Infliximab crystal structures reveal insights into self-association

References

• Rosenberg AS. Effects of protein aggregates: An immunologic perspective. AAPS J 2006; 8:E501-7; PMID:17025268; https://doi.org/10.1208/aapsj080359
   PubMed Web of Science ®Google Scholar
• Fang Y, Gao S, Tai D, Middaugh CR, Fang J. Identification of properties important to protein aggregation using feature selection. BMC Bioinformatics 2013; 14:314; PMID:24165390; https://doi.org/10.1186/1471-2105-14-314
   PubMed Web of Science ®Google Scholar
• Fernandez-Escamilla AM, Rousseau F, Schymkowitz J, Serrano L. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat Biotechnol 2004; 22:1302-6; PMID:15361882; https://doi.org/10.1038/nbt1012
   PubMed Web of Science ®Google Scholar
• Tartaglia GG, Cavalli A, Pellarin R, Caflisch A. Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences. Protein Sci 2005; 14:2723-34; PMID:16195556; https://doi.org/10.1110/ps.051471205
   PubMed Web of Science ®Google Scholar
• Fekete S, Beck A, Veuthey JL, Guillarme D. Theory and practice of size exclusion chromatography for the analysis of protein aggregates. J Pharm Biomed Anal 2014; 101:161-73; PMID:24816223; https://doi.org/10.1016/j.jpba.2014.04.011
   PubMed Web of Science ®Google Scholar
• Krayukhina E, Uchiyama S, Nojima K, Okada Y, Hamaguchi I, Fukui K. Aggregation analysis of pharmaceutical human immunoglobulin preparations using size-exclusion chromatography and analytical ultracentrifugation sedimentation velocity. J Biosci Bioeng 2013; 115:104-10; PMID:22925901; https://doi.org/10.1016/j.jbiosc.2012.07.021
   PubMed Web of Science ®Google Scholar
• Oliva A, Farina JB, Llabres M. Pre-study and in-study validation of a size-exclusion chromatography method with different detection modes for the analysis of monoclonal antibody aggregates. J Chromatogr B Analyt Technol Biomed Life Sci 2016; 1022:206-12; PMID:27107247; https://doi.org/10.1016/j.jchromb.2016.04.022
   PubMed Web of Science ®Google Scholar
• Courtois F, Schneider CP, Agrawal NJ, Trout BL. Rational design of biobetters with enhanced stability. J Pharm Sci 2015; 104:2433-40; PMID:26096711; https://doi.org/10.1002/jps.24520
   PubMed Web of Science ®Google Scholar
• Uchiyama S. Liquid formulation for antibody drugs. Biochim Biophys Acta 2014; 1844:2041-52; PMID:25131621; https://doi.org/10.1016/j.bbapap.2014.07.016
   PubMed Web of Science ®Google Scholar
• Kalonia C, Toprani V, Toth R, Wahome N, Gabel I, Middaugh CR, Volkin DB. Effects of protein conformation, apparent solubility, and protein-protein interactions on the rates and mechanisms of aggregation for an IgG1Monoclonal antibody. J Phys Chem B 2016; 120:7062-75; PMID:27380437; https://doi.org/10.1021/acs.jpcb.6b03878
   PubMed Web of Science ®Google Scholar
• Plath F, Ringler P, Graff-Meyer A, Stahlberg H, Lauer ME, Rufer AC, Graewert MA, Svergun D, Gellermann G, Finkler C, et al. Characterization of mAb dimers reveals predominant dimer forms common in therapeutic mAbs. mAbs 2016; 8:928-40; PMID:27031922; https://doi.org/10.1080/19420862.2016.1168960
   PubMed Web of Science ®Google Scholar
• Skamris T, Tian X, Thorolfsson M, Karkov HS, Rasmussen HB, Langkilde AE, Vestergaard B. Monoclonal antibodies follow distinct aggregation pathways during production-relevant acidic incubation and neutralization. Pharm Res 2016; 33:716-28; PMID:26563206; https://doi.org/10.1007/s11095-015-1821-0
   PubMed Web of Science ®Google Scholar
• Liu B, Guo H, Xu J, Qin T, Xu L, Zhang J, Guo Q, Zhang D, Qian W, Li B, et al. Acid-induced aggregation propensity of nivolumab is dependent on the Fc. mAbs 2016; 8:1107-17; PMID:27310175; https://doi.org/10.1080/19420862.2016.1197443
   PubMed Web of Science ®Google Scholar
• Tian X, Langkilde AE, Thorolfsson M, Rasmussen HB, Vestergaard B. Small-angle x-ray scattering screening complements conventional biophysical analysis: Comparative structural and biophysical analysis of monoclonal antibodies IgG1, IgG2, and IgG4. J Pharm Sci 2014; 103:1701-10; PMID:24700358; https://doi.org/10.1002/jps.23964
   PubMed Web of Science ®Google Scholar
• Zhang H, Cui W, Gross ML. Mass spectrometry for the biophysical characterization of therapeutic monoclonal antibodies. FEBS Lett 2014; 588:308-17; PMID:24291257; https://doi.org/10.1016/j.febslet.2013.11.027
   PubMed Web of Science ®Google Scholar
• Gupta AK, Skinner AR. A review of the use of infliximab to manage cutaneous dermatoses. J Cutan Med Surg 2004; 8:77-89; PMID:15685387; https://doi.org/10.1177/120347540400800202
   PubMed Web of Science ®Google Scholar
• Knight DM, Trinh H, Le J, Siegel S, Shealy D, McDonough M, Scallon B, Moore MA, Vilcek J, Daddona P, et al. Construction and initial characterization of a mouse-human chimeric anti-TNF antibody. Mol Immunol 1993; 30:1443-53; PMID:8232330; https://doi.org/10.1016/0161-5890(93)90106-L
   PubMed Web of Science ®Google Scholar
• Maini RN, Feldmann M. How does infliximab work in rheumatoid arthritis? Arthritis Res 2002; 4(Suppl 2):S22-8; PMID:12110154; https://doi.org/10.1186/ar549
   PubMedGoogle Scholar
• Liang S, Dai J, Hou S, Su L, Zhang D, Guo H, Hu S, Wang H, Rao Z, Guo Y, et al. Structural basis for treating tumor necrosis factor alpha (TNFalpha)-associated diseases with the therapeutic antibody infliximab. J Biol Chem 2013; 288:13799-807; PMID:23504311; https://doi.org/10.1074/jbc.M112.433961
   PubMed Web of Science ®Google Scholar
• Hu S, Liang S, Guo H, Zhang D, Li H, Wang X, Yang W, Qian W, Hou S, Wang H, et al. Comparison of the inhibition mechanisms of adalimumab and infliximab in treating tumor necrosis factor alpha-associated diseases from a molecular view. J Biol Chem 2013; 288:27059-67; PMID:23943614; https://doi.org/10.1074/jbc.M113.491530
   PubMed Web of Science ®Google Scholar
• Stanfield RL, Zemla A, Wilson IA, Rupp B. Antibody elbow angles are influenced by their light chain class. J Mol Biol 2006; 357:1566-74; PMID:16497332; https://doi.org/10.1016/j.jmb.2006.01.023
   PubMed Web of Science ®Google Scholar
• Rupp B. Biomolecular crystallography: Principles, practice, and application to structural biology. New York: Garland Science, 2010; ISBN:9780815340812.
   Google Scholar
• Brown PH, Balbo A, Schuck P. Characterizing protein-protein interactions by sedimentation velocity analytical ultracentrifugation. Current protocols in immunology. edited by John E Coligan (Ed.) [et al] 2008; Chapter 18:Unit 18 5; PMID:8491296; https://doi.org/10.1002/0471142735.im1815s81
   PubMedGoogle Scholar
• Howlett GJ, Minton AP, Rivas G. Analytical ultracentrifugation for the study of protein association and assembly. Curr Opin Chem Biol 2006; 10:430-6; PMID:16935549; https://doi.org/10.1016/j.cbpa.2006.08.017
   PubMed Web of Science ®Google Scholar
• Li S, Schmitz KR, Jeffrey PD, Wiltzius JJ, Kussie P, Ferguson KM. Structural basis for inhibition of the epidermal growth factor receptor by cetuximab. Cancer Cell 2005; 7:301-11; PMID:15837620; https://doi.org/10.1016/j.ccr.2005.03.003
   PubMed Web of Science ®Google Scholar
• McCoy AJ, Grosse-Kunstleve RW, Adams PD, Winn MD, Storoni LC, Read RJ. Phaser crystallographic software. J Appl Crystallogr 2007; 40:658-74; PMID:19461840; https://doi.org/10.1107/S0021889807021206
   PubMed Web of Science ®Google Scholar
• Adams PD, Afonine PV, Bunkoczi G, Chen VB, Davis IW, Echols N, Headd JJ, Hung LW, Kapral GJ, Grosse-Kunstleve RW, et al. PHENIX: A comprehensive python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 2010; 66:213-21; PMID:20124702; https://doi.org/10.1107/S0907444909052925
   PubMed Web of Science ®Google Scholar
• Emsley P, Lohkamp B, Scott WG, Cowtan K. Features and development of Coot. Acta Crystallogr D Biol Crystallogr 2010; 66:486-501; PMID:20383002; https://doi.org/10.1107/S0907444910007493
   PubMed Web of Science ®Google Scholar
• Chen VB, Arendall WB, Headd JJ 3rd, Keedy DA, Immormino RM, Kapral GJ, Murray LW, Richardson JS, Richardson DC. MolProbity: All-atom structure validation for macromolecular crystallography. Acta Crystallogr D Biol Crystallogr 2010; 66:12-21; PMID:20057044; https://doi.org/10.1107/S0907444909042073
   PubMed Web of Science ®Google Scholar
• Silva-Martin N, Bartual SG, Ramirez-Aportela E, Chacon P, Park CG, Hermoso JA. Structural basis for selective recognition of endogenous and microbial polysaccharides by macrophage receptor SIGN-R1. Structure 2014; 22:1595-606; PMID:25450767; https://doi.org/10.1016/j.str.2014.09.001
   PubMed Web of Science ®Google Scholar
• Schuck P. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophysical J 2000; 78:1606-19; PMID:10692345; https://doi.org/10.1016/S0006-3495(00)76713-0
   PubMed Web of Science ®Google Scholar