Chinese hamster ovary mutants for glycosylation engineering of biopharmaceuticals Pharmaceutical

Glyco-engineering for biopharmaceutical production in moss bioreactors

The production of recombinant biopharmaceuticals (pharmaceutical proteins) is a strongly growing area in the pharmaceutical industry. While most products to date are produced in mammalian cell cultures, namely Chinese hamster ovary cells, plant-based production systems gained increasing acceptance over the last years. Different plant systems have been established which are suitable for standard...

Moss – An Innovative Tool for Protein Production

The complete sequencing of the human genome has significantly increased the number of pharmaceutically important proteins (“biopharmaceuticals”) to be produced at large scale. As this tendency is expected to continue, production capacity of biopharmaceuticals has become a strategic issue for the pharmaceutical industry. Mammalian cells such as those of baby hamster kidney and Chinese hamster ov...

Glycomics Profiling of Chinese Hamster Ovary Cell Glycosylation Mutants Reveals N-Glycans of a Novel Size and Complexity*

Identifying biological roles for mammalian glycans and the pathways by which they are synthesized has been greatly facilitated by investigations of glycosylation mutants of cultured cell lines and model organisms. Chinese hamster ovary (CHO) glycosylation mutants isolated on the basis of their lectin resistance have been particularly useful for glycosylation engineering of recombinant glycoprot...

Mutants of Chinese Hamster Ovary Cells Mouse-Human IgG1 Antibodies in Glycosylation on Ig Effector Function: Studies with Chimeric Effect of C2-Associated Carbohydrate Structure

Use of Chinese hamster ovary cells with altered glycosylation patterns to define the carbohydrate specificity of Entamoeba histolytica adhesion

We compared the adherence of E. histolytica trophozoites with a panel of lectin-resistant CHO mutants with altered glycosylation patterns. Our results coupled with data from saccharide inhibition studies indicate that terminal N-acetyllactosamine units on Asn-linked complex type oligosaccharides provide the major determinants on the cellular receptor for E. histolytica adhesion.