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Updated: Apr 17, 2026
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Visualization of HIV-1 Gag Binding to Giant Unilamellar Vesicle GUV Membranes
Published on: July 28, 2016
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AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding
Bettina Strack1, Arianna Calistri, Stewart Craig
1Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute and Department of Pathology, Harvard Medical School, Boston, MA 02115, USA.
Cell
|September 25, 2003
Summary
Researchers discovered a second crucial region in HIV Gag p6 that binds AIP1, linking viral budding machinery to the ESCRT-III complex. This finding enhances our understanding of retroviral release mechanisms.
Area of Science:
- Virology
- Cell Biology
- Molecular Biology
Background:
- Retroviruses like HIV-1 bud from host cells via membrane fission.
- Viral budding relies on specific protein domains, such as the late assembly (L) domain in HIV-1 Gag p6.
- The L domain recruits host factors, including Tsg101, a part of the vacuolar protein sorting (Vps) machinery.
Purpose of the Study:
- To investigate the complete mechanism of viral budding and identify novel components involved.
- To characterize the function of a second L domain region in HIV-1 Gag p6.
- To elucidate the interaction of HIV-1 Gag p6 with host cell machinery.
Main Methods:
- Biochemical assays to study protein-protein interactions.
- Analysis of viral budding processes in infected cells.
- Identification and characterization of protein homologs in yeast and other viruses.
Main Results:
- HIV Gag p6 possesses a second L domain region that binds AIP1, a homolog of yeast Bro1.
- AIP1 interacts with Tsg101 and components of the ESCRT-III complex.
- AIP1 binding to the L domain in EIAV p9 correlates with L domain function.
Conclusions:
- AIP1 is identified as a key component of the viral budding machinery.
- AIP1 bridges a distinct region of the L domain in HIV-1 p6 and EIAV p9 to the ESCRT-III complex.
- This study reveals a more complex mechanism for retroviral release than previously understood.
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