Complex N-glycosylation of Recombinant Proteins by Insect Cells

by Laura A. Palomares and Octavio T. Ramírez
Volume 1, Issue 3 (Fall 2002)

The insect cell/baculovirus expression system typically results in more rapid expression and higher concentrations of recombinant proteins than what can be achieved with other animal cell culture systems. The lack of complex glycosylation in the proteins produced by this system, however, limits its use in the commercial-scale production of therapeutics. Complex glycosylation is required in many cases for adequate protein activity and pharmokinetic characteristics. In contrast to the protein's primary structure, which is encoded by the genetic material and is constant regardless of the host utilized, the extent of glycosylation is determined by the host, and by the protein itself. Even cells from different tissues of the same organism provide different glycosylation profiles. In addition, culture conditions and the cellular metabolic state can also influence protein glycosylation...

Citation:
Palomares LA, Ramírez OT. Complex N-glycosylation of Recombinant Proteins by Insect Cells. BioProcess J, 2002; 1(3): 70-73.