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Single amino acid changes that render human IFN‐alpha 2 biologically active on mouse cells.
Author(s) -
Weber H.,
Valenzuela D.,
Lujber G.,
Gubler M.,
Weissmann C.
Publication year - 1987
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1987.tb04795.x
Subject(s) - biology , biological activity , alpha (finance) , amino acid , biochemistry , alpha interferon , microbiology and biotechnology , interferon , immunology , in vitro , medicine , construct validity , nursing , patient satisfaction
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.