ArticleJournal of virology2009
Divergent Bro1 domains share the capacity to bind human immunodeficiency virus type 1 nucleocapsid and to enhance virus-like particle production.
Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
30 citing papers in PubMed, 47 citations in OpenAlex.
- Nonlytic cellular release of hepatitis A virus requires dual capsid recruitment of the ESCRT-associated Bro1 domain proteins HD-PTP and ALIX.PLoS pathogens · 2022Article
- Review
- How HIV-1 Gag Manipulates Its Host Cell Proteins: A Focus on Interactors of the Nucleocapsid Domain.Viruses · 2020Review
- Zinc Fingers in HIV-1 Gag Precursor Are Not Equivalent for gRNA Recruitment at the Plasma Membrane.Biophysical journal · 2020Article
- Factors promoting nuclear envelope assembly independent of the canonical ESCRT pathway.The Journal of cell biology · 2020Article
- Inside job: how the ESCRTs release HIV-1 from infected cells.Biochemical Society transactions · 2018Review
- Structural Study of the HD-PTP Bro1 Domain in a Complex with the Core Region of STAM2, a Subunit of ESCRT-0.PloS one · 2016Article
- Virus budding and the ESCRT pathway.Cell host & microbe · 2013Review
- Membrane fission reactions of the mammalian ESCRT pathway.Annual review of biochemistry · 2013Review
- Alix serves as an adaptor that allows human parainfluenza virus type 1 to interact with the host cell ESCRT system.PloS one · 2013Article
- Interactions of the human LIP5 regulatory protein with endosomal sorting complexes required for transport.The Journal of biological chemistry · 2012Article
- Dynamics of ESCRT proteins.Cellular and molecular life sciences : CMLS · 2012Review
- HIV-1 assembly, budding, and maturation.Cold Spring Harbor perspectives in medicine · 2012Review
- Two distinct binding modes define the interaction of Brox with the C-terminal tails of CHMP5 and CHMP4B.Structure (London, England : 1993) · 2012Article
- The Phe105 loop of Alix Bro1 domain plays a key role in HIV-1 release.Structure (London, England : 1993) · 2011Article
- The role of cellular factors in promoting HIV budding.Journal of molecular biology · 2011Review
- Host factors involved in retroviral budding and release.Nature reviews. Microbiology · 2011Review
- Alix regulates egress of hepatitis B virus naked capsid particles in an ESCRT-independent manner.Cellular microbiology · 2011Article
- Dynamics of ESCRT protein recruitment during retroviral assembly.Nature cell biology · 2011Article
- Structure of the Bro1 domain protein BROX and functional analyses of the ALIX Bro1 domain in HIV-1 budding.PloS one · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
To promote the release of infectious virions, human immunodeficiency virus type 1 (HIV-1) exploits the endosomal sorting complex required for transport (ESCRT) pathway by engaging Tsg101 and ALIX through late assembly (L) domains in p6 Gag. An LYPx(n)L motif in p6 serves as docking site for the central V domain of ALIX and is required for its ability to stimulate HIV-1 budding. Additionally, the nucleocapsid (NC) domain of Gag binds to the N-terminal Bro1 domain of ALIX, which connects ALIX to the membrane-deforming ESCRT-III complex via its CHMP4 subunits. Since the isolated Bro1 domain of ALIX is sufficient to markedly stimulate virus-like particle (VLP) production in a minimal Gag rescue assay, we examined whether the Bro1 domains of other human proteins possess a similar activity. We now show that the Bro1 domain-only protein Brox and the isolated Bro1 domains of HD-PTP and rhophilin all bind to HIV-1 NC. Furthermore, all shared the capacity to stimulate VLP production by a minimal HIV-1 Gag molecule, and Brox in particular was as potent as the Bro1 domain of ALIX in this assay. Unexpectedly, Brox retained significant activity even if its CHMP4 binding site was disrupted. Thus, the ability to assist in VLP production may be an intrinsic property of the boomerang-shaped Bro1 domain.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.