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Semin Cell Dev Biol. 2018 Aug;80:133-141. doi: 10.1016/j.semcdb.2017.07.005. Epub 2017 Jul 5.

Plant glyco-biotechnology.

Author information

1
Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
2
Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria. Electronic address: richard.strasser@boku.ac.at.

Abstract

Glycosylation is an important protein modification in all eukaryotes. Whereas the early asparagine-linked glycosylation (N-glycosylation) and N-glycan processing steps in the endoplasmic reticulum are conserved between mammals and plants, the maturation of complex N-glycans in the Golgi apparatus differs considerably. Due to a restricted number of Golgi-resident N-glycan processing enzymes and the absence of nucleotide sugars such as CMP-N-acetylneuraminic acid, plants produce only a limited repertoire of different N-glycan structures. Moreover, mammalian mucin-type O-glycosylation of serine or threonine residues has not been described in plants and the required machinery is not encoded in their genome which enables de novo build-up of the pathway. As a consequence, plants are very well-suited for the production of homogenous N- and O-glycans and are increasingly used for the production of recombinant glycoproteins with custom-made glycans that may result in the generation of biopharmaceuticals with improved therapeutic potential.

KEYWORDS:

Endoplasmic reticulum; Glycan function; Glyco-engineering; Golgi apparatus; N-Glycosylation; O-Glycosylation

PMID:
28688929
DOI:
10.1016/j.semcdb.2017.07.005
[Indexed for MEDLINE]
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