New Opportunities in Glycan Engineering for Therapeutic Proteins

Antibodies

Jason C. Rouse¹  Xiaotian Zhong²  Aaron M. D’Antona²  John J. Scarcelli³ 

[1] Analytical R&D, Biotherapeutics Pharmaceutical Sciences, Medicinal Sciences, Pfizer Worldwide R&D, 1 Burtt Road, Andover, MA 01810, USA;BioMedicine Design, Medicinal Sciences, Pfizer Worldwide R&D, 610 Main Street, Cambridge, MA 02139, USA;BioProcess R&D, Biotherapeutics Pharmaceutical Sciences, Medicinal Sciences, Pfizer Worldwide R&D, 1 Burtt Road, Andover, MA 01810, USA;

关键词: glycosylation pathways;    N-acetyl-galactosamine;    mannose-6-phosphate;    lysosomal degradation;    Fab glycans;    antibody diversification;   

DOI  :  10.3390/antib11010005

来源: DOAJ

【 摘 要 】

Glycans as sugar polymers are important metabolic, structural, and physiological regulators for cellular and biological functions. They are often classified as critical quality attributes to antibodies and recombinant fusion proteins, given their impacts on the efficacy and safety of biologics drugs. Recent reports on the conjugates of N-acetyl-galactosamine and mannose-6-phosphate for lysosomal degradation, Fab glycans for antibody diversification, as well as sialylation therapeutic modulations and O-linked applications, have been fueling the continued interest in glycoengineering. The current advancements of the human glycome and the development of a comprehensive network in glycosylation pathways have presented new opportunities in designing next-generation therapeutic proteins.

【 授权许可】

Unknown