N-linked glycan structures of mouse interferon-beta produced by Bombyx mori larvae

Biochem Biophys Res Commun. 2003 Nov 28;311(4):979-86. doi: 10.1016/j.bbrc.2003.10.094.


The full-length mouse interferon-beta (mIFN-beta) cDNA, including the secretion signal peptide coding region under control of the polyhedrin promoter, was introduced into Bombyx mori nucleopolyhedrovirus (BmNPV). Recombinant mIFN-beta (rmIFN-beta) was accumulated in the haemolymph of infected silkworm larvae. Western blot analysis showed isoforms of rmIFN-beta, suggesting that rmIFN-beta is glycosylated. The glycan structures of purified rmIFN-beta were determined. The N-glycans were liberated by hydrazinolysis and the resulting oligosaccharides were labeled with 2-aminopyridine. The pyridylaminated (PA) glycans were purified by gel filtration, reversed-phase HPLC, and size-fractionation HPLC. The structures of the PA-sugar chains were identified by a combination of two-dimensional PA-sugar chain mapping, MS analysis, and exoglycosidase digestions.

Publication types

  • Comparative Study

MeSH terms

  • Animals
  • Bombyx
  • Interferon-beta / chemistry*
  • Interferon-beta / genetics
  • Interferon-beta / metabolism*
  • Larva
  • Mice
  • Molecular Weight
  • Polysaccharides / chemistry*
  • Polysaccharides / metabolism*
  • Protein Conformation
  • Protein Engineering / methods
  • Protein Isoforms / chemistry
  • Protein Isoforms / metabolism
  • Protein Structure, Tertiary
  • Recombinant Proteins
  • Species Specificity
  • Structure-Activity Relationship


  • Polysaccharides
  • Protein Isoforms
  • Recombinant Proteins
  • Interferon-beta