ArticleNature communications2021
Structure of the mature Rous sarcoma virus lattice reveals a role for IP6 in the formation of the capsid hexamer.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 26 citations in OpenAlex.
- The Central Pore of HIV-1 Capsomers Promotes Sustained Stability of the Viral Capsid.Journal of molecular biology · 2026Article
- Retroviruses use different IPNature communications · 2026Article
- Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication.FEMS microbiology reviews · 2026Review
- High-resolution analysis of the human T-cell leukemia virus capsid protein reveals insights into immature particle morphology.Nature communications · 2025Article
- The Human T-cell Leukemia Virus capsid protein is a potential drug target.Nature communications · 2025Article
- Design, Synthesis, and Cellular Characterization of a New Class of IPMK Kinase Inhibitors.Journal of medicinal chemistry · 2025Article
- Review
- Distinct stabilization of the human T cell leukemia virus type 1 immature Gag lattice.Nature structural & molecular biology · 2025Article
- The Assembly of HTLV-1-How Does It Differ from HIV-1?Viruses · 2024Review
- Essential functions of inositol hexakisphosphate (IP6) in murine leukemia virus replication.mBio · 2024Article
- Molecular architecture and conservation of an immature human endogenous retrovirus.bioRxiv : the preprint server for biology · 2023Article
- Structural insights into HIV-1 polyanion-dependent capsid lattice formation revealed by single particle cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- HIV-1 is dependent on its immature lattice to recruit IP6 for mature capsid assembly.Nature structural & molecular biology · 2023Article
- Inositol Hexakisphosphate (IP6) Accelerates Immature HIV-1 Gag Protein Assembly toward Kinetically Trapped Morphologies.Journal of the American Chemical Society · 2022Article
- Exploring high-resolution cryo-ET and subtomogram averaging capabilities of contemporary DEDs.Journal of structural biology · 2022Article
- Review
- High-affinity anti-Arc nanobodies provide tools for structural and functional studies.PloS one · 2022Article
- Review
- Review
- Structure of a Ty1 restriction factor reveals the molecular basis of transposition copy number control.Nature communications · 2021Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
Inositol hexakisphosphate (IP6) is an assembly cofactor for HIV-1. We report here that IP6 is also used for assembly of Rous sarcoma virus (RSV), a retrovirus from a different genus. IP6 is ~100-fold more potent at promoting RSV mature capsid protein (CA) assembly than observed for HIV-1 and removal of IP6 in cells reduces infectivity by 100-fold. Here, visualized by cryo-electron tomography and subtomogram averaging, mature capsid-like particles show an IP6-like density in the CA hexamer, coordinated by rings of six lysines and six arginines. Phosphate and IP6 have opposing effects on CA in vitro assembly, inducing formation of T = 1 icosahedrons and tubes, respectively, implying that phosphate promotes pentamer and IP6 hexamer formation. Subtomogram averaging and classification optimized for analysis of pleomorphic retrovirus particles reveal that the heterogeneity of mature RSV CA polyhedrons results from an unexpected, intrinsic CA hexamer flexibility. In contrast, the CA pentamer forms rigid units organizing the local architecture. These different features of hexamers and pentamers determine the structural mechanism to form CA polyhedrons of variable shape in mature RSV particles.
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Registered trials
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