Abstract
b1,4-Galactosylation of plant N-glycans is a prerequisite for commercial production of certain biopharmaceuticals in plants. Two different types of galactosylated N-glycans have initially been reported in plants as the result of expression of human b1,4-galactosyltransferase 1 (GalT). Here we show that these differences are associated with differences at its N-terminus: the natural short variant of human GalT results in hybrid type N-glycans, whereas the long form generates bi-antennary complex type N-glycans. Furthermore, expression of non-mammalian, chicken and
zebrafish GalT homologues with N-termini resembling the short human GalT N-terminus also induce hybrid type N-glycans. Providing both non-mammalian
GalTs with a 13 amino acid N-terminal extension that distinguishes the two naturally occurring forms of human GalT, acted to increase the levels of biantennary
galactosylated N-glycans when expressed in tobacco leaves. Replacement of the cytosolic tail and transmembrane domain of chicken and zebrafish GalTs
with the corresponding region of rat a2,6-sialyltransferase yielded a gene whose expression enhanced the level of bi-antennary galactosylation even further.
Original language | English |
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Pages (from-to) | 717-728 |
Journal | Transgenic Research |
Volume | 23 |
Issue number | 5 |
DOIs | |
Publication status | Published - 2014 |
Keywords
- golgi-apparatus
- murine beta-1,4-galactosyltransferase
- beta 1,4-galactosyltransferase
- transgenic plants
- gene
- cells
- localization
- antibodies
- oligosaccharides
- glycoproteins