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The yeast retrotransposon Ty encodes proteins that assemble into virus-like particles (Ty-VLPs) which can be readily purified. We have recently shown that expression of the pl protein encoded by the TYA gene of Ty is sufficient for particle formation. In this paper we show that when a heterologous coding sequence, human interferon-alpha 2 (IFN), is fused in frame to the TYA gene, the resulting p1-IFN fusion protein is still assembled into VLPs. These Ty:IFN-VLPs can be easily purified to near homogeneity and furthermore, they induce an antibody response to interferon when they are injected into rabbits. Therefore, these data show that hybrid Ty-VLPs can be used as a convenient system for the efficient purification of fusion proteins in yeast.

Type

Journal article

Journal

Nucleic Acids Res

Publication Date

25/09/1987

Volume

15

Pages

7571 - 7580

Keywords

Animals, Cloning, Molecular, DNA Transposable Elements, Gene Expression Regulation, Genetic Vectors, Interferon Type I, Plasmids, Rabbits, Recombinant Fusion Proteins, Recombinant Proteins, Saccharomyces cerevisiae