Structure and Activity of Recombinant Human Interferon-γ Analogs

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Abstract
We have prepared interferon-γ (IFN-γ) analogs to study the structural role of particular amino acids in relation to their effects on antiviral activity. Three IFN-γ analogs were prepared on the basis of predicted secondary structure. In two of the analogs, [Gln25]-IFN-γ and [Thr45]IFN-γ, changes were made at residue 25 (Asn to Gln) and at residue 45 (Met to Thr), respectively. [Gln25Lys78]IFN-γ had two changes, at residue 25 (Asn to Gln) and residue 78 (Asn to Lys). Another analog, [Cys-Tyr-Cys]IFN-γ, incorporated Cys-Tyr-Cys at the amino terminus. Comparison of the structure and activity of these analogs with that of the natural sequence protein suggested that residues 25 and 78 are at the protein surface and play an important role in antiviral activity. The residue at position 45 was found to be important for maintaining the protein structure, as assessed by circular dichroism spectroscopy. The addition of Cys-Tyr-Cys resulted in a small perturbation of protein structure and a small decrease in antiviral activity.

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