Glycoengineering of antibody (Herceptin) through yeast expression and in vitro enzymatic glycosylation.

ABSTRACT: Monoclonal antibodies (mAbs) have been developed as therapeutics, especially for the treatment of cancer, inflammation, and infectious diseases. Because the glycosylation of mAbs in the Fc region influences their interaction with effector cells that kill antibody-targeted cells, and the current method of antibody production is relatively expensive, efforts have been directed toward the development of alternative expressing systems capable of large-scale production of mAbs with desirable glycoforms. In this study, we demonstrate that the mAb trastuzumab expressed in glycoengineered P. pastoris can be remodeled through deglycosylation by endoglycosidases identified from the Carbohydrate Active Enzymes database and through transglycosylation using glycans with a stable leaving group to

SUBMITTER: Liu CP 

PROVIDER: S-EPMC5789950 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature