References
- Suzuki M, Kato C, Kato A. Therapeutic antibodies: their mechanisms of action and the pathological findings they induce in toxicity studies. J Toxicol Pathol. 2015;28(3):133–9. doi:https://doi.org/10.1293/tox.2015-0031.
- Singh S, Kumar NK, Dwiwedi P, Charan J, Kaur R, Sidhu P, Chugh VK. Monoclonal antibodies: a review. Curr Clin Pharmacol. 2018;13(2):85–99. doi:https://doi.org/10.2174/1574884712666170809124728.
- Wang W, Lu P, Fang Y, Hamuro L, Pittman T, Carr B, Hochman J, Prueksaritanont T. Monoclonal Antibodies with Identical Fc Sequences Can Bind to FcRn Differentially with Pharmacokinetic Consequences. Drug Metab Dispos. 2011;39(9):1469–77. doi:https://doi.org/10.1124/dmd.111.039453.
- Schoch A, Kettenberger H, Mundigl O, Winter G, Engert J, Heinrich J, Emrich T. Charge-mediated influence of the antibody variable domain on FcRn-dependent pharmacokinetics. Proc Natl Acad Sci U S A. 2015;112(19):5997–6002. doi:https://doi.org/10.1073/pnas.1408766112.
- Piche-Nicholas NM, Avery LB, King AC, Kavosi M, Wang M, O’Hara DM, Tchistiakova L, Katragadda M. Changes in complementarity-determining regions significantly alter IgG binding to the neonatal Fc receptor (FcRn) and pharmacokinetics. mAbs. 2018;10(1):81–94. doi:https://doi.org/10.1080/19420862.2017.1389355.
- Janda A, Bowen A, Greenspan NS, Casadevall A. Ig Constant Region Effects on Variable Region Structure and Function. Front Microbiol. 2016;7:22–22. doi:https://doi.org/10.3389/fmicb.2016.00022.
- Yang D, Kroe-Barrett R, Singh S, Roberts CJ, Laue TM. IgG cooperativity – is there allostery? Implications for antibody functions and therapeutic antibody development. mAbs. 2017;9(8):1231–52. doi:https://doi.org/10.1080/19420862.2017.1367074.
- Oda M, Kozono H, Morii H, Azuma T. Evidence of allosteric conformational changes in the antibody constant region upon antigen binding. Int Immunol. 2003;15(3):417–26. doi:https://doi.org/10.1093/intimm/dxg036.
- Sagawa T, Oda M, Morii H, Takizawa H, Kozono H, Azuma T. Conformational changes in the antibody constant domains upon hapten-binding. Mol Immunol. 2005;42(1):9–18. doi:https://doi.org/10.1016/j.molimm.2004.07.004.
- Zhao J, Nussinov R, Ma B. Antigen binding allosterically promotes Fc receptor recognition. mAbs. 2019;11(1):58–74. doi:https://doi.org/10.1080/19420862.2018.1522178.
- Orlandi C, Deredge D, Ray K, Gohain N, Tolbert W, DeVico AL, Wintrode P, Pazgier M, Lewis GK. Antigen-Induced Allosteric Changes in a Human IgG1 Fc Increase Low-Affinity Fcγ Receptor Binding. Structure. 2020;28(5):516–527.e5. doi:https://doi.org/10.1016/j.str.2020.03.001
- Roopenian DC, Akilesh S. FcRn: the neonatal Fc receptor comes of age. Nat Rev Immunol. 2007;7(9):715–25. doi:https://doi.org/10.1038/nri2155.
- Pyzik M, Rath T, Lencer WI, Baker K, Blumberg RS. FcRn: the architect behind the immune and nonimmune functions of IgG and albumin. J Immunol 2015;194(10):4595–603. doi:https://doi.org/10.4049/jimmunol.1403014.
- Vaccaro C, Zhou J, Ober RJ, Ward ES. Engineering the Fc region of immunoglobulin G to modulate in vivo antibody levels. Nat Biotechnol. 2005;23(10):1283–88. doi:https://doi.org/10.1038/nbt1143.
- Petkova SB, Akilesh S, Sproule TJ, Christianson GJ, Al Khabbaz H, Brown AC, Presta LG, Meng YG, Roopenian DC. Enhanced half-life of genetically engineered human IgG1 antibodies in a humanized FcRn mouse model: potential application in humorally mediated autoimmune disease. Int Immunol. 2006;18(12):1759–69. doi:https://doi.org/10.1093/intimm/dxl110.
- Dall’Acqua WF, Kiener PA, Wu H. Properties of Human IgG1s Engineered for Enhanced Binding to the Neonatal Fc Receptor (FcRn). J Biol Chem. 2006;281(33):23514–24. doi:https://doi.org/10.1074/jbc.M604292200.
- Ward ES, Ober RJ.Multitasking by exploitation of intracellular transport functions the many faces of FcRn. Adv Immunol. 2009;103:77–115.
- Devanaboyina SC, Lynch SM, Ober RJ, Ram S, Kim D, Puig-Canto A, Breen S, Kasturirangan S, Fowler S, Peng L, et al. The effect of pH dependence of antibody-antigen interactions on subcellular trafficking dynamics. mAbs. 2013;5(6):851–59. doi:https://doi.org/10.4161/mabs.26389.
- Sampei Z, Haraya K, Tachibana T, Fukuzawa T, Shida-Kawazoe M, Gan SW, Shimizu Y, Ruike Y, Feng S, Kuramochi T, et al. Antibody engineering to generate SKY59, a long-acting anti-C5 recycling antibody. Plos One. 2018;13(12):e0209509. doi:https://doi.org/10.1371/journal.pone.0209509.
- Fukuzawa T, Nezu J. A Novel Recycling Antibody for Complement-mediated Diseases. Curr Med Chem. 2020;27(25):4157–4164. doi:https://doi.org/10.2174/0929867326666191016115853
- Burmeister WP, Gastinel LN, Simister NE, Blum ML, Bjorkman PJ. Crystal structure at 2.2 Å resolution of the MHC-related neonatal Fc receptor. Nature. 1994;372(6504):336–43. doi:https://doi.org/10.1038/372336a0.
- Burmeister WP, Huber AH, Bjorkman PJ. Crystal structure of the complex of rat neonatal Fc receptor with Fc. Nature. 1994;372(6504):379–83. doi:https://doi.org/10.1038/372379a0.
- Vaughn DE, Bjorkman PJ. Structural basis of pH-dependent antibody binding by the neonatal Fc receptor. Structure (London, England: 1993). 1998;6(1):63–73. doi:https://doi.org/10.1016/S0969-2126(98)00008-2.
- Martin WL, West AP Jr., Gan L, Bjorkman PJ. Crystal structure at 2.8 Å of an FcRn/Heterodimeric Fc Complex. Mol Cell. 2001;7(4):867–77. doi:https://doi.org/10.1016/S0969-2126(98)00008-2.
- Borrok MJ, Wu Y, Beyaz N, Yu X-Q, Oganesyan V, Dall’Acqua WF, Tsui P. pH-dependent binding engineering reveals an FcRn affinity threshold that governs IgG recycling. J Biolog Chem. 2015;290(7):4282–4290. doi:https://doi.org/10.1074/jbc.M114.603712
- Wang W, Wang EQ, Balthasar JP. Monoclonal antibody pharmacokinetics and pharmacodynamics. Clin Pharmacol Ther. 2008;84(5):548–58. doi:https://doi.org/10.1038/clpt.2008.170.
- Jensen PF, Larraillet V, Schlothauer T, Kettenberger H, Hilger M, Rand KD. Investigating the Interaction between the Neonatal Fc Receptor and Monoclonal Antibody Variants by Hydrogen/Deuterium Exchange Mass Spectrometry. Mol celL Proteom. 2015;14(1):148–61. doi:https://doi.org/10.1074/mcp.M114.042044.
- Jensen PF, Schoch A, Larraillet V, Hilger M, Schlothauer T, Emrich T, Rand KD. A two-pronged binding mechanism of IgG to the neonatal fc receptor controls complex stability and IgG serum half-life. Mol celL Proteom. 2017;16(3):451–56. doi:https://doi.org/10.1074/mcp.M116.064675.
- Zhang Y, Wecksler AT, Molina P, Deperalta G, Gross ML. Mapping the binding interface of VEGF and a monoclonal antibody Fab-1 Fragment with Fast Photochemical Oxidation of Proteins (FPOP) and mass spectrometry. J Am Soc Mass Spectrom. 2017;28(5):850–58. doi:https://doi.org/10.1007/s13361-017-1601-7.
- Shi L, Liu T, Gross ML, Huang Y. Recognition of human IgG1 by Fcγ Receptors: structural insights from hydrogen–deuterium exchange and fast photochemical oxidation of proteins coupled with mass spectrometry. Biochemistry. 2019;58(8):1074–80. doi:https://doi.org/10.1021/acs.biochem.8b01048.
- Lin M, Krawitz D, Callahan MD, Deperalta G, Wecksler AT. Characterization of ELISA antibody-antigen interaction using footprinting-mass spectrometry and negative staining transmission electron microscopy. J Am Soc Mass Spectrom. 2018;29(5):961–71. doi:https://doi.org/10.1007/s13361-017-1883-9.
- Booth BJ, Ramakrishnan B, Narayan K, Wollacott AM, Babcock GJ, Shriver Z, Viswanathan K. Extending human IgG half-life using structure-guided design. mAbs. 2018;10(7):1098–110. doi:https://doi.org/10.1080/19420862.2018.1490119.
- Sela-Culang I, Alon S, Ofran Y. A systematic comparison of free and bound antibodies reveals binding-related conformational changes. The Journal of Immunology . 2012;189(10):4890–99. doi:https://doi.org/10.4049/jimmunol.1201493.
- Wang X, McKay P, Yee LT, Dutina G, Hass PE, Nijem I, Allison D, Cowan KJ, Lin K, Quarmby V, et al. Impact of SPR biosensor assay configuration on antibody: neonatal Fc receptor binding data. mAbs. 2017;9(2):319–32. doi:https://doi.org/10.1080/19420862.2016.1261774.
- Brambell FW. The transmission of immune globulins from the mother to the foetal and newborn young. Proc Nutr Soc. 1969;28(1):35–41. doi:https://doi.org/10.1079/PNS19690007.
- Rodewald R. pH-dependent binding of immunoglobulins to intestinal cells of the neonatal rat. J Cell Biol. 1976;71(2):666–69. doi:https://doi.org/10.1083/jcb.71.2.666.
- Martins JP, Kennedy PJ, Santos HA, Barrias C, Sarmento B. A comprehensive review of the neonatal Fc receptor and its application in drug delivery. Pharmacol Ther. 2016;161:22–39. doi:https://doi.org/10.1016/j.pharmthera.2016.03.007.
- Datta-Mannan A, Witcher DR, Tang Y, Watkins J, Wroblewski VJ. Monoclonal antibody clearance. J Biol Chem. 2007;282(3):1709–17. doi:https://doi.org/10.1074/jbc.M607161200.
- Baker K, Rath T, Pyzik M, Blumberg RS. The role of FcRn in antigen presentation. Front Immunol. 2014;5:408–408. doi:https://doi.org/10.3389/fimmu.2014.00408.
- Platzer B, Stout M, Fiebiger E. Antigen cross-presentation of immune complexes. Front Immunol. 2014;5:140–140. doi:https://doi.org/10.3389/fimmu.2014.00140.
- Pyzik M, Sand KMK, Hubbard JJ, Andersen JT, Sandlie I, Blumberg RS. The Neonatal Fc Receptor (FcRn): a misnomer? Front Immunol. 2019;10:1540. doi:https://doi.org/10.3389/fimmu.2019.01540.
- Baker K, Rath T, Flak MB, Arthur JC, Chen Z, Glickman JN, Zlobec I, Karamitopoulou E, Stachler MD, Odze RD, et al. Neonatal Fc receptor expression in dendritic cells mediates protective immunity against colorectal cancer. Immunity. 2013;39(6):1095–107. doi:https://doi.org/10.1016/j.immuni.2013.11.003.
- Baker K, Qiao S-W, Kuo TT, Aveson VG, Platzer B, Andersen J-T, Sandlie I, Chen Z, de Haar C, Lencer WI, et al. Neonatal Fc receptor for IgG (FcRn) regulates cross-presentation of IgG immune complexes by CD8-CD11b+ dendritic cells. Proc Natl Acad Sci U S A. 2011;108(24):9927–32. doi:https://doi.org/10.1073/pnas.1019037108.
- Deperalta G, Alvarez M, Bechtel C, Dong K, McDonald R, Ling V. Structural analysis of a therapeutic monoclonal antibody dimer by hydroxyl radical footprinting. mAbs. 2013;5(1):86–101. doi:https://doi.org/10.4161/mabs.22964.
- Wecksler AT, Yin J, Lee Tao P, Kabakoff B, Sreedhara A, Deperalta G. Photodisruption of the structurally conserved Cys-Cys-Trp triads leads to reduction-resistant scrambled intrachain disulfides in an IgG1 monoclonal antibody. Mol Pharm. 2018;15(4):1598–606. doi:https://doi.org/10.1021/acs.molpharmaceut.7b01128.
- Brandt JP, Patapoff TW, Aragon SR. Construction, MD simulation, and hydrodynamic validation of an all-atom model of a monoclonal IgG antibody. Biophys J. 2010;99(3):905–13. doi:https://doi.org/10.1016/j.bpj.2010.05.003.
- Abdiche YN, Yeung YA, Chaparro-Riggers J, Barman I, Strop P, Chin SM, Pham A, Bolton G, McDonough D, Lindquist K, et al. The neonatal Fc receptor (FcRn) binds independently to both sites of the IgG homodimer with identical affinity. mAbs. 2015;7(2):331–43. doi:https://doi.org/10.1080/19420862.2015.1008353.