Open AccessThe productton of hybrid Ty: IFN virus-like particles in yeast
Author(s) -
Michael H. Malim,
Sally E. Adams,
Keith Gull,
Alan J. Kingsman,
Susan M. Kingsman
Publication year - 1987
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/15.18.7571
Subject(s) - biology , heterologous , yeast , fusion protein , gene , microbiology and biotechnology , virus like particle , saccharomyces cerevisiae , fusion gene , coding region , two hybrid screening , interferon , virus , virology , recombinant dna , genetics
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.