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Structural basis of host protein hijacking in human T-cell leukemia virus integration

Author

Listed:
  • Veer Bhatt

    (University of Minnesota
    University of Minnesota)

  • Ke Shi

    (University of Minnesota
    University of Minnesota
    University of Minnesota)

  • Daniel J. Salamango

    (University of Minnesota
    University of Minnesota
    University of Minnesota)

  • Nicholas H. Moeller

    (University of Minnesota
    University of Minnesota
    University of Minnesota)

  • Krishan K. Pandey

    (Saint Louis University)

  • Sibes Bera

    (Saint Louis University)

  • Heather O. Bohl

    (University of Minnesota
    University of Minnesota
    University of Minnesota)

  • Fredy Kurniawan

    (University of Minnesota
    University of Minnesota
    University of Minnesota)

  • Kayo Orellana

    (University of Minnesota
    University of Minnesota
    University of Minnesota)

  • Wei Zhang

    (University of Minnesota
    University of Minnesota
    University of Minnesota
    University of Minnesota)

  • Duane P. Grandgenett

    (Saint Louis University)

  • Reuben S. Harris

    (University of Minnesota
    University of Minnesota
    University of Minnesota
    University of Minnesota)

  • Anna C. Sundborger-Lunna

    (University of Minnesota
    University of Minnesota)

  • Hideki Aihara

    (University of Minnesota
    University of Minnesota
    University of Minnesota)

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 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.

Suggested Citation

  • 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. Harr, 2020. "Structural basis of host protein hijacking in human T-cell leukemia virus integration," Nature Communications, Nature, vol. 11(1), pages 1-9, December.
  • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-16963-6
    DOI: 10.1038/s41467-020-16963-6
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    Cited by:

    1. Allison Ballandras-Colas & Vidya Chivukula & Dominika T. Gruszka & Zelin Shan & Parmit K. Singh & Valerie E. Pye & Rebecca K. McLean & Gregory J. Bedwell & Wen Li & Andrea Nans & Nicola J. Cook & Hind, 2022. "Multivalent interactions essential for lentiviral integrase function," Nature Communications, Nature, vol. 13(1), pages 1-16, December.

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