Evidence map›Paper›PMID 18579586›Full record

ArticleJournal of virology2008

Epstein-Barr virus latent membrane protein 2A preferentially signals through the Src family kinase Lyn.

Mark Rovedo, Richard Longnecker

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.6field-weighted citation impact, top 29% 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

16 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Rewiring of B cell receptor signaling by Epstein-Barr virus LMP2A.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Epstein-Barr virus latent genes.Experimental & molecular medicine · 2015
    Review
  8. Review
  9. EBV-related lymphomas: new approaches to treatment.Current treatment options in oncology · 2013
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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

2 authors at 1 institution in 1 country.

Mark RovedoDepartment of Microbiology and Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611, USA.
Richard Longnecker
Northwestern University · US

Funding

In Vivo Model of Epstein-Barr Virus LatencyR01CA073507 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI LONGNECKER, RICHARD M · 1997 to 2018
$6.1M
EBV LATENT MEMBRANE PROTEIN 2R01CA062234 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI LONGNECKER, RICHARD M · 1994 to 2007
$2.2M
POST GRADUATE PROGRAM IN CUTANEOUS BIOLOGYT32AR007593 · NIAMS · NORTHWESTERN UNIVERSITY · PI GREEN, KATHLEEN JANEE · 1995 to 2004
$694k
NCI NIH HHS CA62234NCI NIH HHS CA73507NCI NIH HHS R01 CA062234NCI NIH HHS R01 CA073507NIAMS NIH HHS T32 AR007593NIAMS NIH HHS T32 AR07593
6 · The paper itself

Abstract

Latent membrane protein 2A (LMP2A) is a viral protein expressed during Epstein-Barr virus (EBV) latency in EBV-infected B cells both in cell culture and in vivo. LMP2A has important roles in modulating B-cell receptor signal transduction and provides survival and developmental signals to B cells in vivo. Although Lyn has been shown to be important in mediating LMP2A signaling, it is still unclear if Lyn is used preferentially or if LMP2A associates promiscuously with other Src family kinase (SFK) members. To investigate the role of various SFKs in LMP2A signaling, we crossed LMP2A transgenic mice (TgE) with Lyn(-/-), Fyn(-/-), or Blk(-/-) mice. TgE Lyn(-/-) mice had a larger immunoglobulin M (IgM)-positive B-cell population than TgE mice, suggesting that the absence of Lyn prevents LMP2A from delivering survival and developmental signals to the B cells. Both TgE Fyn(-/-) and TgE Blk(-/-) mice have an IgM-negative population of splenic B cells, similar to the TgE mice. LMP2A was also transiently transfected into the human EBV-negative B-cell line BJAB to determine which SFK members associate with LMP2A. Lyn was detected in LMP2A immunoprecipitates, whereas Fyn was not. Both Lyn and Fyn were able to bind to an LMP2A mutant which contained a sequence shown previously to bind tightly to the SH2 domain of multiple SFK members. From these results, we conclude that LMP2A preferentially associates with and signals through Lyn compared to its association with other SFKs. This preferential association is due in part to the SH2 domain of Lyn associating with LMP2A.

Indexed as

Signal TransductionAnimalsB-LymphocytesCell Line, TumorCrosses, GeneticHomozygoteLymphomaMiceMice, TransgenicMutationProtein BindingProtein Structure, Tertiarysrc-Family KinasesTransfectionViral Matrix ProteinsVirus LatencyEBV-associated membrane antigen, Epstein-Barr viruslyn protein-tyrosine kinasesrc-Family KinasesViral Matrix Proteins

Identifiers

PMID18579586
PMCPMC2519656
OpenAlexW2144042793

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.