ArticleJournal of virology2002
Characterization of a putative alpha-helix across the capsid-SP1 boundary that is critical for the multimerization of human immunodeficiency virus type 1 gag.
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 78 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
78 citing papers in PubMed.
- Article
- Initiation of HIV-1 Gag lattice assembly is required for recognition of the viral genome packaging signal.eLife · 2023Article
- Pseudotyped Viruses for Retroviruses.Advances in experimental medicine and biology · 2023Article
- Review
- Advances in HIV-1 Assembly.Viruses · 2022Review
- HIV-1 capsid variability: viral exploitation and evasion of capsid-binding molecules.Retrovirology · 2021Review
- CryoET structures of immature HIV Gag reveal six-helix bundle.Communications biology · 2021Article
- Inositol phosphates promote HIV-1 assembly and maturation to facilitate viral spread in human CD4+ T cells.PLoS pathogens · 2021Article
- Mechanisms of PI(4,5)P2 Enrichment in HIV-1 Viral Membranes.Journal of molecular biology · 2020Article
- HIV-1 Maturation: Lessons Learned from Inhibitors.Viruses · 2020Review
- Effects of an HIV-1 maturation inhibitor on the structure and dynamics of CA-SP1 junction helices in virus-like particles.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Biochemical Reconstitution of HIV-1 Assembly and Maturation.Journal of virology · 2020Article
- Structures of immature EIAV Gag lattices reveal a conserved role for IP6 in lentivirus assembly.PLoS pathogens · 2020Article
- Resistance to Second-Generation HIV-1 Maturation Inhibitors.Journal of virology · 2019Article
- Retroviral Gag protein-RNA interactions: Implications for specific genomic RNA packaging and virion assembly.Seminars in cell & developmental biology · 2019Review
- HIV-1 Matrix Protein Interactions with tRNA: Implications for Membrane Targeting.Journal of molecular biology · 2018Article
- Conserved Interaction of Lentiviral Vif Molecules with HIV-1 Gag and Differential Effects of Species-Specific Vif on Virus Production.Journal of virology · 2017Article
- Analysis of the functional compatibility of SIV capsid sequences in the context of the FIV gag precursor.PloS one · 2017Article
- Mechanistic Studies and Modeling Reveal the Origin of Differential Inhibition of Gag Polymorphic Viruses by HIV-1 Maturation Inhibitors.PLoS pathogens · 2016Article
- Structure-Activity Relationships of the Human Immunodeficiency Virus Type 1 Maturation Inhibitor PF-46396.Journal of virology · 2016Article
18 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A 14-amino-acid spacer peptide termed SP1 that separates the capsid (CA) and nucleocapsid (NC) sequences plays an active role in the assembly of human immunodeficiency virus type 1. This activity of SP1 involves its amino-terminal residues that, together with adjacent CA residues, constitute a putative alpha-helical structure spanning Gag residues from positions 359 to 371. In this study, we have determined that the virus assembly determinants within this putative alpha-helix were residues H359, K360, A361, L364, A367, and M368, of which K360 and A367 contribute to virus production to lesser extents. Notably, changes of the two basic amino acids H359 and K360 to arginine (R) impaired virus production, whereas mutations L364I and M368I, in contrast to L364A and M368A, generated near-wild-type levels of virus particles. This suggests that within Gag complexes, amino acids H359 and K360 are involved in stricter steric interactions than L364 and M368. Since L364 and M368 are separated by four residues and thus presumably located on the same side of the helical surface, they may initiate synergistic hydrophobic interactions to stabilize Gag association. Further analysis in the context of the protease-negative mutation D185H confirmed the key roles of amino acids H359, A361, L364, and M368 in virus assembly. Importantly, when transfected cells were subjected to Dounce homogenization and the cell lysates were treated by ultracentrifugation at 100,000 x g, Gag molecules containing each of the H359A, A361V, L364A, and M368A mutations were found mainly in the supernatant fraction (S100), whereas approximately 80% of wild-type Gag proteins were found in the pellet. Therefore, these four mutations must have prevented Gag from generating large complexes.
Indexed as
Identifiers
What OpenQuestion holds
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.