Byung-Kwon Choi

TL;DR: It is demonstrated that human antibodies with specific human N-glycan structures can be produced in glycoengineered lines of the yeast Pichia pastoris and that antibody-mediated effector functions can be optimized by generating specific glycoforms.

TL;DR: Yeast is a widely used recombinant protein expression system expanded by engineering the yeast Pichia pastoris to secrete human glycoproteins with fully complex terminally sialylated N-glycans, allowing it to replicate the sequential steps of human glycosylation.

TL;DR: In this article, the authors proposed a method to obtain a Man5GlcNAc2 core structure which can then be modified by heterologous expression of one or more enzymes, e.g., glycosyltransferases, sugar transporters and mannosidases, to yield human-like glycoproteins.

TL;DR: In this article, a lower eukaryotic host cell producing human-like glycoproteins characterized as having a terminal β-galactose residue and essentially lacking fucose and sialic acid residues.

TL;DR: The results suggest that the glycosylation status of recombinant proteins can be improved by heterologous STT3 expression, which will allow for the customization of therapeutic protein profiles.