Single amino acid changes that render human IFN-alpha 2 biologically active on mouse cells.
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.
D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D004262:DNA Restriction Enzymes; D005796:Genes; D006801:Humans; D007370:Interferon Type I / Q000235:genetics* / Q000494:pharmacology; D008574:Mengovirus / Q000187:drug effects; D051379:Mice; D008958:Models, Molecular; D009154:Mutation; D009693:Nucleic Acid Hybridization; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D014721:Vesicular stomatitis Indiana virus / Q000187:drug effects
D007370:Interferon Type I; D004262:DNA Restriction Enzymes