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Posttranslational modifications to plants – glycosylation

Part 3. Proteomics

3.5. Proteome Diversity

Short Specialist Review

  1. Yoram Tekoah

Published Online: 15 JUL 2006

DOI: 10.1002/047001153X.g305321

Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics

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.

Author Information

  1. Ben-Gurion University of the Negev, Beer-Sheva, Israel

Publication History

  1. 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.


  • glycosylation;
  • posttranslational modification;
  • plants;
  • algae;
  • therapeutic proteins