Expression of human CMP-N-acetylneuraminic acid synthetase and CMP-sialic acid transporter in tobacco suspension-cultured cell

Biochem Biophys Res Commun. 2006 Jan 27;339(4):1184-9. doi: 10.1016/j.bbrc.2005.11.130. Epub 2005 Dec 5.

Abstract

Plant cells have no beta1,4-galactosylated and sialylated glycan, which plays important roles in biological functions in animal cells. Previously, we generated transgenic tobacco BY2 suspension-cultured cells that produced human beta1,4-galactosyltransferase [N.Q. Palacpac, S. Yoshida, H. Sakai, Y. Kimura, K. Fujiyama, T. Yoshida, T. Seki, Stable expression of human beta1,4-galactosyltransferase in plant cells modifies N-linked glycosylation pattern, Proc. Natl. Acad. Sci. USA 96 (1999) 4692-4697]. In this study, we introduced two critical genes encoding human CMP-N-acetylneuraminic acid synthetase and CMP-sialic acid transporter into tobacco suspension-cultured cell to pave a route for sialic biosynthetic pathway. The recombinant human proteins showed their biological activities. These results show that the plant cell can be a useful bioreactor for the production of mammalian glycoproteins.

MeSH terms

  • Cells, Cultured
  • Gene Expression Regulation, Plant / physiology
  • Glycoproteins / biosynthesis
  • Humans
  • N-Acetylneuraminic Acid / biosynthesis*
  • N-Acylneuraminate Cytidylyltransferase / genetics
  • N-Acylneuraminate Cytidylyltransferase / metabolism*
  • Nicotiana / genetics
  • Nicotiana / metabolism*
  • Nucleotide Transport Proteins / genetics
  • Nucleotide Transport Proteins / metabolism*
  • Plants, Genetically Modified / metabolism*
  • Protein Engineering / methods*
  • Recombinant Proteins / biosynthesis

Substances

  • Glycoproteins
  • Nucleotide Transport Proteins
  • Recombinant Proteins
  • SLC35A1 protein, human
  • N-Acylneuraminate Cytidylyltransferase
  • N-Acetylneuraminic Acid