Evidence map›Paper›PMID 16873257›Full record

ArticleJournal of virology2006

Evidence for a role of the cellular ND10 protein PML in mediating intrinsic immunity against human cytomegalovirus infections.

Nina Tavalai, Peer Papior, Sabine Rechter, Martina Leis, Thomas Stamminger

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 150 papers.

0numbers the graph read from it
0cells of the map it votes in
150citing papers in PubMed
10.9field-weighted citation impact, top 1% 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

150 citing papers in PubMed, 209 citations in OpenAlex.

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  19. Expanding the Known Functional Repertoire of the Human Cytomegalovirus pp71 Protein.Frontiers in cellular and infection microbiology · 2020
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90 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

Nina TavalaiInstitut für Klinische und Molekulare Virologie der Universität Erlangen-Nürnberg, Schlossgarten 4, 91054 Erlangen, Germany.
Peer Papior
Sabine Rechter
Martina Leis
Thomas Stamminger
Friedrich-Alexander-Universität Erlangen-Nürnberg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Several viruses, including human cytomegalovirus (HCMV), encode proteins that colocalize with a cellular subnuclear structure known as ND10. Since only viral DNA deposited at ND10 initiates transcription, ND10 structures were hypothesized to be essential for viral replication. On the other hand, interferon treatment induces an up-regulation of ND10 structures and viruses have evolved polypeptides that disperse the dot-like accumulation of ND10 proteins, suggesting that ND10 could also be part of an intrinsic defense mechanism. In order to obtain evidence for either a proviral or an antiviral function of ND10, we generated primary human fibroblasts with a stable, short interfering RNA-mediated knockdown (kd) of PML. In these cells, other ND10-associated proteins like hDaxx showed a diffuse nuclear distribution. Interestingly, we observed that HCMV infection induced the de novo formation of ND10-like hDaxx and Sp100 accumulations that colocalized with IE2 and were disrupted, in the apparent absence of PML, in an IE1-dependent manner during the first hours after infection. Furthermore, infection of PML-kd cells with wild-type HCMV at a low multiplicity of infection resulted in enhanced replication. In particular, a significantly increased plaque formation was detected, suggesting that more cells are able to support initiation of replication in the absence of PML. While there was no difference in viral DNA uptake between PML-kd and control cells, we observed a considerable increase in the number of immediate-early (IE) protein-positive cells, indicating that the depletion of PML augments the initiation of viral IE gene expression. These results strongly suggest that PML functions as part of an intrinsic immune mechanism against cytomegalovirus infections.

Indexed as

Gene Expression Regulation, ViralAdaptor Proteins, Signal TransducingAntigens, NuclearAutoantigensCell NucleusCo-Repressor ProteinsCytomegalovirusCytomegalovirus InfectionsFibroblastsHumansImmediate-Early ProteinsMolecular ChaperonesNeoplasm ProteinsNuclear ProteinsPromyelocytic Leukemia ProteinTrans-ActivatorsAdaptor Proteins, Signal TransducingAntigens, NuclearAutoantigensCo-Repressor ProteinsDAXX protein, humanIE1 protein, cytomegalovirusIE2 protein, CytomegalovirusImmediate-Early ProteinsMolecular ChaperonesNeoplasm ProteinsNuclear ProteinsPML protein, humanPromyelocytic Leukemia ProteinSP100 protein, humanTrans-ActivatorsTranscription FactorsTumor Suppressor ProteinsViral Proteins

Identifiers

PMID16873257
PMCPMC1563799
OpenAlexW2160623917

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.