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Is sequence conservation in interferons due to selection for functional proteins?

D Valenzuela, H Weber, C Weissmann

    Nature
    |February 21, 1985
    PubMed
    Summary
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    Mutations in conserved residues of human alpha-interferon (IFN-alpha) did not affect its antiviral activity. This suggests that some conserved amino acids in interferons are not essential for function.

    Area of Science:

    • Biochemistry
    • Immunology
    • Molecular Biology

    Background:

    • The human alpha-interferon (IFN-alpha) gene family comprises at least 14 functional members with up to 20% sequence variation.
    • Human IFN-beta is distantly related to IFN-alpha, sharing 33% residue identity, and both interferons are known to compete for the same cellular receptors.

    Purpose of the Study:

    • To investigate the functional importance of conserved amino acid residues in human interferons.
    • To test the hypothesis that evolutionary conservation of residues indicates essentiality for protein function.

    Main Methods:

    • Site-directed point mutagenesis was used to alter strictly conserved codons (48 and 49) in the IFN-alpha 2 gene.
    • Mutant IFN-alpha proteins with substitutions at positions 48 (Phe to Tyr, Ser, Cys) and 49 (Gln to His) were generated.

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  • The antiviral activity of the mutant proteins was compared to that of wild-type IFN-alpha.
  • A mutation at a conserved residue (Glu62 to Lys) in both IFN-alpha and IFN-beta was also tested for its effect on antiviral activity.

    • Main Results:

    • Mutant IFN-alpha proteins with substitutions at positions 48 and 49 exhibited biological activities indistinguishable from wild-type IFN-alpha.
    • Replacing Glu62 with Lys in conserved regions of alpha and beta interferons did not alter antiviral activity.

    Conclusions:

    • The study demonstrates that certain conserved amino acid residues in human interferons are not essential for their antiviral function.
    • These findings challenge the assumption that all evolutionarily conserved residues are critical for protein activity and suggest a more complex relationship between sequence conservation and function in interferons.