Поправка: Эволюция антиCD20 Лечения множественным склерозом: оптимизация характеристик и функций антител.
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Cree Bruce A C, Berger Joseph R, Greenberg Benjamin
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Correction: The Evolution of Anti‑CD20 Treatment for Multiple Sclerosis: Optimization of Antibody Characteristics and Function.
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In this article, Fig. 5A appeared incorrectly and have now been corrected in the original publication. For completeness and transparency, the old incorrect and the correct versions are given below.
Incorrect Fig. 5 :
Polymorphisms of FcγIIIa-receptor and anti-CD20 mAb Fc-binding affinity. A FcγRIIIa polymorphisms on NK cells modulate the strength of interaction with the Fc region and determine the strength of anti-CD20 IgG1 binding. The FcγRIIIa 158F polymorphism has weaker IgG binding than the FcγRIIIa 158V polymorphism. Adapted from Zhong M, van der Walt A, Campagna MP, Stankovich J, Butzkueven H, Jokubaitis V. The pharmacogenetics of rituximab: potential implications for anti-CD20 therapies in multiple sclerosis. Neurotherapeutics, volume 17. pp. 1768–1784. Copyright 2020, the American Society for Experimental NeuroTherapeutics, Inc. [79]. B Ublituximab, due to its glycoengineering, has enhanced affinity for all variants of the FcγRIIIa receptor, with the highest binding and relative affinity for FcγRIIIa 158V and FcγRIIIa 158F variant receptors compared with other, non-glycoengineered anti-CD20 mAbs [74]. ADCC antibody-dependent cell-mediated cytotoxicity, CD cluster of differentiation, Fc fragment crystallizable, FCGR Fc gamma receptor gene, FcγR Fc gamma receptor, IgG immunoglobulin G, Ka association constant, KD equilibrium dissociation constant, mAb monoclonal antibody, NK natural killer, SNP single-nucleotide polymorphism
Correct Fig. 5 :
Polymorphisms of FcγIIIa-receptor and anti-CD20 mAb Fc-binding affinity. A FcγRIIIa polymorphisms on NK cells modulate the strength of interaction with the Fc region and determine the strength of anti-CD20 IgG1 binding. The FcγRIIIa 158F polymorphism has weaker IgG binding than the FcγRIIIa 158V polymorphism. Adapted from Zhong M, van der Walt A, Campagna MP, Stankovich J, Butzkueven H, Jokubaitis V. The pharmacogenetics of rituximab: potential implications for anti-CD20 therapies in multiple sclerosis. Neurotherapeutics, volume 17. pp. 1768–1784. Copyright 2020, the American Society for Experimental NeuroTherapeutics, Inc. [79]. B Ublituximab, due to its glycoengineering, has enhanced affinity for all variants of the FcγRIIIa receptor, with the highest binding and relative affinity for FcγRIIIa 158V and FcγRIIIa 158F variant receptors compared with other, non-glycoengineered anti-CD20 mAbs [74]. ADCC antibody-dependent cell-mediated cytotoxicity, CD cluster of differentiation, Fc fragment crystallizable, FCGR Fc gamma receptor gene, FcγR Fc gamma receptor, IgG immunoglobulin G, Ka association constant, KD equilibrium dissociation constant, mAb monoclonal antibody, NK natural killer, SNP single-nucleotide polymorphism
The original article has been corrected.