Distinct stabilization of the human T cell leukemia virus type 1 immature Gag lattice.
Martin ObrMathias PercipalleDarya ChernikovaHuixin YangAndreas ThaderGergely PinkeDario PorleyLouis M ManskyRobert A DickFlorian K M SchurPublished in: Nature structural & molecular biology (2024)
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.
Keyphrases
- high resolution
- endothelial cells
- acute myeloid leukemia
- bone marrow
- induced pluripotent stem cells
- induced apoptosis
- sars cov
- crispr cas
- mass spectrometry
- electron microscopy
- pluripotent stem cells
- cell proliferation
- high glucose
- cell cycle arrest
- signaling pathway
- endoplasmic reticulum stress
- oxidative stress
- high density
- disease virus