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Structural basis underlying viral hijacking of a histone chaperone complex

Author

Listed:
  • Hongda Huang

    (Structural Biology Program, Memorial Sloan-Kettering Cancer Center)

  • Zhong Deng

    (Gene Expression and Regulation Program, The Wistar Institute)

  • Olga Vladimirova

    (Gene Expression and Regulation Program, The Wistar Institute)

  • Andreas Wiedmer

    (Gene Expression and Regulation Program, The Wistar Institute)

  • Fang Lu

    (Gene Expression and Regulation Program, The Wistar Institute)

  • Paul M. Lieberman

    (Gene Expression and Regulation Program, The Wistar Institute)

  • Dinshaw J. Patel

    (Structural Biology Program, Memorial Sloan-Kettering Cancer Center)

Abstract

The histone H3.3 chaperone DAXX is implicated in formation of heterochromatin and transcription silencing, especially for newly infecting DNA virus genomes entering the nucleus. Epstein-Barr virus (EBV) can efficiently establish stable latent infection as a chromatinized episome in the nucleus of infected cells. The EBV tegument BNRF1 is a DAXX-interacting protein required for the establishment of selective viral gene expression during latency. Here we report the structure of BNRF1 DAXX-interaction domain (DID) in complex with DAXX histone-binding domain (HBD) and histones H3.3-H4. BNRF1 DID contacts DAXX HBD and histones through non-conserved loops. The BNRF1-DAXX interface is responsible for BNRF1 localization to PML-nuclear bodies typically associated with host-antiviral resistance and transcriptional repression. Paradoxically, the interface is also required for selective transcription activation of viral latent cycle genes required for driving B-cell proliferation. These findings reveal molecular details of virus reprogramming of an antiviral histone chaperone to promote viral latency and cellular immortalization.

Suggested Citation

  • Hongda Huang & Zhong Deng & Olga Vladimirova & Andreas Wiedmer & Fang Lu & Paul M. Lieberman & Dinshaw J. Patel, 2016. "Structural basis underlying viral hijacking of a histone chaperone complex," Nature Communications, Nature, vol. 7(1), pages 1-10, November.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12707
    DOI: 10.1038/ncomms12707
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