brischwein K, Schlereth B, Guller B, Steiger C, Wolf A, Lutterbuese R, Offner S, Locher M, Urbig T, Raum T, et al. MT110: A novel bispecific single-chain antibody construct with high efficacy in eradicating established tumors. Mol Immunol. 2006;43(8):1129–43. doi:https://doi.org/10.1016/j.molimm.2005.07.034.
- Pendzialek J, Roose K, Smet A, Schepens B, Kufer P, Raum T, Baeuerle PA, Muenz M, Saelens X, Fiers W. Bispecific T cell engaging antibody constructs targeting a universally conserved part of the viral M2 ectodomain cure and prevent influenza A virus infection. Antiviral Res. 2017;141:155–64. doi:https://doi.org/10.1016/j.antiviral.2017.02.016.
- Kufer P, Lutterbuse R, Kohleisen B, Zeman S, Bauerle P. Pharmaceutical compositions comprising bispecific anti-CD3, anti-CD-19 antibody constructs for the treatment of B-cell related disorders. United States patent US 7,635,472 B2. 2009.
- Spiesberger K, Paulfranz F, Egger A, Reiser J, Vogl C, Rudolf-Scholik J, Mayrhofer C, Grosse-Hovest L, Brem G. Large-scale purification of r28M: A bispecific scFv antibody targeting human melanoma produced in transgenic cattle. PLoS One. 2015;10(10):e0140471. doi:https://doi.org/10.1371/journal.pone.0140471.
- Grosse-Hovest L, Muller S, Minoia R, Wolf E, Zakhartchenko V, Wenigerkind H, Lassnig C, Besenfelder U, Muller M, Lytton SD, et al. Cloned transgenic farm animals produce a bispecific antibody for T cell-mediated tumor cell killing. Proc Natl Acad Sci USA. 2004;101(18):6858–63. doi:https://doi.org/10.1073/pnas.0308487101.
- Bjorck L, Protein L. A novel bacterial cell wall protein with affinity for Ig L chains. J Immunol. 1988;140:1194–97.
- Graille M, Stura EA, Housden NG, Beckingham JA, Bottomley SP, Beale D, Taussig MJ, Sutto BJ, Gore MG, Charbonnier JB. Complex between peptostreptococcus magnus protein L and a human antibody reveals structural convergence in the interaction modes of Fab binding proteins. Structure. 2001;9(8):679–87. doi:https://doi.org/10.1016/S0969-2126(01)00630-X.
- Nilson BH, Logdberg L, Kastern W, Bjorck L, Akerstrom B. Purification of antibodies using protein L-binding framework structures in the light chain variable domain. J Immunol Methods. 1993;164(1):33–40. doi:https://doi.org/10.1016/0022-1759(93)90273-A.
- Tustian AD, Endicott C, Adams B, Mattila J, Bak H. Development of purification processes for fully human bispecific antibodies based upon modification of protein A binding avidity. MAbs. 2016;8(4):828–38. doi:https://doi.org/10.1080/19420862.2016.1160192.
- Arakawa T, Philo JS, Tsumoto K, Yumioka R, Ejima D. Elution of antibodies from a Protein-A column by aqueous arginine solutions. Protein Expr Purif. 2004;36(2):244–48. doi:https://doi.org/10.1016/j.pep.2004.04.009.
- Ejima D, Yumioka R, Tsumoto K, Arakawa T. Effective elution of antibodies by arginine and arginine derivatives in affinity column chromatography. Anal Biochem. 2005;345(2):250–57. doi:https://doi.org/10.1016/j.ab.2005.07.004.
- Inoue N, Takai E, Arakawa T, Shiraki K. Specific decrease in solution viscosity of antibodies by arginine for therapeutic formulations. Mol Pharmaceutics. 2014;11(6):1889–96. doi:https://doi.org/10.1021/mp5000218.
- Tsumoto K, Umetsu M, Kumagai I, Ejima D, Philo JS, Arakawa T. Role of arginine in protein refolding, solubilization, and purification. Biotechnol Prog. 2004;20(5):1301–08. doi:https://doi.org/10.1021/bp0498793.
- Chen J, Liu Y, Wang Y, Ding H, Su Z. Different effects of L-arginine on protein refolding: suppressing aggregates of hydrophobic interaction, not covalent binding. Biotechnol Prog. 2008;24(6):1365–72. doi:https://doi.org/10.1002/btpr.93.
- Meingast C, Heldt CL. Arginine-enveloped virus inactivation and potential mechanisms. Biotechnol Prog. 2019;e2931.
- Chen C, Wakabayashi T, Muraoka M, Feng S, Chia WS, Chong CK, Ching TJ, Soehano I, Shimizu Y, Igawa T, et al. Controlled conductivity at low pH in Protein L chromatography enables separation of bispecific and other antibody formats by their binding valency. MAbs. 2019;11(4):632–38. doi:https://doi.org/10.1080/19420862.2019.1583996.
- Bolton GR, Selvitelli KR, Iliescu I, Cecchini DJ. Inactivation of viruses using novel protein A wash buffers. Biotechnol Prog. 2015;31(2):406–13. doi:https://doi.org/10.1002/btpr.2024.
- Shukla D, Trout BL. Interaction of arginine with proteins and the mechanism by which it inhibits aggregation. J Phys Chem B. 2010;114(42):13426–38. doi:https://doi.org/10.1021/jp108399g.
- Shukla D, Zamolo L, Cavallotti C, Trout BL. Understanding the role of arginine as an eluent in affinity chromatography via molecular computations. J Phys Chem B. 2011;115(11):2645–54. doi:https://doi.org/10.1021/jp111156z.
- Das U, Hariprasad G, Ethayathulla AS, Manral P, Das TK, Pasha S, Mann A, Ganguli M, Verma AK, Bhat R, et al. Inhibition of protein aggregation: supremolecular assemblies of arginine hold the key. PLoS One. 2007;2(11):e1176. doi:https://doi.org/10.1371/journal.pone.0001176.
- Sackett DL, Wolff J. Nile red as a polarity-sensitive fluorescent probe of hydrophobic protein surfaces. Anal Biochem. 1987;167(2):228–34. doi:https://doi.org/10.1016/0003-2697(87)90157-6.
- Fowler SD, Greenspan P. Application of nile red, a fluorescent hydrophobic probe, for the detection of neutral lipid deposits in tissue sections: comparison with oil red O. J Histochem Cytochem. 1985;33(8):833–36. doi:https://doi.org/10.1177/33.8.4020099.
- Sun S, Gallo C. Arginine derivative wash in protein purification using affinity chromatography. United States patent US 7,714,111 B2. 2010.
- Frauenschuh A, Bill K. Wash solution comprising arginine for the affinity chromatography step in antibody purification. United States patent US 2017/0,044,211 A1. 2017.
- QIAamp® Viral RNA. Mini handbook; March 2018. version. QIAGEN.
- Nian R, Zhang W, Tan L, Lee J, Bi X, Yang Y, Gan HT, Gagnon P. Advance chromatin extraction improves capture performance of protein A affinity chromatography. J Chromatogr A. 2016;1431:1–7. doi:https://doi.org/10.1016/j.chroma.2015.12.044.