ArticleJournal of virology2002
Blockade of human immunodeficiency virus type 1 expression by caveolin-1.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.
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.
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Who cites it
17 citing papers in PubMed, 1 synthesis or guideline pooled it, 26 citations in OpenAlex.
- Multiple Inhibitory Factors Act in the Late Phase of HIV-1 Replication: a Systematic Review of the Literature.Microbiology and molecular biology reviews : MMBR · 2018Pooled it
- Occludin, caveolin-1, and Alix form a multi-protein complex and regulate HIV-1 infection of brain pericytes.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Review
- Pharmacological Inhibition of PPARy Boosts HIV Reactivation and Th17 Effector Functions, While Preventing Progeny Virion Release and dePathogens & immunity · 2020Article
- Review
- Identification of molecular sub-networks associated with cell survival in a chronically SIVmac-infected human CD4+ T cell line.Virology journal · 2014Article
- Establishing Restricted Expression of Caveolin-1 in HIV Infected Cells and Inhibition of Virus Replication.The open microbiology journal · 2014Article
- Caveolin-1 suppresses human immunodeficiency virus-1 replication by inhibiting acetylation of NF-κB.Virology · 2012Article
- Caveolin 1 inhibits HIV replication by transcriptional repression mediated through NF-κB.Journal of virology · 2011Article
- New glimpses of caveolin-1 functions in embryonic development and human diseases.Frontiers in biology · 2011Review
- HIV infection upregulates caveolin 1 expression to restrict virus production.Journal of virology · 2010Article
- Caveolin-1 modulates HIV-1 envelope-induced bystander apoptosis through gp41.Journal of virology · 2010Article
- Caveolin-1 influences human influenza A virus (H1N1) multiplication in cell culture.Virology journal · 2010Article
- HIV-1 assembly: viral glycoproteins segregate quantally to lipid rafts that associate individually with HIV-1 capsids and virions.Cell host & microbe · 2008Article
- Discovering regulated networks during HIV-1 latency and reactivation.Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing · 2006Article
- LEDGF/p75 determines cellular trafficking of diverse lentiviral but not murine oncoretroviral integrase proteins and is a component of functional lentiviral preintegration complexes.Journal of virology · 2004Article
- Interactions between calcium regulatory pathways and mechanosensitive channels in airways.Expert review of respiratory medicineReview
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Caveolin-1 (Cav-1) is a major protein constituent of caveolae, a type of plasma membrane raft. We observed that coexpression of human Cav-1 with human immunodeficiency virus type 1 (HIV-1) blocked virion production from cells that are ordinarily highly permissive. Further investigation showed that this effect is specific, occurs at low ratios of Cav-1 to HIV-1 DNA, depends on expression of Cav-1 protein, and involves severely impaired expression of HIV-1 proteins. Cav-1 also blocked HIV-2 expression. In contrast, Cav-1 did not inhibit protein expression by a paramyxovirus and did not induce apoptosis or affect cellular morphology, cell viability, or cell cycle progression. Although only small amounts of HIV-1 virions were released from Cav-1-transfected cells, these were fully infectious. Deletion mutagenesis showed that the C-terminal 78 residues were as active as the full-length (178-amino-acid) protein in producing the block. In contrast, the 100 most N-terminal amino acids of Cav-1, which include the previously identified oligomerization and scaffolding domains, were shown to be dispensable. Study of single-amino-acid-exchange mutants of Cav-1 established that palmitoylation was not required. Additional deletion mutants then identified the hydrophobic, membrane-associated domain (residues 101 to 135) as the main determinant. Cellular distribution of wild-type and mutant proteins correlated with ability to block HIV-1 expression. Finally, Cav-2 also blocked HIV-1 expression. These data show that coexpression of caveolins can markedly inhibit expression of HIV proviral DNA and establish that the inhibition is mediated by the hydrophobic, membrane-associated 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.