Galatosylation and sialylation of mammalian glycoproteins produced by baculovirus-madiated gene expression in insect cells

Biotechnol Lett. 2005 Jul;27(14):1035-9. doi: 10.1007/s10529-005-8107-2.

Abstract

The baculovirus expression vector system (BEVS) is used extensively for the production of proteins from exogenous cDNAs. However, BEVS is not ideal for pharmaceutical production of glycoproteins owing to the properties of the N-glycans in the expressed products and that insect cells lack several of the enzymes required for mammalian-type N-glycan synthesis. This study describes the effective mammalian-like production of glycoproteins, such as beta-1,4-galactosyltransferase and alpha-2,6-sialyltransferase, in the insect cell line Sf9.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Baculoviridae*
  • Glycosylation
  • Humans
  • Protein Modification, Translational / genetics*
  • Rats
  • Recombinant Proteins / biosynthesis*
  • Recombinant Proteins / genetics
  • Sialyltransferases / biosynthesis*
  • Sialyltransferases / genetics
  • Spodoptera
  • beta-D-Galactoside alpha 2-6-Sialyltransferase

Substances

  • Recombinant Proteins
  • Sialyltransferases
  • N-acetyllactosaminide alpha-2,3-sialyltransferase
  • beta-D-Galactoside alpha 2-6-Sialyltransferase