EMD-17936
Structure of immature HTLV-1 CA-NTD from in vitro assembled MA126-CANC tubes: axis angle 10 degrees
EMD-17936
Subtomogram averaging4.5 Å
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Map released: 23/08/2023
Last modified: 26/02/2025
Sample Organism:
Human T-cell leukemia virus type I
Sample: Human T-cell leukemia virus type I
Fitted models: 8pud (Avg. Q-score: 0.355)
Deposition Authors: Obr M
,
Percipalle M
,
Chernikova D
,
Yang H
,
Thader A
,
Pinke G
,
Porley D
,
Mansky LM
,
Dick RA
,
Schur FKM
Sample: Human T-cell leukemia virus type I
Fitted models: 8pud (Avg. Q-score: 0.355)
Deposition Authors: Obr M
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Distinct stabilization of the human T cell leukemia virus type 1 immature Gag lattice.
Obr M
,
Percipalle M
,
Chernikova D
,
Yang H
,
Thader A
,
Pinke G
,
Porley D
,
Mansky LM
,
Dick RA
,
Schur FKM
(2025) Nat Struct Mol Biol , 32 , 268 - 276
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(2025) Nat Struct Mol Biol , 32 , 268 - 276
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.
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.