Development of Biosimilars: Analysis of Etanercept Glycosylation as a Case Study
Mario DiPaola*, Jing Li and Elaine Stephens
Blue Stream Laboratories, Inc. Cambridge MA 02138, USA
- *Corresponding Author:
- Mario DiPaola
Blue Stream Laboratories
Inc. Cambridge 02138, USA
E-mail: [email protected]
Received Date: November 06, 2013; Accepted Date: December 27, 2013; Published Date: December 30, 2013
Citation: DiPaola M, Li J, Stephens E (2013) Development of Biosimilars: Analysis of Etanercept Glycosylation as a Case Study. J Bioanal Biomed 5: 180-186. doi: 10.4172/1948-593X.1000096
Copyright: © 2013 DiPaola M, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Glycosylation is a critical attribute of glycoprotein products as it has been shown that the type and degree of glycosylation can have a significant impact on the product efficacy and immunogenicity. In developing generic forms of glycoprotein based therapeutic products, it is necessary to characterize the glycosylation of these products to ensure that it conforms with the original product as well as natural form of the product. In this study, we have focused on the characterization of the N-linked glycans and, in less details, on the O-linked glycans found on Etanercept (EnbrelTM). Using a series of methodologies, we mapped the N-linked glycosylation sites in Etanercept and also defined the types of glycan structures associated with each site. Separately, we also determined the extent of Etanercept O-glycosylation and the type of O-linked glycans.