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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.


Journal article


Nucleic Acids Res

Publication Date





7571 - 7580


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