ArticleNature structural & molecular biology2025
Distinct stabilization of the human T cell leukemia virus type 1 immature Gag lattice.
Article in Nature structural & molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Retroviruses use different IPNature communications · 2026Article
- Confidence-guided cryo-EM map optimisation with LocScale-2.0.Nature communications · 2026Article
- 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
- Review
- Pathogen-induced hijacking of host SUMOylation: from molecular mechanisms and prospects for therapeutic modulation.Frontiers in immunology · 2025Review
- 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
- Stimuli-responsive materials in oral diseases: a review.Clinical oral investigations · 2024Review
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Abstract
Human T cell leukemia virus type 1 (HTLV-1) immature particles differ in morphology from other retroviruses, suggesting a distinct way of assembly. Here we report the results of cryo-electron tomography studies of HTLV-1 virus-like particles assembled in vitro, as well as derived from cells. This work shows that HTLV-1 uses a distinct mechanism of Gag-Gag interactions to form the immature viral lattice. Analysis of high-resolution structural information from immature capsid (CA) tubular arrays reveals that the primary stabilizing component in HTLV-1 is the N-terminal domain of CA. Mutagenesis analysis supports this observation. This distinguishes HTLV-1 from other retroviruses, in which the stabilization is provided primarily by the C-terminal domain of CA. These results provide structural details of the quaternary arrangement of Gag for an immature deltaretrovirus and this helps explain why HTLV-1 particles are morphologically distinct.
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