Bouamr F, Loomis BR, De Los Santos M, Goff SP; HIV DRP Symposium Antiviral Drug Resistance (4th: 2003: Chantilly, Va.).
Program Abstr HIV DRP Symp Antivir Drug Resist. 2003 Dec 7-10; 4: Abstract no. 68.
Howard Hughes Medical Institute
Retroviral Gag proteins contain short domains called Late domains, or L domains, that facilitate the final stages of viral budding by recruiting cellular proteins normally involved in cellular trafficking and sorting of membrane proteins into multivesicular bodies and lysosomes. A major player in this process, the cellular protein Tsg101, binds the PTAP motif in HIV-1 and HTLV-I Gag proteins; this interaction is required for the budding and release of both viruses. Recently an interaction between Tsg101 and Hrs, an early endosomal protein, was described. It was hypothesized that HIV-1 Gag, and most likely HTLV-I Gag, mimics Hrs to attract Tsg101 to the site of viral budding. Co-immunoprecipitation analysis showed that Tsg101 and Hrs are found in a complex in the cell. Expression of HIV-1 Gag in 293T cells diminished the amounts of Hrs protein pulled down by Tsg101. We and others showed that the C-terminal region of Hrs is important for its binding to Tsg101 in a yeast two hybrid assay. We co-expressed various domains of Hrs with HIV-1 Gag in 293T cells and showed that only a fragment carrying the C-terminal region of the protein interfered with the release of HIV-1. Data showing the effect of other Hrs mutations on HIV-1 budding and release will be presented and discussed.
Publication Types:
Keywords:
- Gene Products, gag
- Genes, gag
- HIV-1
- Human T-lymphotropic virus 1
- Phosphoproteins
- Protein Transport
- Two-Hybrid System Techniques
- genetics
- hepatocyte growth factor-regulated tyrosine kinase substrate
Other ID:
UI: 102268493
From Meeting Abstracts