Evidence that the endosomal sorting complex required for transport-II (ESCRT-II) is required for efficient human immunodeficiency virus-1 (HIV-1) production
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BACKGROUND: Egress of a number of different virus species from infected cells depends on proteins of the endosomal sorting complexes required for transport (ESCRT) pathway. HIV has also hijacked this system to bud viruses outward from the cell surface. How ESCRT-I activates ESCRT-III in this process remains unclear with conflicting published evidence for the requirement of ESCRT-II which fulfils this role in other systems. We investigated the role of ESCRT-II using knockdown mediated by siRNA and shRNA, mutants which prevent ESCRT-I/ESCRT-II interaction and a CRISPR/Cas9 EAP45 knockout cell line. RESULTS: Depletion or elimination of ESCRT-II components from an HIV infected cell produces two distinct effects. The overall production of HIV-1 Gag is reduced leading to a diminished amount of intracellular virion protein. In addition depletion of ESCRT-II produces an effect similar to that seen when ESCRT-I and -III components are depleted, that of a delayed Gag p26 to p24 +p2 cleavage associated with a reduction in export of virion particles and a visible reduction in budding efficiency in virus producing cells. Mutants that interfere with ESCRT-I interacting with ESCRT-II similarly reduce virus export. The export defect is independent of the decrease in overall Gag production. Using a mutant virus which cannot use the ALIX mediated export pathway exacerbates the decrease in virus export seen when ESCRT-II is depleted. ESCRT-II knockdown does not lead to complete elimination of virus release suggesting that the late domain role of ESCRT-II is required for optimal efficiency of viral budding but that there are additional pathways that the virus can employ to facilitate this. CONCLUSION: ESCRT-II contributes to efficient HIV virion production and export by more than one pathway; both by a transcriptional or post transcriptional mechanism and also by facilitating efficient virus export from the cell through interactions with other ESCRT components.
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Loss of ALIX recruitment to viral budding sites or cytokinetic bridges impairs but does not terminate these events.
“the loss of ALIX recruitment to viral budding sites through HIV L domain deletion or to cytokinetic bridges via cellular depletion by RNA interference (RNAi) impairs but does not terminate these events.”
From Budding of a Retrovirus: Some Assemblies Required (2020) · cites this paper as [18]
The Background identifies the YPXL motif as the route by which HIV-1 Gag recruits ALIX, and the Results (‘Knockdown of ESCRT-II has an additive effect on release of YPXL mutant virus’; page unavailable) report reduced, rather than abolished, virion export after YPXL mutation. Our copy does not report ALIX depletion by RNAi at cytokinetic bridges or its effect on cytokinesis; its discussion of cytokinesis concerns ESCRT-II. (LLM, conf=0.87)
Experimental — accuracy not yet measuredRedundant and parallel ESCRT-III recruiting axes are mandated.
“This mandates the presence of redundant and parallel ESCRT-III recruiting axes perhaps fulfilled by the intermediary ESCRT-II complex [13,17,18] or additional ALIX homologs and orthologs [19,20,21].”
From Budding of a Retrovirus: Some Assemblies Required (2020) · cites this paper as [18]
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Meusser, B., Purfürst, B., & Luft, F. C. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014710 · Cited by 10 · see citing works
ESCRT-III on endosomes: new functions, new activation pathway
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Pathways Toward a Functional HIV-1 Cure: Balancing Promise and Perils of CRISPR Therapy
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Exosomes and Their Role in Viral Infections
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Extracellular vesicles: the double-edged sword in viral infections
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- Authors
- Meng, B., Ip, N. C. Y., Prestwood, L. J., Abbink, T. E. M., & Lever, A. M. L.
- Affiliations
- University of Cambridge (GB)
- Corresponding author
- Lever, Andrew M L
- Venue
- Retrovirology
- Published
- 2015-08-14
- Volume
- 12
- Issue
- 1
- Pages
- 72-72
- ISSN
- 1742-4690 (ISSN-L)
- PMC
- PMC4535389
- OpenAlex
- W2147257015
- Cited by
- 65
- References
- 52
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 4 · 2023: 4 · 2022: 4 · 2021: 6 · 2020: 12 · 2019: 6 · 2018: 8 · 2017: 7 · 2016: 7 · 2015: 1
- FWCI
- 3.88
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Retrovirology (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Pure Amsterdam UMC (publishedVersion, other-oa)
- Amsterdam UMC (VU Amsterdam) - Institutional Repository (publishedVersion)
- National University of Singapore (submittedVersion, cc-by)
- VU Research Portal (submittedVersion, other-oa)
- Data Archiving and Networked Services (DANS) (submittedVersion, other-oa)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Funders
- University of Cambridge Clinical School MB/PhD Programme, Frank Edward Elmore Fund and James Baird Fund, Magdalene College Leslie Wilson Minor Award, and Overseas Research Students Awards Scheme (RCAG/032)
- Medical Research Council (RCAG/269)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Virus-based gene therapy research
- Keywords
- ESCRT-II, HIV-1, viral budding, late domain, Gag processing, Alix, ESCRT-I, ESCRT-III
- MeSH terms
- Biological Transport, Cell Line, Humans, Mutation, Protein Binding, Virion, HIV-1, Protein Structure, Tertiary, RNA, Small Interfering, gag Gene Products, Human Immunodeficiency Virus, Gene Knockout Techniques, Endosomal Sorting Complexes Required for Transport, Virus Release, CRISPR-Cas Systems
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