Evidence map›Paper›PMID 17344282›Full record

ArticleJournal of virology2007

The human cytomegalovirus virion possesses an activated casein kinase II that allows for the rapid phosphorylation of the inhibitor of NF-kappaB, IkappaBalpha.

Maciej T Nogalski, Jagat P Podduturi, Ian B DeMeritt, Liesl E Milford, Andrew D Yurochko

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Deletion of the non-adjacent genesFrontiers in immunology · 2023
    Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
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  14. Article
  15. Protein kinase CK2, an important regulator of the inflammatory response?Journal of molecular medicine (Berlin, Germany) · 2008
    Review
  16. Review
  17. Tegument proteins of human cytomegalovirus.Microbiology and molecular biology reviews : MMBR · 2008
    Review
  18. Article
  19. Article
  20. Article
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.

Maciej T NogalskiDepartment of Microbiology and Immunology, Center for Molecular and Tumor Virology, Louisiana State University Health Sciences Center, 1501 Kings Highway, Shreveport, LA 71130-3932, USA.
Jagat P Podduturi
Ian B DeMeritt
Liesl E Milford
Andrew D Yurochko
Louisiana State University Health Sciences Center Shreveport · US

Funding

RECRUITMENT YEAR FOR PI#5P20RR018724 · NCRR · LOUISIANA STATE UNIV HSC SHREVEPORT · PI TSUNODA, IKUO · 2003 to 2011
$16.1M
Analysis of HCMV Infection of Monocytes and MacrophagesR01AI056077 · NIAID · LOUISIANA STATE UNIV HSC SHREVEPORT · PI YUROCHKO, ANDREW D · 2004 to 2020
$4.7M
COBRE Center for Molecular and Tumor VirologyP20GM103433 · NIGMS · LOUISIANA STATE UNIV HSC SHREVEPORT · PI O'CALLAGHAN, DENNIS JOHN · 2012 to 2012
$1.9M
NCRR NIH HHS P20 RR018724NCRR NIH HHS P20-RR018724NIAID NIH HHS R01 AI056077NIAID NIH HHS R01-AI56077NIGMS NIH HHS P20 GM103433
6 · The paper itself

Abstract

We documented that the NF-kappaB signaling pathway was rapidly induced following human cytomegalovirus (HCMV) infection of human fibroblasts and that this induced NF-kappaB activity promoted efficient transactivation of the major immediate-early promoter (MIEP). Previously, we showed that the major HCMV envelope glycoproteins, gB and gH, initiated this NF-kappaB signaling event. However, we also hypothesized that there were additional mechanisms utilized by the virus to rapidly upregulate NF-kappaB. In this light, we specifically hypothesized that the HCMV virion contained IkappaBalpha kinase activity, allowing for direct phosphorylation of IkappaBalpha following virion entry into infected cells. In vitro kinase assays performed on purified HCMV virion extract identified bona fide IkappaBalpha kinase activity in the virion. The enzyme responsible for this kinase activity was identified as casein kinase II (CKII), a cellular serine-threonine protein kinase. CKII activity was necessary for efficient transactivation of the MIEP and IE gene expression. CKII is generally considered to be a constitutively active kinase. We suggest that this molecular characteristic of CKII represents the biologic rationale for the viral capture and utilization of this kinase early after infection. The packaging of CKII into the HCMV virion identifies that diverse molecular mechanisms are utilized by HCMV for rapid NF-kappaB activation. We propose that HCMV possesses multiple pathways to increase NF-kappaB activity to ensure that the correct temporal regulation of NF-kappaB occurs following infection and that sufficient threshold levels of NF-kappaB are reached in the diverse array of cells, including monocytes and endothelial cells, infected in vivo.

Indexed as

Blotting, WesternCasein Kinase IICells, CulturedCytomegalovirusGenes, Immediate-EarlyHumansI-kappa B KinaseI-kappa B ProteinsImmunoprecipitationNF-kappa BNF-KappaB Inhibitor alphaPhosphorylationPromoter Regions, GeneticTranscriptional ActivationViral ProteinsVirionCasein Kinase III-kappa B KinaseI-kappa B ProteinsNF-kappa BNF-KappaB Inhibitor alphaNFKBIA protein, humanViral Proteins

Identifiers

PMID17344282
PMCPMC1900216
OpenAlexW2142374314

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.