Differential N-Glycan Modifications of Human Alpha 1-Acid Glycoprotein (a1 AGP) Produced in Different Silkworm Strains using the Baculovirus Expression System

摘要

N-glycosylation plays an important role in various biological activities and in the structural stability of serum glycoproteins. The baculovirus expression system (BES) is widely used to produce recombinant proteins but in some case it is not suitablefor medical use because of the differences in N-linked glycans between insects and mammals. We reported that human serum protein alpha 1-acid protein (qIAGP) is effectively used as a model protein for evaluating the validity of engineering the insect-type N-glycosylation pathway. Using this protein, the productivity and N-linked glycan structures were compared among the 37 different silkworm strains. Interestingly, there was no difference in N-linked glycan structure among the silkworm strains, but there was difference in the degree of N-glycosylation.