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Purification of Viral DNA for the Identification of Associated Viral and Cellular Proteins
Published on: August 31, 2017
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Structural basis underlying viral hijacking of a histone chaperone complex.
Hongda Huang1, Zhong Deng2, Olga Vladimirova2
1Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10065, USA.
Nature Communications
|September 2, 2016
Summary
Epstein-Barr virus (EBV) protein BNRF1 reprograms the antiviral histone chaperone DAXX. This interaction promotes viral latency and cellular immortalization by altering gene expression.
Area of Science:
- Molecular Biology
- Virology
- Epigenetics
Background:
- Histone chaperone DAXX is involved in heterochromatin formation and transcription silencing.
- Epstein-Barr virus (EBV) establishes latent infection via a chromatinized episome.
- EBV tegument protein BNRF1 interacts with DAXX and is crucial for viral gene expression during latency.
Purpose of the Study:
- To elucidate the molecular mechanism of BNRF1-DAXX interaction and its role in EBV latency.
Main Methods:
- Reported the crystal structure of the BNRF1 DAXX-interaction domain (DID) in complex with DAXX histone-binding domain (HBD) and histones H3.3-H4.
Main Results:
- BNRF1 DID binds DAXX HBD and histones via non-conserved loops.
- The BNRF1-DAXX interface mediates BNRF1 localization to PML-nuclear bodies.
- This interface is essential for both host antiviral response modulation and viral gene activation during latency.
Conclusions:
- The BNRF1-DAXX interaction is a key viral strategy to reprogram host antiviral machinery.
- This reprogramming facilitates EBV latency, B-cell proliferation, and cellular immortalization.
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