The glycosylation heterogeneity of recombinant human IFN-gamma

J Interferon Cytokine Res. 1998 May;18(5):287-95. doi: 10.1089/jir.1998.18.287.

Abstract

The cloning of the cDNA for human interferon-gamma (IFN-gamma) has resulted in its expression in Escherichia coli, baculovirus-infected insect cells, Chinese hamster ovary (CHO) cells, and the mammary gland of transgenic mice. Large quantities of highly purified recombinant IFN-gamma have been generated, aided by the use of highly specific neutralizing monoclonal antibodies, with a view to its production as a human therapeutic protein. The primary source of structural heterogeneity for IFN-gamma during its production in mammalian expression systems is glycosylation, which can profoundly affect the three-dimensional structure of a glycoprotein and its biological function. A number of analytical approaches have been developed recently to allow a detailed analysis of the carbohydrate structures associated with IFN-gamma, the principal advances being in the areas of capillary electrophoresis and mass spectrometry. The implementation of these high-resolution analytical tools to determine the glycosylation profile of IFN-gamma makes it one of the best characterized recombinant glycoproteins. Recombinant human IFN-gamma acts as a model secretory glycoprotein, typifying the intrinsic glycosylation processing events associated with production of a potential therapeutic glycoprotein.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • CHO Cells
  • Cricetinae
  • Electrophoresis, Capillary / methods
  • Glycopeptides / analysis*
  • Glycosylation
  • Humans
  • Interferon-gamma / chemistry*
  • Mass Spectrometry / methods
  • Mice
  • Oligosaccharides / analysis*
  • Recombinant Proteins
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Substances

  • Glycopeptides
  • Oligosaccharides
  • Recombinant Proteins
  • Interferon-gamma