Cyclosporine Directly Causes Oxidative Stress and Promotes Epstein–Barr Virus Transformation of Human B Cells

2001 ◽  
Vol 100 (2) ◽  
pp. 166-170 ◽  
Author(s):  
Changuo Chen ◽  
Thomas D. Johnston ◽  
K.Sudhakar Reddy ◽  
J.Clint Merrick ◽  
Michael Mastrangelo ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
B Cells ◽  
Epstein Barr Virus ◽  
Barr Virus ◽  
Human B Cells ◽  
Virus Transformation ◽  
Epstein Barr

scholarly journals An ATM/Chk2-Mediated DNA Damage-Responsive Signaling Pathway Suppresses Epstein-Barr Virus Transformation of Primary Human B Cells

2010 ◽  
Vol 8 (6) ◽  
pp. 510-522 ◽  
Author(s):  
Pavel A. Nikitin ◽  
Christopher M. Yan ◽  
Eleonora Forte ◽  
Alessio Bocedi ◽  
Jason P. Tourigny ◽  
...  
Keyword(s):  
Dna Damage ◽  
B Cells ◽  
Signaling Pathway ◽  
Epstein Barr Virus ◽  
Barr Virus ◽  
Human B Cells ◽  
Virus Transformation ◽  
Epstein Barr

scholarly journals An ATM/Chk2-mediated DNA damage responsive signaling pathway suppresses Epstein-Barr virus transformation of primary human B cells

2010 ◽  
Vol 5 (S1) ◽  
Author(s):  
Pavel Nikitin ◽  
Chris Yan ◽  
Eleonora Forte ◽  
Alessio Bocedi ◽  
Jay Tourigny ◽  
...  
Keyword(s):  
Dna Damage ◽  
B Cells ◽  
Signaling Pathway ◽  
Epstein Barr Virus ◽  
Barr Virus ◽  
Human B Cells ◽  
Virus Transformation ◽  
Epstein Barr

scholarly journals Chromosomal rearrangements after ex vivo Epstein–Barr virus (EBV) infection of human B cells

Oncogene ◽  
2009 ◽  
Vol 29 (4) ◽  
pp. 503-515 ◽  
Author(s):  
S Lacoste ◽  
E Wiechec ◽  
A G dos Santos Silva ◽  
A Guffei ◽  
G Williams ◽  
...  
Keyword(s):  
B Cells ◽  
Epstein Barr Virus ◽  
Ex Vivo ◽  
Chromosomal Rearrangements ◽  
Barr Virus ◽  
Ebv Infection ◽  
Human B Cells ◽  
Epstein Barr

scholarly journals Rewiring of B cell receptor signaling by Epstein–Barr virus LMP2A

2020 ◽  
Vol 117 (42) ◽  
pp. 26318-26327
Author(s):  
Kamonwan Fish ◽  
Federico Comoglio ◽  
Arthur L. Shaffer ◽  
Yanlong Ji ◽  
Kuan-Ting Pan ◽  
...  
Keyword(s):  
Cell Cycle ◽  
B Cells ◽  
B Cell ◽  
Epstein Barr Virus ◽  
Cell Receptor ◽  
B Cell Receptor ◽  
Barr Virus ◽  
Human B Cells ◽  
Bcr Signaling ◽  
Epstein Barr

Epstein–Barr virus (EBV) infects human B cells and reprograms them to allow virus replication and persistence. One key viral factor in this process is latent membrane protein 2A (LMP2A), which has been described as a B cell receptor (BCR) mimic promoting malignant transformation. However, how LMP2A signaling contributes to tumorigenesis remains elusive. By comparing LMP2A and BCR signaling in primary human B cells using phosphoproteomics and transcriptome profiling, we identified molecular mechanisms through which LMP2A affects B cell biology. Consistent with the literature, we found that LMP2A mimics a subset of BCR signaling events, including tyrosine phosphorylation of the kinase SYK, the calcium initiation complex consisting of BLNK, BTK, and PLCγ2, and its downstream transcription factor NFAT. However, the majority of LMP2A-induced signaling events markedly differed from those induced by BCR stimulation. These included differential phosphorylation of kinases, phosphatases, adaptor proteins, transcription factors such as nuclear factor κB (NF-κB) and TCF3, as well as widespread changes in the transcriptional output of LMP2A-expressing B cells. LMP2A affected apoptosis and cell-cycle checkpoints by dysregulating the expression of apoptosis regulators such as BCl-xL and the tumor suppressor retinoblastoma-associated protein 1 (RB1). LMP2A cooperated with MYC and mutant cyclin D3, two oncogenic drivers of Burkitt lymphoma, to promote proliferation and survival of primary human B cells by counteracting MYC-induced apoptosis and by inhibiting RB1 function, thereby promoting cell-cycle progression. Our results indicate that LMP2A is not a pure BCR mimic but rather rewires intracellular signaling in EBV-infected B cells that optimizes cell survival and proliferation, setting the stage for oncogenic transformation.

scholarly journals Epstein-Barr virus efficiently immortalizes human B cells without neutralizing the function of p53.

1995 ◽  
Vol 14 (7) ◽  
pp. 1382-1391 ◽  
Author(s):  
M.J. Allday ◽  
A. Sinclair ◽  
G. Parker ◽  
D.H. Crawford ◽  
P.J. Farrell
Keyword(s):  
B Cells ◽  
Epstein Barr Virus ◽  
Barr Virus ◽  
Human B Cells ◽  
Epstein Barr

scholarly journals Compatibility of the gH homologues of Epstein–Barr virus and related lymphocryptoviruses

2007 ◽  
Vol 88 (8) ◽  
pp. 2129-2136 ◽  
Author(s):  
Liguo Wu ◽  
Lindsey M. Hutt-Fletcher
Keyword(s):  
B Cells ◽  
Epithelial Cells ◽  
B Cell ◽  
Cell Fusion ◽  
Epstein Barr Virus ◽  
Common Marmoset ◽  
Barr Virus ◽  
Human B Cells ◽  
The Common ◽  
Epstein Barr

Glycoprotein gH, together with its chaperone gL and a third glycoprotein gB, is essential for cell–cell fusion and virus–cell fusion mediated by herpesviruses. Epstein–Barr virus (EBV), the prototype human lymphocryptovirus, requires a fourth glycoprotein gp42 to support fusion with B cells in addition to epithelial cells. Two other lymphocryptoviruses, the rhesus lymphocryptovirus (Rh-LCV) and the common marmoset lymphocryptovirus (CalHV3), have been sequenced in their entirety and each has a gp42 homologue. Combinations of proteins from EBV, Rh-LCV and CalHV3 were able to mediate fusion of epithelial cells, but, even when complexed with EBV gp42, only Rh-LCV and not CalHV3 proteins were able to mediate fusion with human B cells. CalHV3 gL was also unable to function effectively as a chaperone for EBV or Rh-LCV gH. The Rh-LCV gH homologue supported more fusion than EBV gH with an epithelial cell and supported the highest levels of fusion with a B cell. Chimeric constructs made from Rh-LCV gH and EBV gH that have 85.4 % sequence identity should prove useful for mapping the regions of gH that are of importance to fusion as a whole and to B-cell fusion in particular.

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