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-Structure paper
Title | Structural basis of host protein hijacking in human T-cell leukemia virus integration. |
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Journal, issue, pages | Nat Commun, Vol. 11, Issue 1, Page 3121, Year 2020 |
Publish date | Jun 19, 2020 |
Authors | Veer Bhatt / Ke Shi / Daniel J Salamango / Nicholas H Moeller / Krishan K Pandey / Sibes Bera / Heather O Bohl / Fredy Kurniawan / Kayo Orellana / Wei Zhang / Duane P Grandgenett / Reuben S Harris / Anna C Sundborger-Lunna / Hideki Aihara / |
PubMed Abstract | Integration of the reverse-transcribed viral DNA into host chromosomes is a critical step in the life-cycle of retroviruses, including an oncogenic delta(δ)-retrovirus human T-cell leukemia virus ...Integration of the reverse-transcribed viral DNA into host chromosomes is a critical step in the life-cycle of retroviruses, including an oncogenic delta(δ)-retrovirus human T-cell leukemia virus type-1 (HTLV-1). Retroviral integrase forms a higher order nucleoprotein assembly (intasome) to catalyze the integration reaction, in which the roles of host factors remain poorly understood. Here, we use cryo-electron microscopy to visualize the HTLV-1 intasome at 3.7-Å resolution. The structure together with functional analyses reveal that the B56γ (B'γ) subunit of an essential host enzyme, protein phosphatase 2 A (PP2A), is repurposed as an integral component of the intasome to mediate HTLV-1 integration. Our studies reveal a key host-virus interaction underlying the replication of an important human pathogen and highlight divergent integration strategies of retroviruses. |
External links | Nat Commun / PubMed:32561747 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.7 Å |
Structure data | EMDB-21301, PDB-6voy: |
Chemicals | ChemComp-ZN: ChemComp-MG: |
Source |
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Keywords | DNA BINDING PROTEIN/DNA / Integrase / Intasome / DNA BINDING PROTEIN-DNA complex |