ESCRT-III protein requirements for HIV-1 budding
Open accessAbstract
Two early-acting components of the cellular ESCRT pathway, ESCRT-I and ALIX, participate directly in HIV-1 budding. The membrane fission activities of ESCRT-III subunits are also presumably required, but humans express 11 different CHMP/ESCRT-III proteins whose functional contributions are not yet clear. We therefore depleted cells of each of the different CHMP proteins and protein families and examined the effects on HIV-1 budding. Virus release was profoundly inhibited by codepletion of either CHMP2 or CHMP4 family members, resulting in ≥100-fold titer reductions. CHMP2A and CHMP4B proteins bound one another, and this interaction was required for budding. By contrast, virus release was reduced only modestly by depletion of CHMP3 and CHMP1 proteins (2- to 8-fold titer reductions) and was unaffected by depletion of other human ESCRT-III proteins. HIV-1 budding therefore requires only a subset of the known human ESCRT-III proteins, with the CHMP2 and CHMP4 families playing key functional roles.
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Membrane scission at the bud neck is mediated by the cellular ESCRT system, which is recruited through linear motifs in Gag.
“Membrane scission at the bud neck is mediated by the cellular ESCRT system, which is recruited through linear motifs in Gag [20].”
From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [20]
Key ESCRT-III components, such as CHMP2 and CHMP4, and VPS4 ATPase, are recruited to the budding site at the plasma membrane.
“key ESCRT-III components, such as charged multivesicular body proteins 2 and 4 (CHMP2 and CHMP4), and the vacuolar protein sorting-associated protein 4 ATPase (VPS4 ATPase), are recruited to the budding site at the plasma membrane”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Morita et al. 2011
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“Membrane scission at the bud neck is mediated by the cellular ESCRT system, which is recruited through linear motifs in Gag [20].”
BackgroundUbiquitin conjugation to Gag is essential for ESCRT-mediated HIV-1 budding
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“These components assemble into spiral filaments on the inner membrane of the budding virion’s neck, facilitating the decisive intrinsic membrane separation necessary for the completion of virion release (Hanson et al. 2008 , Jouvenet et al. 2011b , Morita et al. 2011 , Shen et al. 2014 ).”
- Authors
- Morita, E., Sandrin, V., McCullough, J., Katsuyama, A., Baci Hamilton, I., & Sundquist, W. I.
- Affiliations
- University of Utah (US)
- Corresponding author
- Sundquist, Wesley I.
- Venue
- Cell Host & Microbe
- Publisher
- Elsevier BV
- Published
- 2011-03
- Volume
- 9
- Issue
- 3
- Pages
- 235-242
- ISSN
- 1931-3128 (ISSN-L)
- PMC
- PMC3070458
- OpenAlex
- W2050887754
- Cited by
- 242
- References
- 38
- Citations by year
- 2026: 9 · 2025: 14 · 2024: 13 · 2023: 14 · 2022: 10 · 2021: 22 · 2020: 15 · 2019: 13 · 2018: 9 · 2017: 8 · 2016: 16 · 2015: 24 · 2014: 16 · 2013: 19 · 2012: 28
- FWCI
- 11.51
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Host & Microbe (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- University of Utah
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (AI-051174, R01AI051174, R37AI051174)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Virus-based gene therapy research
- Keywords
- HIV-1 budding, CHMP2A, CHMP4B, CHMP3, membrane fission, viral release, protein-protein interaction, ESCRT pathway
- MeSH terms
- Models, Molecular, Recombinant Proteins, HIV-1, HIV Infections, Mutagenesis, Site-Directed, Virus Assembly, Two-Hybrid System Techniques, RNA Interference, Protein Interaction Domains and Motifs, Endosomal Sorting Complexes Required for Transport, Virus Release
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