Evidence map›Paper›PMID 16227252›Full record

ArticleJournal of virology2005

A redox-sensitive cysteine in Zta is required for Epstein-Barr virus lytic cycle DNA replication.

Pu Wang, Latasha Day, Jayaraju Dheekollu, Paul M Lieberman

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.2field-weighted citation impact, top 22% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 29 citations in OpenAlex.

  1. Reconstructing EBV reactivation and DNA damage response kinetics in morphologic pseudotime.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  5. Stimulus-responsive viral vectors for controlled delivery of therapeutics.Journal of controlled release : official journal of the Controlled Release Society · 2017
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Pu WangThe Wistar Institute, Philadelphia, PA 19104, USA.
Latasha Day
Jayaraju Dheekollu
Paul M Lieberman
The Wistar Institute · US

Funding

Functions of the General Coactivator TFIIAR01GM054687 · NIGMS · WISTAR INSTITUTE · PI LIEBERMAN, PAUL M. · 1996 to 2005
$1.5M
NCI NIH HHS CA 86678NIGMS NIH HHS GM 54687NIGMS NIH HHS R01 GM054687
6 · The paper itself

Abstract

Epstein-Barr virus (EBV) reactivation from latency is known to be sensitive to redox regulation. The immediate-early protein Zta is a member of the basic-leucine zipper (bZIP) family of DNA binding proteins that stimulates viral and cellular transcription and nucleates a replication complex at the viral lytic origin. Zta shares with several members of the bZIP family a conserved cysteine residue (C189) that confers redox regulation of DNA binding. In this work, we show that replacement of C189 with serine (C189S) eliminated lytic cycle DNA replication function of Zta. The mechanistic basis for this replication defect was investigated. We show that C189S was not significantly altered for DNA binding activity in vitro or in vivo. We also show that C189S was not defective for transcription activation of EBV early gene promoters. C189S was deficient for transcription activation of several viral late genes that depend on lytic replication and therefore was consistent with a primary defect of C189S in activating lytic replication. C189S was not defective in binding methylated DNA binding sites and was capable of activating Rta from endogenous latent viral genomes, in contrast to the previously characterized S186A mutation. C189S was slightly impaired for its ability to form a stable complex with Rta, although this did not prevent Rta recruitment to OriLyt. C189S did provide some resistance to oxidation and nitrosylation, which potently inhibit Zta DNA binding activity in vitro. Interestingly, this redox sensitivity was not strictly dependent on C189S but involved additional cysteine residues in Zta. These results provide evidence that the conserved cysteine in the bZIP domain of Zta plays a primary role in EBV lytic cycle DNA replication.

Indexed as

DNA ReplicationAmino Acid SequenceAmino Acid SubstitutionCell LineCysteineDNA-Binding ProteinsDNA, ViralHerpesvirus 4, HumanHumansMolecular Sequence DataOxidation-ReductionSequence AlignmentSerineTrans-ActivatorsUp-RegulationViral ProteinsBZLF1 protein, Herpesvirus 4, HumanCysteineDNA-Binding ProteinsDNA, ViralSerineTrans-ActivatorsViral Proteins

Identifiers

PMID16227252
PMCPMC1262569
OpenAlexW2114349065

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.