8PU7

Structure of immature HTLV-1 CA-NTD from in vitro assembled MA126-CANC tubes: axis angle -20 degrees

8PU7 の概要

• エントリーDOI: 10.2210/pdb8pu7/pdb
• EMDBエントリー: 17929 17930 17931 17932 17933 17934 17935 17936 17937 17938 17939 17940 17941 17942 17943
• 分子名称: Gag protein (Fragment) (1 entity in total)
• 機能のキーワード: retrovirus, htlv, immature capsid, ca, ca-ntd, viral protein
• 由来する生物種: Human T-cell leukemia virus type I
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 41909.43

構造登録者

Obr, M.,Percipalle, M.,Chernikova, D.,Yang, H.,Thader, A.,Pinke, G.,Porley, D.,Mansky, L.M.,Dick, R.A.,Schur, F.K.M. (登録日: 2023-07-17, 公開日: 2023-08-23, 最終更新日: 2025-02-26)

主引用文献

Obr, M.,Percipalle, M.,Chernikova, D.,Yang, H.,Thader, A.,Pinke, G.,Porley, D.,Mansky, L.M.,Dick, R.A.,Schur, F.K.M.
Distinct stabilization of the human T cell leukemia virus type 1 immature Gag lattice.
Nat.Struct.Mol.Biol., 32:268-276, 2025

PubMed 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.

PubMed: 39242978
DOI: 10.1038/s41594-024-01390-8

実験手法

ELECTRON MICROSCOPY (4.8 Å)