ArticleJournal of virology2003
Elimination of protease activity restores efficient virion production to a human immunodeficiency virus type 1 nucleocapsid deletion mutant.
Article in Journal of virology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 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.
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Who cites it
39 citing papers in PubMed, 56 citations in OpenAlex.
- Evasion of CARD8 activation during HIV-1 assembly.Science advances · 2025Article
- A high-throughput approach to evaluating NCp7 RNA binding activity for HIV-1 drug discovery.SLAS discovery : advancing life sciences R & D · 2025Article
- Structural Determinants of Virion Assembly and Release in the C Terminus of the Mason-Pfizer Monkey Virus Capsid Protein.Journal of virology · 2021Article
- Non-active site mutants of HIV-1 protease influence resistance and sensitisation towards protease inhibitors.Retrovirology · 2020Article
- Inhibition of HIV Maturation via Selective Unfolding and Cross-Linking of Gag Polyprotein by a Mercaptobenzamide Acetylator.Journal of the American Chemical Society · 2019Article
- Retroviral Gag protein-RNA interactions: Implications for specific genomic RNA packaging and virion assembly.Seminars in cell & developmental biology · 2019Review
- Inhibition of HIV-1 Gag-membrane interactions by specific RNAs.RNA (New York, N.Y.) · 2017Article
- Functional Equivalence of Retroviral MA Domains in Facilitating Psi RNA Binding Specificity by Gag.Viruses · 2016Article
- The Host RNAs in Retroviral Particles.Viruses · 2016Review
- The matrix domain contributes to the nucleic acid chaperone activity of HIV-2 Gag.Retrovirology · 2016Article
- Live-cell observation of cytosolic HIV-1 assembly onset reveals RNA-interacting Gag oligomers.The Journal of cell biology · 2015Article
- HIV-1 matrix domain removal ameliorates virus assembly and processing defects incurred by positive nucleocapsid charge elimination.FEBS open bio · 2015Article
- Murine leukemia virus Gag localizes to the uropod of migrating primary lymphocytes.Journal of virology · 2014Article
- Retrovirus-specific differences in matrix and nucleocapsid protein-nucleic acid interactions: implications for genomic RNA packaging.Journal of virology · 2014Article
- Elements in HIV-1 Gag contributing to virus particle assembly.Virus research · 2013Article
- Extreme genetic fragility of the HIV-1 capsid.PLoS pathogens · 2013Article
- Functional redundancy in HIV-1 viral particle assembly.Journal of virology · 2012Article
- Human endogenous retrovirus K Gag coassembles with HIV-1 Gag and reduces the release efficiency and infectivity of HIV-1.Journal of virology · 2012Article
- Budding of retroviruses utilizing divergent L domains requires nucleocapsid.Journal of virology · 2012Article
- Solution properties of murine leukemia virus gag protein: differences from HIV-1 gag.Journal of virology · 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
8 authors at 2 institutions in 1 country.
Funding
Abstract
The nucleocapsid (NC) region of human immunodeficiency virus type 1 (HIV-1) Gag is required for specific genomic RNA packaging. To determine if NC is absolutely required for virion formation, we deleted all but seven amino acids from NC in a full-length NL4-3 proviral clone. This construct, DelNC, produced approximately four- to sixfold fewer virions than did the wild type, and these virions were noninfectious (less than 10(-6) relative to the wild type) and severely genomic RNA deficient. Immunoblot and high-pressure liquid chromatography analyses showed that all of the mature Gag proteins except NC were present in the mutant virion preparations, although there was a modest decrease in Gag processing. DelNC virions had lower densities and were more heterogeneous than wild-type particles, consistent with a defect in the interaction assembly or I domain. Electron microscopy showed that the DelNC virions displayed a variety of aberrant morphological forms. Inactivating the protease activity of DelNC by mutation or protease inhibitor treatment restored virion production to wild-type levels. DelNC-protease mutants formed immature-appearing particles that were as dense as wild-type virions without incorporating genomic RNA. Therefore, protease activity combined with the absence of NC causes the defect in DelNC virion production, suggesting that premature processing of Gag during assembly causes this effect. These results show that HIV-1 can form particles efficiently without NC.
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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.