Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

The yeast retrotransposon, Ty, encodes a set of proteins that are assembled into virus-like particles, Ty-VLPs (refs 1, 2). These proteins include Ty-VLP structural proteins, a protease that mediates cleavage of primary translation products and a reverse transcriptase. The major structural components of Ty-VLPs are proteolytic products of the primary translation product, p1 (ref. 3). We have recently shown that protein p1 alone can form Ty-VLPs (ref. 3). Here we demonstrate that p1 fusion proteins, comprising most of p1 and part of human immunodeficiency virus (HIV) protein gp120, form hybrid HIV:Ty-VLPs. These hybrid particles provide a rapid means of preparing and evaluating HIV antigens for a variety of immunological purposes.

Original publication




Journal article



Publication Date





68 - 70


Base Sequence, DNA Transposable Elements, Genes, Genes, Fungal, Genes, Viral, HIV, Nucleic Acid Hybridization, Protein Biosynthesis, Saccharomyces cerevisiae, Viral Envelope Proteins