Glycosylation of Therapeutic Proteins
Glycosylation is one of the most common posttranslational modifications that influence structure, stability and function of therapeutic proteins expressed in CHO cells. Lectin-resistant CHO mutants with a wide variety of alterations in the glycosylation have been isolated by selection for resistance to the cytotoxicity of plant lectins. These CHO mutants have been used widely to elucidate deeper insights into the mechanisms underlying glycosylation, to identify genes that involved in glycosylation activities, and for glycoengineering. My research project centers on developing NGS data analysis pipelines in order to investigate genes involved in glycosylation pathways in both wide-type and lectin-resistant CHO cells and define correlation between genomic variations and glycosylation phenotypes.