Structure-based engineering of a novel CD3ε-targeting antibody for reduced polyreactivity

References

• Zhou S, Liu M, Ren F, Meng X, Yu J. The landscape of bispecific T cell engager in cancer treatment. Biomarker Res. 2021;9:38. doi:10.1186/s40364-021-00294-9. pmid = 34039409, pmcid = PMC8157659.
   PubMed Web of Science ®Google Scholar
• Baeuerle PA, Reinhardt C. Bispecific T-Cell engaging antibodies for cancer therapy. Cancer Res. 2009;69:4941–19. doi:10.1158/0008-5472.can-09-0547. pmid = 19509221.
   PubMed Web of Science ®Google Scholar
• Demaria O, Gauthier L, Debroas G, Vivier E. Natural killer cell engagers in cancer immunotherapy: next generation of immuno-oncology treatments. Eur J Immunol. 2021;51:1934–42mid = 34145579. doi:10.1002/eji.202048953.
   PubMed Web of Science ®Google Scholar
• Tian Z, Liu M, Zhang Y, Wang X. Bispecific T cell engagers: an emerging therapy for management of hematologic malignancies. J Hematol Oncol. 2021;14:75. doi:10.1186/s13045-021-01084-4. pmid = 33941237, pmcid = PMC8091790.
   PubMed Web of Science ®Google Scholar
• Bargou R, Leo E, Zugmaier G, Klinger M, Goebeler M, Knop S, Noppeney R, Viardot A, Hess G, Schuler M, et al. Tumor regression in cancer patients by very low doses of a T cell–Engaging antibody. Science. 2008;321:974–77mid = 18703743. doi:10.1126/science.1158545.
   PubMed Web of Science ®Google Scholar
• Kaplon H, Crescioli S, Chenoweth A, Reichert JV, Janice M. Antibodies to watch in 2023. mAbs. 2023. doi:10.1080/19420862.2022.2153410.
   PubMed Web of Science ®Google Scholar
• Ledbetter JA, Gentry LE, June CH, Rabinovitch PS, Purchio AF. Stimulation of T cells through the CD3/T-cell receptor complex: role of cytoplasmic calcium, protein kinase C translocation, and phosphorylation of pp60c-src in the activation pathway. Mol Cell Biol. 1987;7:650–56. doi:10.1128/mcb.7.2.650-656.1987. pmid = 2434833, pmcid = PMC365120.
   PubMed Web of Science ®Google Scholar
• Cibrián D, Sánchez-madrid F. CD69: from activation marker to metabolic gatekeeper. Eur J Immunol. 2017;47:946–53. doi:10.1002/eji.201646837. pmid = 28475283, pmcid = PMC6485631.
   PubMed Web of Science ®Google Scholar
• González-Amaro R, Cortés JR, Sánchez-Madrid F, Martín P. Is CD69 an effective brake to control inflammatory diseases? Trends Mol Med. 2013;19:625–32. doi:10.1016/j.molmed.2013.07.006. pmid = 23954168, pmcid = PMC4171681.
   PubMed Web of Science ®Google Scholar
• Li J, Stagg NJ, Johnston J, Harris MJ, Menzies SA, DiCara D, Clark V, Hristopoulos M, Cook R, Slaga D, et al. Membrane-Proximal epitope facilitates efficient T cell synapse formation by anti-FcRH5/CD3 and is a requirement for myeloma cell killing. Cancer Cell. 2017;31:383–95. pmid = 28262555, pmcid = PMC5357723. doi:10.1016/j.ccell.2017.02.001.
   PubMed Web of Science ®Google Scholar
• Razvag Y, Neve-Oz Y, Sajman J, Reches M, Sherman E. Nanoscale kinetic segregation of TCR and CD45 in engaged microvilli facilitates early T cell activation. Nat Commun. 2018;9:732. doi:10.1038/s41467-018-03127-w. pmid = 29467364, pmcid = PMC5821895.
   PubMed Web of Science ®Google Scholar
• Clynes RA, Desjarlais JR. Redirected T cell cytotoxicity in cancer therapy. Annu Rev Med. 2018;70:1–14mid = 30379598. doi:10.1146/annurev-med-062617-035821.
   PubMed Web of Science ®Google Scholar
• Hötzel I, Theil F-P, Bernstein LJ, Prabhu S, Deng R, Quintana L, Lutman J, Sibia R, Chan P, Bumbaca D, et al. A strategy for risk mitigation of antibodies with fast clearance. mAbs. 2012;4:753–60. pmid = 23778268, pmcid = PMC3502242. doi:10.4161/mabs.22189.
   PubMed Web of Science ®Google Scholar
• Jain T, Sun T, Durand S, Hall A, Houston NR, Nett JH, Sharkey B, Bobrowicz B, Caffry I, Yu Y, et al. Biophysical properties of the clinical-stage antibody landscape. Proceedings of the National Academy of Sciences. 2017; 114:944–49. doi:10.1073/pnas.1616408114, pmid = 28096333.
   Google Scholar
• Tessier PM, Jinkoji J, Cheng Y-C, Prentice JL, Lenhoff AM. Self-Interaction nanoparticle spectroscopy: a nanoparticle-based protein interaction assay. J Am Chem Soc. 2008;130:3106–12. doi:10.1021/ja077624q. pmid = 18271584.
   PubMed Web of Science ®Google Scholar
• Shehata L, Maurer DP, Wec AZ, Lilov A, Champney E, Sun T, Archambault K, Burnina I, Lynaugh H, Zhi X, et al. Affinity maturation enhances antibody specificity but compromises conformational stability. Cell Rep. 2019;28:3300–8.e3304mid = 31553901. doi:10.1016/j.celrep.2019.08.056.
   PubMed Web of Science ®Google Scholar
• Avery LB, Wade J, Wang M, Tam A, King A, Piche-Nicholas N, Kavosi MS, Penn S, Cirelli D, Kurz JC, et al. Establishing in vitro in vivo correlations to screen monoclonal antibodies for physicochemical properties related to favorable human pharmacokinetics. mAbs. 2017;10: pmid = 29271699, pmcid = PMC5825195. doi:10.1080/19420862.2017.1417718.
   PubMed Web of Science ®Google Scholar
• Kraft TE, Richter WF, Emrich T, Knaupp A, Schuster M, Wolfert A, Kettenberger H. Heparin chromatography as an in vitro predictor for antibody clearance rate through pinocytosis. mAbs. 2019;12:1683432. doi:10.1080/19420862.2019.1683432. pmid = 31769731, pmcid = PMC6927760.
   Web of Science ®Google Scholar
• Xu Y, Roach W, Sun T, Jain T, Prinz B, T-Y Y, Torrey J, Thomas J, Bobrowicz P, Vásquez M, et al. Addressing polyspecificity of antibodies selected from an in vitro yeast presentation system: a FACS-based, high-throughput selection and analytical tool. Protein Eng Design Select. 2013;26:663–70. pmid = 24046438. doi:10.1093/protein/gzt047.
   PubMed Web of Science ®Google Scholar
• Liu Y, Caffry I, Wu J, Geng SB, Jain T, Sun T, Reid F, Cao Y, Estep P, Yu Y, et al. High-throughput screening for developability during early-stage antibody discovery using self-interaction nanoparticle spectroscopy. mAbs. 2013;6:483–92. pmid = 24492294, pmcid = PMC3984336. doi:10.4161/mabs.27431.
   PubMed Web of Science ®Google Scholar
• Ausserwöger H, Schneider MM, Herling TW, Arosio P, Invernizzi G, Knowles TPJ, Lorenzen N. Non-specificity as the sticky problem in therapeutic antibody development. Nat Rev Chem. 2022:1–18. doi:10.1038/s41570-022-00438-x.
   PubMed Web of Science ®Google Scholar
• Cunningham O, Scott M, Zhou ZS, Finlay WJJ. Polyreactivity and polyspecificity in therapeutic antibody development: risk factors for failure in preclinical and clinical development campaigns. mAbs. 2021;13:1999195mid = 34780320. doi:10.1080/19420862.2021.1999195.
   Web of Science ®Google Scholar
• Mouquet H, Scheid JF, Zoller MJ, Krogsgaard M, Ott RG, Shukair S, Artyomov MN, Pietzsch J, Connors M, Pereyra F, et al. Polyreactivity increases the apparent affinity of anti-HIV antibodies by heteroligation. Nature. 2010;467:591–95. pmid = 20882016, pmcid = PMC3699875. doi:10.1038/nature09385.
   PubMed Web of Science ®Google Scholar
• Yadav R, Sukumaran S, Zabka TS, Li J, Oldendorp A, Morrow G, Reyes A, Cheu M, Li J, Wallin JJ, et al. Nonclinical pharmacokinetics and pharmacodynamics characterization of anti-CD79b/CD3 T Cell-Dependent bispecific antibody using a surrogate molecule: a potential therapeutic agent for B cell malignancies. Pharmaceutics. 2022;14:970. pmid = 35631556, pmcid = PMC9147001. doi:10.3390/pharmaceutics14050970.
   PubMed Web of Science ®Google Scholar
• Haber L, Olson K, Kelly MP, Crawford A, DiLillo DJ, Tavaré R, Ullman E, Mao S, Canova L, Sineshchekova O, et al. Generation of T-cell-redirecting bispecific antibodies with differentiated profiles of cytokine release and biodistribution by CD3 affinity tuning. Sci Rep. 2021;11:14397mid = 34257348. doi:10.1038/s41598-021-93842-0.
   PubMed Web of Science ®Google Scholar
• Mandikian D, Takahashi N, Lo AA, Li J, Eastham-Anderson J, Slaga D, Ho J, Hristopoulos M, Clark R, Totpal K, et al. Relative target affinities of T-Cell–dependent bispecific antibodies determine biodistribution in a solid tumor mouse model. Mol Cancer Ther. 2018;17:molcanther.0657.2017. pmid = 29339550. doi:10.1158/1535-7163.mct-17-0657.
   PubMed Web of Science ®Google Scholar
• Poussin M, Sereno A, Wu X, Huang F, Manro J, Cao S, Carpenito C, Glasebrook A Jr, Demarest S, Demarest SJ. Dichotomous impact of affinity on the function of T cell engaging bispecific antibodies. J ImmunoTher Cancer. 2021;9:e002444. pmid = 34253637, pmcid = PMC8276301. doi:10.1136/jitc-2021-002444.
   PubMedGoogle Scholar
• Staflin K, Zafra CLZD, Schutt LK, Clark V, Zhong F, Hristopoulos M, Clark R, Li J, Mathieu M, Chen X, et al. Target arm affinities determine preclinical efficacy and safety of anti-HER2/CD3 bispecific antibody. JCI Insight. 2020;5:e133757. pmid = 32271166, pmcid = PMC7205277. doi:10.1172/jci.insight.133757.
   PubMed Web of Science ®Google Scholar
• Bortoletto N, Scotet E, Myamoto Y, D’oro U, Lanzavecchia A. Optimizing anti-cd3 affinity for effective T cell targeting against tumor cells. Eur J Immunol. 2002;32:3102–07. doi:10.1002/1521-4141(200211)32:11<3102:aid-immu3102>3.0.co;2-c. pmid = 12385030.
   PubMed Web of Science ®Google Scholar
• Ellerman D. Bispecific T-cell engagers: towards understanding variables influencing the in vitro potency and tumor selectivity and their modulation to enhance their efficacy and safety. Methods. 2019;154:102–17. pmid = 30395966. doi:10.1016/j.ymeth.2018.10.026.
   PubMed Web of Science ®Google Scholar
• Zorn JA, Wheeler ML, Barnes RM, Kaberna J, Morishige W, Harris M, Huang RYC, Lohre J, Chang YC, Chau B, et al. Humanization of a strategic CD3 epitope enables evaluation of clinical T-cell engagers in a fully immunocompetent in vivo model. Sci Rep. 2022;12:3530mid = 35241687. doi:10.1038/s41598-022-06953-7.
   Web of Science ®Google Scholar
• Camacho CJ, Kimura SR, DeLisi C, Vajda S. Kinetics of Desolvation-Mediated Protein–Protein Binding. Biophys J. 2000;78:1094–105. doi:10.1016/s0006-3495(00)76668-9. pmid = 10692300, pmcid = PMC1300713.
   PubMed Web of Science ®Google Scholar
• Bogan AA, Thorn KS. Anatomy of hot spots in protein interfaces11edited by J. Wells. J Mol Biol. 1998;280:1–9. doi:10.1006/jmbi.1998.1843. pmid = 9653027.
   PubMed Web of Science ®Google Scholar
• The antibody society. Therapeutic monoclonal antibodies approved or in regulatory review. [accessed June 15, 2020].
   Google Scholar
• Chen Xiaocheng, Dennis Mark S, Ebens, Jr Allen J, Junttila, Teemu T, Kelley Robert F, Mathieu Mary A, Sun Liping L. 2015. Anti-CD3 antibodies and methods of use. US10174124B2.
   Google Scholar
• Datta-Mannan A, Lu J, Witcher DR, Leung D, Tang Y, Wroblewski VJ. The interplay of non-specific binding, target-mediated clearance and FcRn interactions on the pharmacokinetics of humanized antibodies. mAbs. 2015;7:1084–93. doi:10.1080/19420862.2015.1075109. pmid = 26337808, pmcid = PMC4966429.
   PubMed Web of Science ®Google Scholar
• Igawa T, Tsunoda H, Tachibana T, Maeda A, Mimoto F, Moriyama C, Nanami M, Sekimori Y, Nabuchi Y, Aso Y, et al. Reduced elimination of IgG antibodies by engineering the variable region. Protein Eng Design Select. 2010;23:385–92mid = 20159773. doi:10.1093/protein/gzq009.
   PubMed Web of Science ®Google Scholar
• Li B, Tesar D, Boswell CA, Cahaya HS, Wong A, Zhang J, Meng YG, Eigenbrot C, Pantua H, Diao J, et al. Framework selection can influence pharmacokinetics of a humanized therapeutic antibody through differences in molecule charge. mAbs. 2014;6:1255–64. pmid = 25517310, pmcid = PMC4623330. doi:10.4161/mabs.29809.
   PubMed Web of Science ®Google Scholar
• Adams PD, Afonine PV, Bunkóczi G, Chen VB, Davis IW, Echols N, Headd JJ, Hung LW, Kapral GJ, Grosse-Kunstleve RW, et al.Zwart\it PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallographica Section D. 2010; 66:213–21. doi:10.1107/S0907444909052925.
   Google Scholar
• Emsley Bl P, Scott WG, Cowtan K, Cowtan K. Features and development of Coot. Acta Crystal Sec D. 2010;66:486–501. doi:10.1107/S0907444910007493.
   PubMedGoogle Scholar
• Emsley P, Cowtan K. Cowtan PEaK.\it Coot: model-building tools for molecular graphics. Acta Crystal Sec D. 2004;60:2126–32. doi:10.1107/S0907444904019158.
   PubMed Web of Science ®Google Scholar
• McCoy RWG-K AJ, Adams PD, Winn MD, Storoni LC, Storoni LC, Read RJ. Phaser crystallographic software. J App Crystal. 2007;40:658–74. doi:10.1107/S0021889807021206.
   PubMed Web of Science ®Google Scholar
• Yu Y, Schürpf T, Springer TA. How Natalizumab Binds and Antagonizes α4 Integrins*. J Biol Chem. 2013;288:32314–25. doi:10.1074/jbc.m113.501668. pmid = 24047894.
   PubMed Web of Science ®Google Scholar
• Sheffler W, Baker D. RosettaHoles: rapid assessment of protein core packing for structure prediction, refinement, design, and validation. Protein Sci. 2009;18:229–39. doi:10.1002/pro.8. pmid = 19177366, pmcid = PMC2708028.
   PubMed Web of Science ®Google Scholar
• Kjer-Nielsen L, Dunstone MA, Kostenko L, Ely LK, Beddoe T, Mifsud NA, Purcell AW, Brooks AG, McCluskey J, Rossjohn J Crystal structure of the human T cell receptor CD3εγ heterodimer complexed to the therapeutic mAb OKT3. Proceedings of the National Academy of Sciences. 2004; 101:7675–80. doi:10.1073/pnas.0402295101, pmid = 15136729, pmcid = PMC419665.
   Google Scholar
• Arnett KL, Harrison SC, Wiley DC Crystal structure of a human CD3-ε/δ dimer in complex with a UCHT1 single-chain antibody fragment. Proceedings of the National Academy of Sciences of the United States of America. 2004; 101:16268–73. doi:10.1073/pnas.0407359101, pmid = 15534202.
   Google Scholar
• Dong D, Zheng L, Lin J, Zhang B, Zhu Y, Li N, Xie S, Wang Y, Gao N, Huang Z. Structural basis of assembly of the human T cell receptor–cd3 complex. Nature. 2019;573:546–52mid = 31461748. doi:10.1038/s41586-019-1537-0.
   PubMed Web of Science ®Google Scholar
• Sušac L, Vuong MT, Thomas C, Bülow Sv OB, Santos C, Am FR, Hummer G, Tampé R, Davis SJ, Davis SJ. Structure of a fully assembled tumor-specific T cell receptor ligated by pMHC. Cell. 2022;185:3201–13.e3219. doi:10.1016/j.cell.2022.07.010.
   PubMed Web of Science ®Google Scholar
• Chen Y, Zhu Y, Li X, Gao W, Zhen Z, Dong D, Huang B, Ma Z, Zhang A, Song X, et al. Cholesterol inhibits TCR signaling by directly restricting TCR-CD3 core tunnel motility. Mol Cell. 2022;82:1278–87.e1275mid = 35271814. doi:10.1016/j.molcel.2022.02.017.
   PubMed Web of Science ®Google Scholar
• Jurrus E, Engel D, Star K, Monson K, Brandi J, Felberg LE, Brookes DH, Wilson L, Chen J, Liles K, et al. Improvements to the APBS biomolecular solvation software suite. Protein Sci. 2018;27:112–28. pmid = 28836357, pmcid = PMC5734301, eprint = 1707.00027. doi:10.1002/pro.3280.
   PubMed Web of Science ®Google Scholar
• Liu YD, Goetze AM, Bass RB, Flynn GC. N-terminal Glutamate to Pyroglutamate Conversion in vivo for Human IgG2 Antibodies. J Biol Chem. 2011;286:11211–17. doi:10.1074/jbc.m110.185041. pmid = 21282104, pmcid = PMC3064176.
   PubMed Web of Science ®Google Scholar
• Leong SR, Sukumaran S, Hristopoulos M, Totpal K, Stainton S, Lu E, Wong A, Tam L, Newman R, Vuillemenot BR, et al. An anti-CD3/anti–CLL-1 bispecific antibody for the treatment of acute myeloid leukemia. Blood. 2017;129:609–18. doi:10.1182/blood-2016-08-735365. pmid = 27908880, pmcid = PMC5290988.
   PubMed Web of Science ®Google Scholar
• Yadav S, Laue TM, Kalonia DS, Singh SN, Shire SJ. The influence of charge distribution on self-Association and viscosity behavior of monoclonal antibody solutions. Mol Pharm. 2012;9:791–802mid = 22352470. doi:10.1021/mp200566k.
   PubMed Web of Science ®Google Scholar
• Birtalan S, Zhang Y, Fellouse FA, Shao L, Schaefer G, Sidhu SS. The intrinsic contributions of tyrosine, serine, glycine and arginine to the affinity and specificity of antibodies. J Mol Biol. 2008;377:1518–28. doi:10.1016/j.jmb.2008.01.093. pmid = 18336836.
   PubMed Web of Science ®Google Scholar
• DeKosky BJ, Lungu OI, Park D, Johnson EL, Charab W, Chrysostomou C, Kuroda D, Ellington AD, Ippolito GC, Gray JJ, et al. Large-scale sequence and structural comparisons of human naive and antigen-experienced antibody repertoires. Proceedings of the National Academy of Sciences. 2016; 113:E2636–45. doi:10.1073/pnas.1525510113, pmid = 27114511, pmcid = PMC4868480.
   Google Scholar
• Sheinerman FB, Norel R, Honig B. Electrostatic aspects of protein–protein interactions. Curr Opin Struct Biol. 2000;10:153–59. doi:10.1016/s0959-440x(00)00065-8. pmid = 10753808.
   PubMed Web of Science ®Google Scholar
• Marvin JS, Lowman HB. Redesigning an antibody fragment for faster association with its antigen. Biochemistry. 2003;42:7077–83mid = 12795603. doi:10.1021/bi026947q.
   PubMed Web of Science ®Google Scholar
• Gabdoulline RR, Wade RC. Biomolecular diffusional association. Curr Opin Struct Biol. 2002;12:204–13mid = 11959498. doi:10.1016/s0959-440x(02)00311-1.
   PubMed Web of Science ®Google Scholar
• Bugelski PJ, Achuthanandam R, Capocasale RJ, Treacy G, Bouman-Thio E. Monoclonal antibody-induced cytokine-release syndrome. Expert Rev Clin Immunol. 2009;5:499–521. doi:10.1586/eci.09.31. pmid = 20477639.
   PubMed Web of Science ®Google Scholar
• Dudgeon K, Rouet R, Kokmeijer I, Schofield P, Stolp J, Langley D, Stock D, Christ D General strategy for the generation of human antibody variable domains with increased aggregation resistance. Proceedings of the National Academy of Sciences. 2012; 109:10879–84. doi:10.1073/pnas.1202866109, pmid = 22745168, pmcid = PMC3390889.
   Google Scholar
• Perchiacca JM, Ladiwala ARA, Bhattacharya M, Tessier PM. Aggregation-resistant domain antibodies engineered with charged mutations near the edges of the complementarity-determining regions. Protein Eng Design Select. 2012;25:591–602mid = 22843678. doi:10.1093/protein/gzs042.
   PubMed Web of Science ®Google Scholar
• Wec AZ, Wrapp D, Herbert AS, Maurer DP, Haslwanter D, Sakharkar M, Jangra RK, Dieterle ME, Lilov A, Huang D, et al. Broad neutralization of SARS-related viruses by human monoclonal antibodies. Science. 2020;369:731–36mid = 32540900. doi:10.1126/science.abc7424.
   PubMed Web of Science ®Google Scholar
• Akari H, Nam K-H, Mori K, Otani I, Shibata H, Adachi A, Terao K, Yoshikawa Y. Effects of SIVmac Infection on Peripheral Blood CD4+CD8+T Lymphocytes in Cynomolgus Macaques. Clin Immun. 1999;91:321–29mid = 10370378. doi:10.1006/clim.1999.4700.
   PubMed Web of Science ®Google Scholar
• Sakharkar M, Rappazzo CG, Wieland-Alter WF, Hsieh C-L, Wrapp D, Esterman ES, Kaku CI, Wec AZ, Geoghegan JC, McLellan JS, et al. Prolonged evolution of the human B cell response to SARS-CoV-2 infection. Sci Immun. 2021;6:eabg6916. pmid = 33622975, pmcid = PMC8128290. doi:10.1126/sciimmunol.abg6916.
   PubMed Web of Science ®Google Scholar
• Myszka DG. Improving biosensor analysis. J Mol Recogn. 1999;12:279–84. doi:10.1002/(sici)1099-1352(199909/10)12:5<279:aid-jmr473>3.0.co;2-3. pmid = 10556875.
   PubMed Web of Science ®Google Scholar
• Sule Shantanu V, Sukumar M, Weiss William F, Marcelino-Cruz Anna M, Sample T, Tessier Peter M. High-Throughput analysis of concentration-Dependent antibody self-Association. Biophys J. 2011;101:1749–57. doi:10.1016/j.bpj.2011.08.036. pmid = 21961601, pmcid = PMC3183799.
   PubMed Web of Science ®Google Scholar
• Kelly RL, Geoghegan JC, Feldman J, Jain T, Kauke M, Le D, Zhao J, Wittrup KD. Chaperone proteins as single component reagents to assess antibody nonspecificity. mAbs. 2017;9:1036–40. doi:10.1080/19420862.2017.1356529. pmid = 28745541, pmcid = PMC5627595.
   PubMed Web of Science ®Google Scholar
• Kozlowski LP. IPC – Isoelectric point calculator. Biol Direct. 2016;11:55. doi:10.1186/s13062-016-0159-9. pmid = 27769290, pmcid = PMC5075173.
   PubMed Web of Science ®Google Scholar
• EMBOSS. Date.
   Google Scholar
• Evans PR, Murshudov GN, GN EPaM. How good are my data and what is the resolution? Acta Crystal Sec D. 2013;69:1204–14. doi10.1107/S0907444913000061.
   PubMedGoogle Scholar
• Kabsch W. It XDS. Acta crystallographica section D. Acta Crystallogr D Biol Crystallogr. 2010;66(2):125–32. doi:10.1107/S0907444909047337.
   PubMedGoogle Scholar
• Vonrhein C, Cf PK, Sharff O, Smart A, Paciorek T, Womack W, Bricogne G, Bricogne G. Data processing and analysis with the autoPROC toolbox. Acta Crystal Sec D. 2011;67:293–302. doi:10.1107/S0907444911007773.
   PubMedGoogle Scholar
• He F, Woods CE, Becker GW, Narhi LO, Razinkov VI., Razinkov VI. High-throughput assessment of thermal and colloidal stability parameters for monoclonal antibody formulations. J Pharm Sci. 2011;100:5126–41. doi:10.1002/jps.22712.
   PubMed Web of Science ®Google Scholar
• Rappazzo CG, Tse LV, Kaku CI, Wrapp D, Sakharkar M, Huang D, Deveau LM, Yockachonis TJ, Herbert AS, Battles MB, et al. Broad and potent activity against SARS-like viruses by an engineered human monoclonal antibody. Science. pp.eabf4830. 2021. doi:10.1126/science.abf4830
   Web of Science ®Google Scholar
• Stein C, Pejchal R, Mccreary J, Barlow K, Sivasubramanian A, Battles MB inventors; Adimab; WO2022150785A2s assignee.^assignees. variant Ch3 Domains engineered for preferential Ch3 heterodimerization, multi-Specific antibodies comprising the same, and methods of making thereof.
   Google Scholar
• Barlow K, Sivasubramanian A, Battles MB inventors; Adimab; WO2022150787A2s assignee.^assignees. Variant Ch1 Domains and Variant Cl Domains engineered for preferential chain pairing and multi-specific antibodies comprising the same.
   Google Scholar
• Sharkey B, Pudi S, Moyer IW, Zhong L, Prinz B, Baruah H, Lynaugh H, Kumar S, Wittrup KD, Nett JH. Purification of common light chain IgG-like bispecific antibodies using highly linear pH gradients. mAbs. 2017;9:257–68. doi:10.1080/19420862.2016.1267090. pmid = 27937066, pmcid = PMC5297495.
   PubMed Web of Science ®Google Scholar