ArticleJournal of virology2003
Functional surfaces of the human immunodeficiency virus type 1 capsid protein.
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 292 papers.
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Who cites it
292 citing papers in PubMed, 418 citations in OpenAlex.
- The Central Pore of HIV-1 Capsomers Promotes Sustained Stability of the Viral Capsid.Journal of molecular biology · 2026Article
- Mis-localized nucleoporin POM121C potently inhibits nuclear entry of HIV-1 but leads to the outgrowth of viral escape mutants.Journal of virology · 2026Article
- Capsid-Targeting Biologic Achieves Broad HIV-1 Neutralization with a High Barrier to Resistance.International journal of molecular sciences · 2026Article
- Anti-capsid nanobodies function as HIV-1 capsid inhibitors by intracellular capsid degradation.Communications biology · 2026Article
- HIV capsid inhibitors: Mechanisms, resistance, and therapeutic advances.PLoS pathogens · 2026Review
- Atomistic characterization of the maturation mechanisms in the HIV-1 capsid domain.Nature communications · 2026Article
- Article
- Damaging the conical morphology of HIV-1 capsid by targeting the FG-binding pocket and disfavoring pentameric subunits needed for core closure.bioRxiv : the preprint server for biology · 2026Article
- Transient Occupancy and Pore Dynamics: IP6 Behavior in HIV-1The journal of physical chemistry. B · 2026Article
- Nuclear pore passage of the HIV capsid is driven by its unusual surface amino acid composition.Nature structural & molecular biology · 2025Article
- Discovery of Lenacapavir: First-in-Class Twice-Yearly Capsid Inhibitor for HIV-1 Treatment and Pre-exposure Prophylaxis.Journal of medicinal chemistry · 2025Article
- Preclinical virology profiles of the HIV-1 capsid inhibitors VH4004280 and VH4011499.Antimicrobial agents and chemotherapy · 2025Article
- Impact of HIV-1 capsid polymorphisms on viral infectivity and susceptibility to lenacapavir.mBio · 2025Article
- Distinct stabilization of the human T cell leukemia virus type 1 immature Gag lattice.Nature structural & molecular biology · 2025Article
- Cell-free assays reveal that the HIV-1 capsid protects reverse transcripts from cGAS immune sensing.PLoS pathogens · 2025Article
- The role of HIV-1 Gag and genomic RNA interactions in virion assembly.Frontiers in microbiology · 2025Article
- Determinants in the HTLV-1 Capsid Major Homology Region that are Critical for Virus Particle Assembly.Journal of molecular biology · 2024Article
- The Assembly of HTLV-1-How Does It Differ from HIV-1?Viruses · 2024Review
- Human Immunodeficiency Virus Type 1 Gag Polyprotein Modulates Membrane Physical Properties like a Surfactant: Potential Implications for Virus Assembly.ACS infectious diseases · 2024Article
- Arg18 Substitutions Reveal the Capacity of the HIV-1 Capsid Protein for Non-Fullerene Assembly.Viruses · 2024Article
232 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
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human immunodeficiency virus type 1 initially assembles and buds as an immature particle that is organized by the viral Gag polyprotein. Gag is then proteolyzed to produce the smaller capsid protein CA, which forms the central conical capsid that surrounds the RNA genome in the mature, infectious virus. To define CA surfaces that function at different stages of the viral life cycle, a total of 48 different alanine-scanning surface mutations in CA were tested for their effects on Gag protein expression, processing, particle production and morphology, capsid assembly, and infectivity. The 27 detrimental mutations fall into three classes: 13 mutations significantly diminished or altered particle production, 9 mutations failed to assemble normal capsids, and 5 mutations supported normal viral assembly but were nevertheless reduced more than 20-fold in infectivity. The locations of the assembly-defective mutations implicate three different CA surfaces in immature particle assembly: one surface encompasses helices 4 to 6 in the CA N-terminal domain (NTD), a second surrounds the crystallographically defined CA dimer interface in the C-terminal domain (CTD), and a third surrounds the loop preceding helix 8 at the base of the CTD. Mature capsid formation required a distinct surface encompassing helices 1 to 3 in the NTD, in good agreement with a recent structural model for the viral capsid. Finally, the identification of replication-defective mutants with normal viral assembly phenotypes indicates that CA also performs important nonstructural functions at early stages of the viral life cycle.
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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.