ArticleNature communications2016
Structural basis underlying viral hijacking of a histone chaperone complex.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 36 citations in OpenAlex.
- A System-Level Perspective on Epstein-Barr Virus Persistence: The Partial Lytic Reactivation.International journal of molecular sciences · 2026Review
- Histone variant H2A.Z cooperates with EBNA1 to maintain Epstein-Barr virus latent epigenome.mBio · 2025Article
- Physiology and molecular biology of plants : an international journal of functional plant biology · 2025Article
- Chromatin Control of EBV Infection and Latency.Current topics in microbiology and immunology · 2025Article
- Daxx and HIRA go viral - How chromatin remodeling complexes affect DNA virus infection.Tumour virus research · 2025Review
- Review
- Epstein-Barr virus protein BKRF4 restricts nucleosome assembly to suppress host antiviral responses.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Epstein-Barr Virus (EBV) Is Mostly Latent and Clonal in Angioimmunoblastic T Cell Lymphoma (AITL).Cancers · 2022Article
- Epstein-Barr virus BNRF1 destabilizes SMC5/6 cohesin complexes to evade its restriction of replication compartments.Cell reports · 2022Article
- Epigenetic control of the Epstein-Barr lifecycle.Current opinion in virology · 2022Review
- Defective Epstein-Barr Virus Genomes and Atypical Viral Gene Expression in B-Cell Lines Derived from Multiple Myeloma Patients.Journal of virology · 2021Article
- RUNX1-mediated alphaherpesvirus-host trans-species chromatin interaction promotes viral transcription.Science advances · 2021Article
- Phase separation and DAXX redistribution contribute to LANA nuclear body and KSHV genome dynamics during latency and reactivation.PLoS pathogens · 2021Article
- Article
- Structures of capsid and capsid-associated tegument complex inside the Epstein-Barr virus.Nature microbiology · 2020Article
- Epigenetic lifestyle of Epstein-Barr virus.Seminars in immunopathology · 2020Review
- Control of Viral Latency by Episome Maintenance Proteins.Trends in microbiology · 2020Review
- DAXX in cancer: phenomena, processes, mechanisms and regulation.Nucleic acids research · 2019Review
- Dynamics and Mechanisms in the Recruitment and Transference of Histone Chaperone CIA/ASF1.International journal of molecular sciences · 2019Article
- Viral FGARAT ORF75A promotes early events in lytic infection and gammaherpesvirus pathogenesis in mice.PLoS pathogens · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.