Glycosylation Pattern of Biotechnologically Produced Proteins - Lectin Array Technology as a Versatile Tool for Screening?

Abstract

Approximately 50 - 60% of all human proteins are glycosylated. Glycosylation can not only affect the structure of proteins, but also their biological activity, serum half-life, pharmacokinetics, pharmacodynamics, and immunogenicity. For biotechnologically derived proteins, analysis of glycosylation patterns is thus of utmost importance. Standard techniques are based on high performance liquid chromatography, mass spectrometry and capillary electrophoresis. Lectin microarrays are an orthogonal tool which is very promising for studying glycosylation patterns. However, though the advantages of lectin arrays for the analysis of glycoproteins have been discussed especially in review articles currently only a handful of publications are available, which are presenting data about therapeutic proteins analyzed with this promising technology. Within this review article, important aspects for analysis of therapeutic glycoproteins are highlighted from the perspective of the lectin array technology. This includes cell lines for the production of therapeutic proteins, influence of cell culture conditions on glycosylation, glycosylated antibodies and their effector functions, glycoengineering, regulatory guidance for biosimilars and methods for glycosylation analysis with special emphasis on lectin microarrays. The available literature proves that especially the lectin array technology is a upcoming tool for screening the glycosylation pattern of biotechnologically produced proteins. The technology is also versatile and more applications will be utilized in the near future for example for biomarker resarch and application as a diagnostic tool.