Evidence map›Paper›PMID 27792904›Full record

ArticleVirology2017

Epstein-Barr Virus Latent Membrane Protein 2A (LMP2A) enhances IL-10 production through the activation of Bruton's tyrosine kinase and STAT3.

Ryan Incrocci, Levi Barse, Amanda Stone, Sai Vagvala, Michael Montesano, Vijay Subramaniam, Michelle Swanson-Mungerson

Open access · greenAbstract read
In one paragraph

Article in Virology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.2field-weighted citation impact, top 10% 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

33 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
  2. Epstein-Barr Virus in Multiple Sclerosis: Past, Present, and Future.Neurology(R) neuroimmunology & neuroinflammation · 2025
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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

7 authors at 1 institution in 1 country.

Ryan IncrocciDepartment of Microbiology and Immunology, Chicago College of Osteopathic Medicine, Midwestern University, 555 31st Street, Downers Grove, IL 60515, United States.
Levi BarseDepartment of Biomedical Sciences, College of Health Sciences, Midwestern University, 555 31st Street, Downers Grove, IL 60515, United States.
Amanda StoneDepartment of Microbiology and Immunology, Chicago College of Osteopathic Medicine, Midwestern University, 555 31st Street, Downers Grove, IL 60515, United States.
Sai VagvalaDepartment of Microbiology and Immunology, Chicago College of Osteopathic Medicine, Midwestern University, 555 31st Street, Downers Grove, IL 60515, United States.
Michael MontesanoDepartment of Microbiology and Immunology, Chicago College of Osteopathic Medicine, Midwestern University, 555 31st Street, Downers Grove, IL 60515, United States.
Vijay SubramaniamDepartment of Biomedical Sciences, College of Health Sciences, Midwestern University, 555 31st Street, Downers Grove, IL 60515, United States.
Michelle Swanson-MungersonDepartment of Microbiology and Immunology, Chicago College of Osteopathic Medicine, Midwestern University, 555 31st Street, Downers Grove, IL 60515, United States. Electronic address: mswans@midwestern.edu.
Midwestern University · US

Funding

Functions of Epstein-Barr Virus LMP2A in LatencyR15CA149690 · NCI · MIDWESTERN UNIVERSITY · PI SWANSON-MUNGERSON, MICHELLE · 2010 to 2010
$219k
NCI NIH HHS R15 CA149690
6 · The paper itself

Abstract

Previous data demonstrate that Epstein-Barr Virus Latent Membrane Protein 2A (LMP2A) enhances IL-10 to promote the survival of LMP2A-expressing B cell lymphomas. Since STAT3 is an important regulator of IL-10 production, we hypothesized that LMP2A activates a signal transduction cascade that increases STAT3 phosphorylation to enhance IL-10. Using LMP2A-negative and -positive B cell lines, the data indicate that LMP2A requires the early signaling molecules of the Syk/RAS/PI3K pathway to increase IL-10. Additional studies indicate that the PI3K-regulated kinase, BTK, is responsible for phosphorylating STAT3, which ultimately mediates the LMP2A-dependent increase in IL-10. These data are the first to show that LMP2A signaling results in STAT3 phosphorylation in B cells through a PI3K/BTK-dependent pathway. With the use of BTK and STAT3 inhibitors to treat B cell lymphomas in clinical trials, these findings highlight the possibility of using new pharmaceutical approaches to treat EBV-associated lymphomas that express LMP2A.

Indexed as

Agammaglobulinaemia Tyrosine KinaseB-LymphocytesCell LineEnzyme ActivationEpstein-Barr Virus InfectionsHerpesvirus 4, HumanHost-Pathogen InteractionsHumansInterleukin-10Phosphatidylinositol 3-KinasesPhosphorylationProtein-Tyrosine KinasesSignal TransductionSTAT3 Transcription FactorViral Matrix ProteinsAgammaglobulinaemia Tyrosine KinaseBTK protein, humanEBV-associated membrane antigen, Epstein-Barr virusInterleukin-10Phosphatidylinositol 3-KinasesProtein-Tyrosine KinasesSTAT3 Transcription FactorViral Matrix ProteinsB cellBruton's tyrosine kinase (BTK)Epstein-Barr virusInterleukin-10Latent Membrane Protein 2ASignal Transducer and Activator of Transcription 3 (STAT3)

Identifiers

PMID27792904
PMCPMC5127766
OpenAlexW2540742595

What OpenQuestion holds

Textmetadata
LicenceTDM
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.