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Glycoprotein sialylation in plants?

Nature Biotechnology volume 22, pages 1351–1352 (2004)Cite this article

To the editor:

A Brief Communication by Shah et al. in a previous issue (Nat. Biotechnol. 21, 1470–1471, 2003) claims evidence for sialylated endogenous glycoconjugates in plant cells. This work is of particular relevance to large-scale transgenic plant production systems for recombinant human protein therapeutics, which often require complex glycosylation, such as sialylation, for stability, solubility, folding, pharmacokinetics/pharmacodynamics and/or activity.

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Figure 1: Lectin blotting analysis of proteins from A. thaliana and N. tabacum using affinity detection with lectins SNA I and MAA.
Figure 2: LC/MS analysis on DMB-derivatized samples prepared from tobacco BY2 protein extracts.

References

  1. Gomord, V. et al. Plant Biotechnol. J. 2, 83–100 (2004).

    Article  CAS  PubMed  Google Scholar 

  2. Bardor, M. et al. Glycobiology 13, 427–434 (2003).

    Article  CAS  PubMed  Google Scholar 

  3. Wee, E.G., Sherrier, D.J., Prime, T.A. & Dupree, P. Plant Cell 10, 1759–1768 (1998).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  4. Lerouge, P. et al. Plant Mol. Biol. 38, 31–48 (1998).

    Article  CAS  PubMed  Google Scholar 

  5. von Schaewen, A., Sturm, A., O'Neill, J. & Chrispeels, M.J. Plant Physiol. 102, 1109–1118 (1993).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  6. Perez, S. et al. Biochimie 89, 109–121 (2003).

    Article  CAS  Google Scholar 

  7. Delmas, F. et al. Plant Physiol. 133, 348–360 (2003).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  8. Bakker, H. et al. Proc. Natl. Acad. Sci. USA 98, 2899–2904 (2001).

    Article  CAS  PubMed  Google Scholar 

Download references

Acknowledgements

This study was supported by CNRS, the University of Rouen, Région Haute Normandie and MEDICAGO. The authors thank Sandra Diaz and Ajit Varki for fruitful advice for the LC/MS recording of DMB-derivatives.

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Authors and Affiliations

  1. CNRS-UMR 6037, IFRMP 23, GDR 2590, Université de Rouen, Mont Saint Aignan, 76821, France

    Martial Séveno, Muriel Bardor, Thomas Paccalet, Véronique Gomord, Patrice Lerouge & Loïc Faye

  2. Department of Medicine and Cellular Medicine, Glycobiology Research and Training Center, University of California, San Diego, La Jolla, 92093-0687, California, USA

    Muriel Bardor

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  1. Martial Séveno
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Correspondence to Loïc Faye.

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Séveno, M., Bardor, M., Paccalet, T. et al. Glycoprotein sialylation in plants?. Nat Biotechnol 22, 1351–1352 (2004). https://doi.org/10.1038/nbt1104-1351

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