ArticleProceedings of the National Academy of Sciences of the United States of America2023
Structural insights into HIV-1 polyanion-dependent capsid lattice formation revealed by single particle cryo-EM.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 47 papers.
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47 citing papers in PubMed, 59 citations in OpenAlex.
- The Central Pore of HIV-1 Capsomers Promotes Sustained Stability of the Viral Capsid.Journal of molecular biology · 2026Article
- Mechanisms of HIV-1 assembly, release and maturation.Nature reviews. Microbiology · 2026Review
- Structural basis of lenacapavir-induced HIV-1 capsid defects during virion maturation.Nature communications · 2026Article
- MxB N-Terminus Adopts a Stable α-Helix to Engage the HIV-1 Capsid Trimer Interface.bioRxiv : the preprint server for biology · 2026Article
- Lenacapavir allosterically remodels the HIV-1 capsid.Science advances · 2026Article
- Retroviruses use different IPNature communications · 2026Article
- HIV-1 capsid interactions with Nuclear Pore Complex components support nuclear entry via affinity gradient.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Article
- A geometric criterion links HIV-1 capsid topography to its biophysical properties and function.Nature communications · 2026Article
- Initiation of Long-Acting Antiretroviral Combinations Achieve Sustained Virologic Remission in Early-Life SIV Infection.Research square · 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
- Mechanistic insights into lenacapavir-induced off-pathway HIV-1 capsid assembly.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Lenacapavir prevents production of infectious HIV-1 by abrogating immature virus assembly.bioRxiv : the preprint server for biology · 2026Article
- Stoichiometric binding of Cyclophilin-A to the HIV-1 capsid modulates its mechanoelastic properties.bioRxiv : the preprint server for biology · 2026Article
- Structural, biophysical, and virological mechanistic characterization of HIV-1 capsid-targeting antivirals.bioRxiv : the preprint server for biology · 2025Article
- Distinct Target Site of Lenacapavir in Immature HIV-1 and Concurrent Binding with the Maturation Inhibitor Bevirimat.Journal of the American Chemical Society · 2025Article
- Article
- Translocation of HIV capsid core through the Nuclear Pore Complex by affinity gradient.bioRxiv : the preprint server for biology · 2025Article
- Structural Basis for HIV-1 Maturation Inhibition by PF-46396 Determined by MAS NMR.Journal of the American Chemical Society · 2025Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 2 institutions in 3 countries.
Funding
Abstract
The HIV-1 capsid houses the viral genome and interacts extensively with host cell proteins throughout the viral life cycle. It is composed of capsid protein (CA), which assembles into a conical fullerene lattice composed of roughly 200 CA hexamers and 12 CA pentamers. Previous structural analyses of individual CA hexamers and pentamers have provided valuable insight into capsid structure and function, but detailed structural information about these assemblies in the broader context of the capsid lattice is lacking. In this study, we combined cryoelectron tomography and single particle analysis (SPA) cryoelectron microscopy to determine structures of continuous regions of the capsid lattice containing both hexamers and pentamers. We also developed a method of liposome scaffold-based in vitro lattice assembly ("lattice templating") that enabled us to directly study the lattice under a wider range of conditions than has previously been possible. Using this approach, we identified a critical role for inositol hexakisphosphate in pentamer formation and determined the structure of the CA lattice bound to the capsid-targeting antiretroviral drug GS-6207 (lenacapavir). Our work reveals key structural details of the mature HIV-1 CA lattice and establishes the combination of lattice templating and SPA as a robust strategy for studying retroviral capsid structure and capsid interactions with host proteins and antiviral compounds.
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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.