Glycosylation of monoclonal antibody products: Current status and future prospects

• Published in: Biotechnology progress Vol. 32; no. 5; pp. 1091 - 1102
• Main Authors: Batra, Jyoti, Rathore, Anurag S.
• Format: Journal Article
• Language: English
• Published: United States Blackwell Publishing Ltd 01.09.2016; Wiley Subscription Services, Inc
• Subjects: Animals; Antibodies, Monoclonal - chemistry; Antibodies, Monoclonal - metabolism; CH2 domain; effector function; Glycosylation; Humans; monoclonal antibodies; Polysaccharides - chemistry; Polysaccharides - metabolism; structural heterogeneity; effector function; glycosylation; CH2 domain; structural heterogeneity; monoclonal antibodies
• ISSN: 8756-7938; 1520-6033
• DOI: 10.1002/btpr.2366

Protein based therapeutics have started to dominate the pharmaceutical landscape primarily due to the high efficacy that they have demonstrated against complex diseases. Despite the significant success, issues with regards to safety, efficacy and quality of biotherapeutics have been a point of considerable debate and concern among the various stakeholders. The correlation between the glycoform profile and the safety and efficacy of a drug, in particular, has garnered significant attention of researchers worldwide. An escalated emphasis is presently given to develop an understanding of how the various process parameters as well molecular biology considerations contribute to glycan heterogeneity. This paper aims to review the major developments that have occurred in this area over the last decade. The impact of the various process parameters on glycan expression, methods for obtaining a pre‐determined glycan levels/profiles of a protein therapeutic and developments in the area of real‐time glycan monitoring and control are discussed. © 2016 American Institute of Chemical Engineers Biotechnol. Prog., 32:1091–1102, 2016