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Sialylated endogenous glycoconjugates in plant cells

Abstract

Bioengineered plants are emerging as promising systems for the production of therapeutically valuable proteins. It has been commonly accepted that plants do not perform mammalian-like post-translational modifications, particularly sialylation of glycoconjugates, and no evidence has previously been reported to suggest that they have such capabilities. Here we report the presence of sialylated glycoconjugates in suspension-cultured cells of Arabidopsis thaliana and suggest that a genetic and enzymatic basis for sialylation exists in plants.

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Figure 1: Detection of sialyoglycoproteins from A. thaliana suspension-cultured cells using biotinylated SNA-I and MAA lectins.
Figure 2: Elution profiles of DMB-sialic acid derivatives from reversed-phase C18 chromotography using isocratic conditions of 9% acetonitrile, 7% methanol and 84% water at the flow rate of 0.65 ml/min.

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Acknowledgements

This study was supported by the Wallace Research Foundation and by the Arizona Biodesign Institute. We thank Charles J. Arntzen and J. Kenneth Hoober for advice and discussions, and Daniel Brune and Amy Smith for mass spectrometric analyses.

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Correspondence to Lokesh Joshi.

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The authors declare no competing financial interests.

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Shah, M., Fujiyama, K., Flynn, C. et al. Sialylated endogenous glycoconjugates in plant cells. Nat Biotechnol 21, 1470–1471 (2003). https://doi.org/10.1038/nbt912

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