ArticleThe Journal of biological chemistry2011
Evidence of a role for soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) machinery in HIV-1 assembly and release.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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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
18 citing papers in PubMed, 32 citations in OpenAlex.
- Review
- Dynamics of the blood plasma proteome during hyperacute HIV-1 infection.Nature communications · 2024Article
- Subtype Differences in the Interaction of HIV-1 Matrix with Calmodulin: Implications for Biological Functions.Biomolecules · 2021Article
- How HIV-1 Gag Manipulates Its Host Cell Proteins: A Focus on Interactors of the Nucleocapsid Domain.Viruses · 2020Review
- Specificities of secretion and uptake of exosomes and other extracellular vesicles for cell-to-cell communication.Nature cell biology · 2019Review
- Roles of Cellular NSF Protein in Entry and Nuclear Egress of Budded Virions of Autographa californica Multiple Nucleopolyhedrovirus.Journal of virology · 2017Article
- Induction of Antihuman C-C Chemokine Receptor Type 5 Antibodies by a Bovine Herpesvirus Type-4 Based Vector.Frontiers in immunology · 2017Article
- High-efficiency antibody discovery achieved with multiplexed microscopy.Microscopy (Oxford, England) · 2016Article
- TIM-family proteins inhibit HIV-1 release.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Solution structure of calmodulin bound to the binding domain of the HIV-1 matrix protein.The Journal of biological chemistry · 2014Article
- Molecular Events in Late Stages of HIV-1 Replication.JSM microbiology · 2013Article
- Human Ubc9 is involved in intracellular HIV-1 Env stability after trafficking out of the trans-Golgi network in a Gag dependent manner.PloS one · 2013Article
- Defective HIV-1 particle assembly in AP-3-deficient cells derived from patients with Hermansky-Pudlak syndrome type 2.Journal of virology · 2012Article
- SNAREs in HIV-1 assembly.Communicative & integrative biology · 2012Article
- Loss of soluble N-ethylmaleimide-sensitive factor attachment protein α (αSNAP) induces epithelial cell apoptosis via down-regulation of Bcl-2 expression and disruption of the Golgi.The Journal of biological chemistry · 2012Article
- HIV type 1 Gag as a target for antiviral therapy.AIDS research and human retroviruses · 2012Review
- HIV Assembly and Budding: Ca(2+) Signaling and Non-ESCRT Proteins Set the Stage.Molecular biology international · 2012Article
- Role of the HIV-1 Matrix Protein in Gag Intracellular Trafficking and Targeting to the Plasma Membrane for Virus Assembly.Frontiers in microbiology · 2012Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Retrovirus assembly is a complex process that requires the orchestrated participation of viral components and host-cell factors. The concerted movement of different viral proteins to specific sites in the plasma membrane allows for virus particle assembly and ultimately budding and maturation of infectious virions. The soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins constitute the minimal machinery that catalyzes the fusion of intracellular vesicles with the plasma membrane, thus regulating protein trafficking. Using siRNA and dominant negative approaches we demonstrate here that generalized disruption of the host SNARE machinery results in a significant reduction in human immunodeficiency virus type 1 (HIV-1) and equine infectious anemia virus particle production. Further analysis of the mechanism involved revealed a defect at the level of HIV-1 Gag localization to the plasma membrane. Our findings demonstrate for the first time a role of SNARE proteins in HIV-1 assembly and release, likely by affecting cellular trafficking pathways required for Gag transport and association with the plasma membrane.
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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.