Single amino acid changes that render human IFN-alpha 2 biologically active on mouse cells

EMBO J. 1987 Mar;6(3):591-8. doi: 10.1002/j.1460-2075.1987.tb04795.x.

Abstract

Human IFN-alpha 1 and IFN-alpha 2 differ in 28 of 166 amino acids and show very different specific antiviral activities on human and murine cells. We have identified, by hybrid scanning and site-directed mutagenesis, three residues in IFN-alpha 2, in positions 121, 125 and 132 which, when replaced individually or jointly by their IFN-alpha 1 counterparts, modify its activity on mouse cells by up to 400-fold. We argue that these residues are involved in direct contacts with the mouse interferon receptor.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Line
  • DNA Restriction Enzymes
  • Genes*
  • Humans
  • Interferon Type I / genetics*
  • Interferon Type I / pharmacology
  • Mengovirus / drug effects
  • Mice
  • Models, Molecular
  • Mutation*
  • Nucleic Acid Hybridization
  • Protein Conformation
  • Structure-Activity Relationship
  • Vesicular stomatitis Indiana virus / drug effects

Substances

  • Interferon Type I
  • DNA Restriction Enzymes