Posttranslational modifications to plants – glycosylation
Part 3. Proteomics
3.5. Proteome Diversity
Short Specialist Review
Published Online: 15 JUL 2006
Copyright © 2005 John Wiley & Sons, Ltd
Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics
How to Cite
Tekoah, Y. 2006. Posttranslational modifications to plants – glycosylation. Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics. 3:3.5.
- Published Online: 15 JUL 2006
Posttranslational modifications (PTMs) of plants include glycosylation. As in mammals, plants attach both N- and O-linked glycans, but the systems are not identical. More is known about the N-linked type glycans. The complex N-linked glycans of plants differ markedly in structure from those of animals. They more closely resemble those of insects and molluscs by not containing terminal sialic acids. The complex type glycans may contain an α-(1,3)-fucose (Fuc) linked to the proximal GlcNAc residue and/or a β-(1,2)-xylose (Xyl) residues attached to the α-linked mannose (Man) of the glycan core, similar to what is found in insects and molluscs. These additional epitopes are thought to have antigenic and/or allergenic properties. Less is known about O-linked glycans in plants. Recently, plants and algae have been utilized for the production of therapeutic proteins. Much more information on glycosylation of plants and algae and the ability to manipulate the glycosylation will have to be acquired, if these therapeutic proteins are to be effective.
- posttranslational modification;
- therapeutic proteins