Analyses of chicken sialyltransferases related to N-glycosylation

Yusuke Kojima, Akifumi Mizutani, Yuya Okuzaki, Ken ichi Nishijima, Hidenori Kaneoka, Takako Sasamoto, Katsuhide Miyake, Shinji Iijima

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Proteins exogenously expressed and deposited in the egg whites of transgenic chickens did not contain terminal sialic acid in their N-glycan. Since this sugar is important for the biological stability of therapeutic proteins, we examined chicken sialyltransferases (STs). Based on homologies in DNA sequences, we cloned and expressed several chicken STs, which appeared to be involved in N-glycosylation in mammals, in 293FT cells. Enzymatic activity was detected with ST3Gal3, ST3Gal6 and ST6Gal1 using galactose-β1,4- N-acetylglucosamine (Galβ1,4GlcNAc) as an acceptor. Using Golgi fractions from the cell-free extracts of chicken organs, α2,3- and/or α2,6-ST activities were detected in the liver and kidney, but were absent in the oviduct cells in which egg-white proteins were produced. This result suggested that the lack of ST activities in oviduct cells mainly caused the lack of sialic acid in the N-glycan of proteins exogenously expressed and deposited in egg white.

Original languageEnglish
Pages (from-to)623-628
Number of pages6
JournalJournal of Bioscience and Bioengineering
Volume119
Issue number6
DOIs
Publication statusPublished - Jun 1 2015

Keywords

  • Chicken
  • N-Glycosylation
  • Oviduct
  • Sialic acid
  • Sialyltransferase
  • Transgenic chicken

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

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  • Cite this

    Kojima, Y., Mizutani, A., Okuzaki, Y., Nishijima, K. I., Kaneoka, H., Sasamoto, T., Miyake, K., & Iijima, S. (2015). Analyses of chicken sialyltransferases related to N-glycosylation. Journal of Bioscience and Bioengineering, 119(6), 623-628. https://doi.org/10.1016/j.jbiosc.2014.11.009