Plant Physiol. Drug Metab Dispos
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Published on March 7, 2008; 10.1104/pp.108.117572

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Received February 7, 2008
Accepted March 3, 2008

Construction of a functional CMP-sialic acid (CMP-Neu5Ac) biosynthesis pathway in Arabidopsis thaliana

Alexandra Castilho , Martin Pabst , Renaud Leonard , Christiane Veit , Friedrich Altmann , Lukas Mach , Josef Glossl , Richard Strasser *, and Herta Steinkellner

Institute of Applied Genetics and Cell Biology, University of Natural Resources and Applied Life Sciences, BOKU-Vienna, Muthgasse 18, A-1190 Vienna, Austria; Department of Chemistry, University of Natural Resources and Applied Life Sciences, BOKU-Vienna, Muthgasse 18, A-1190 Vienna, Austria

* Corresponding author; email: richard.strasser{at}boku.ac.at.

Previous studies have reported that plants contain negligible amounts of free or protein-bound N-acetylneuraminic acid (Neu5Ac). This is a major disadvantage for the use of plants as a biopharmaceutical expression system since N-glycans with terminal Neu5Ac residues are important for the biological activities and half-lives of recombinant therapeutic glycoproteins in humans. For the synthesis of Neu5Ac-containing N-glycans, plants have to acquire the ability to synthesize Neu5Ac and its nucleotide-activated derivative, cytidine monophospho-N-acetylneuraminic acid (CMP-Neu5Ac).

In this study we have generated transgenic Arabidopsis thaliana plants expressing three key enzymes of the mammalian Neu5Ac biosynthesis pathway: UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine-kinase (GNE), N-acetylneuraminic acid phosphate-synthase (NANS), and CMP-N-acetylneuraminic acid synthetase (CMAS). Simultaneous expression of GNE and NANS resulted in the generation of significant Neu5Ac amounts (1275 nmol g-1 fresh weight in leaves) in planta, which could be further converted to CMP-Neu5Ac (2.4 nmol g-1 fresh weight in leaves) by co-expression of CMAS. These findings are a major step towards the production of Neu5Ac-containing glycoproteins in plants.






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