Preprint Review Version 1 Preserved in Portico This version is not peer-reviewed

Glycosylation Shapes the Efficacy and Safety of Diverse Protein, Gene and Cell Therapies

Version 1 : Received: 2 March 2023 / Approved: 3 March 2023 / Online: 3 March 2023 (10:43:51 CET)

A peer-reviewed article of this Preprint also exists.

Rocamora, F.; Peralta, A.G.; Shin, S.; Sorrentino, J.; Wu, M.; Toth, E.A.; Fuerst, T.R.; Lewis, N.E. Glycosylation Shapes the Efficacy and Safety of Diverse Protein, Gene and Cell Therapies. Biotechnology Advances 2023, 108206, doi:10.1016/j.biotechadv.2023.108206. Rocamora, F.; Peralta, A.G.; Shin, S.; Sorrentino, J.; Wu, M.; Toth, E.A.; Fuerst, T.R.; Lewis, N.E. Glycosylation Shapes the Efficacy and Safety of Diverse Protein, Gene and Cell Therapies. Biotechnology Advances 2023, 108206, doi:10.1016/j.biotechadv.2023.108206.

Abstract

Over recent decades, therapeutic proteins have had widespread success in treating a myriad of diseases. Glycosylation, a near universal feature of this class of drugs, is a critical quality attribute that significantly influences the physical properties, safety profile and biological activity of therapeutic proteins. Optimizing protein glycosylation, therefore, offers an important avenue to developing more efficacious therapies. In this review, we discuss specific examples of how variations in glycan structure and glycoengineering impacts the stability, safety, and clinical efficacy of protein-based drugs that are already in the market as well as those that are still in preclinical development. We also highlight the impact of glycosylation on next generation biologics such as T cell-based cancer therapy and gene therapy.

Keywords

glycosylation, glycoengineering, biologic, therapeutic protein, gene therapy, cell-based therapy, monoclonal antibody

Subject

Engineering, Bioengineering

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