Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
23554 | Journal of Biotechnology | 2013 | 4 Pages |
Overlapping glycosylation sequon (OGS) is composed of two overlapping N-glycosylation sequons and has been found in certain glycoproteins with pharmaceutical value. With a growing interest to produce pharmaceutical glycoproteins in plants, it is important to establish the glycosylation pattern of OGS-containing proteins expressed in varying plant tissues. Here, a chimeric OGS (NNST)-containing gene and its mutated forms (NNAT and NASNAT) were expressed in callus-derived tomato plantlets. Tissue extracts from the recombinant leaf and callus were used in immunoblotting and glycoprotein detection. We found that the glycosylation patterns of the NNST-containing chimeric protein differ from that of NNAT- and NASNAT-containing proteins.
► OGS motif in recombinant proteins is accessible. ► Glycosylation pattern of an OGS-containing protein differs between tomato tissues. ► Presence or absence of an OGS motif in plant-expressed glycoproteins is important.