Impact of structural modifications of IgG antibodies on effector functions.

Autor:	Damelang T; Sanquin Research, Department of Experimental Immunohematology and Landsteiner Laboratory, Amsterdam, Netherlands.; Sanquin Research, Department of Immunopathology, Amsterdam, Netherlands.; Department of Biomolecular Mass Spectrometry and Proteomics, Utrecht Institute for Pharmaceutical Sciences and Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, Netherlands.; Department of Antibody Research & Technologies', Genmab, Utrecht, Netherlands., Brinkhaus M; Sanquin Research, Department of Experimental Immunohematology and Landsteiner Laboratory, Amsterdam, Netherlands.; Department of Biomolecular Mass Spectrometry and Proteomics, Utrecht Institute for Pharmaceutical Sciences and Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, Netherlands., van Osch TLJ; Sanquin Research, Department of Experimental Immunohematology and Landsteiner Laboratory, Amsterdam, Netherlands.; Department of Biomolecular Mass Spectrometry and Proteomics, Utrecht Institute for Pharmaceutical Sciences and Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, Netherlands., Schuurman J; Department of Antibody Research & Technologies', Genmab, Utrecht, Netherlands., Labrijn AF; Department of Antibody Research & Technologies', Genmab, Utrecht, Netherlands., Rispens T; Sanquin Research, Department of Immunopathology, Amsterdam, Netherlands., Vidarsson G; Sanquin Research, Department of Experimental Immunohematology and Landsteiner Laboratory, Amsterdam, Netherlands.; Department of Biomolecular Mass Spectrometry and Proteomics, Utrecht Institute for Pharmaceutical Sciences and Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, Netherlands.
Jazyk:	angličtina
Zdroj:	Frontiers in immunology [Front Immunol] 2024 Jan 08; Vol. 14, pp. 1304365. Date of Electronic Publication: 2024 Jan 08 (Print Publication: 2023).
DOI:	10.3389/fimmu.2023.1304365
Abstrakt:	Immunoglobulin G (IgG) antibodies are a critical component of the adaptive immune system, binding to and neutralizing pathogens and other foreign substances. Recent advances in molecular antibody biology and structural protein engineering enabled the modification of IgG antibodies to enhance their therapeutic potential. This review summarizes recent progress in both natural and engineered structural modifications of IgG antibodies, including allotypic variation, glycosylation, Fc engineering, and Fc gamma receptor binding optimization. We discuss the functional consequences of these modifications to highlight their potential for therapeutical applications. Competing Interests: TD, JS, and AL were employed by and/or own warrants and/or stocks in Genmab. The work of MB was funded by argenx. JS and AL are inventors of patents/pending patent applications on technologies and mutations mentioned in this review. GV serves as a consultant for argenx. Genmab and argenx are both biotechnology companies that develop therapeutic antibodies. The remaining authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest. (Copyright © 2024 Damelang, Brinkhaus, van Osch, Schuurman, Labrijn, Rispens and Vidarsson.)
Databáze:	MEDLINE
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