scholarly journals Human B cells express two types of interleukin-1 receptors

Blood ◽  
1990 ◽  
Vol 75 (10) ◽  
pp. 2017-2023 ◽  
Author(s):  
D Benjamin ◽  
SK Dower
Keyword(s):  
Binding Sites ◽  
Interleukin 1 ◽  
Cell Lineage ◽  
Relative Molecular Mass ◽  
Affinity Binding ◽  
Interleukin 1 Beta ◽  
Binding Assays ◽  
Barr Virus ◽  
Human B Cells ◽  
Epstein Barr

Abstract Several reports demonstrate that interleukin-1 alpha (IL-1 alpha) and interleukin-1 beta (IL-1 beta), although distantly related at the primary sequence level, bind to the same receptor. This raises the question of what separation, if any, there might be between their biologic activities. Receptor binding assays and cross-competition studies in three Epstein Barr virus (EBV) positive cell lines showed that a subset of IL-1 receptors may bind IL-1 alpha preferentially and that a separate subset may bind IL-1 beta preferentially. Crosslinking studies with 125I-IL-1 alpha or 125I-IL-1 beta demonstrated the expression of both relative molecular mass (Mr) 80,500 IL-1 receptor, known to be T cell-specific, and Mr 69,500 IL-1 receptor, recently detected on B-cell lineage only. Whether the high affinity binding sites correspond to Mr 80,500 and the low affinity binding sites to Mr 69,500 remains to be elucidated.

scholarly journals Human B cells express two types of interleukin-1 receptors

Blood ◽  
1990 ◽  
Vol 75 (10) ◽  
pp. 2017-2023
Author(s):  
D Benjamin ◽  
SK Dower
Keyword(s):  
Binding Sites ◽  
Interleukin 1 ◽  
Cell Lineage ◽  
Relative Molecular Mass ◽  
Affinity Binding ◽  
Interleukin 1 Beta ◽  
Binding Assays ◽  
Barr Virus ◽  
Human B Cells ◽  
Epstein Barr

Several reports demonstrate that interleukin-1 alpha (IL-1 alpha) and interleukin-1 beta (IL-1 beta), although distantly related at the primary sequence level, bind to the same receptor. This raises the question of what separation, if any, there might be between their biologic activities. Receptor binding assays and cross-competition studies in three Epstein Barr virus (EBV) positive cell lines showed that a subset of IL-1 receptors may bind IL-1 alpha preferentially and that a separate subset may bind IL-1 beta preferentially. Crosslinking studies with 125I-IL-1 alpha or 125I-IL-1 beta demonstrated the expression of both relative molecular mass (Mr) 80,500 IL-1 receptor, known to be T cell-specific, and Mr 69,500 IL-1 receptor, recently detected on B-cell lineage only. Whether the high affinity binding sites correspond to Mr 80,500 and the low affinity binding sites to Mr 69,500 remains to be elucidated.

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

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 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 Establishment and characterization of an Epstein-Barr virus transformed cell line with strong phagocytic activity

Blood ◽  
1989 ◽  
Vol 74 (1) ◽  
pp. 430-436 ◽  
Author(s):  
P von den Driesch ◽  
R Bhardwaj ◽  
HD Flad ◽  
DC Neugebauer ◽  
HJ Pielken ◽  
...  
Keyword(s):  
Cell Line ◽  
Phagocytic Activity ◽  
Antigen Processing ◽  
Epstein Barr Virus ◽  
Interleukin 1 ◽  
Immunoglobulin M ◽  
Nuclear Antigen ◽  
Barr Virus ◽  
Transformed Cell Line ◽  
Epstein Barr

Abstract An immunoglobulin M (IgM)-positive cell line, Ms 28, apparently spontaneously transformed by Epstein-Barr virus (EBV) was established from peripheral blood cells of a patient with immature myeloblastic leukemia. It has been characterized according to phenotype, cytochemistry, and membrane antigen pattern. The cell line expresses lymphoid markers like CD 19, CD 22, and CD 30 and synthesizes and secretes IgM. Monocyte markers CD 11c, CD 14, and CD 15 are absent. Neither interleukin-1 (IL-1), nor tumor necrosis factor (TNF-alpha) are produced. But Ms 28 cells show strong phagocytic activity and engulf Latex particles and sheep RBCs (SRBCs) that need not to be opsonized. The phagocytic activity can be inhibited by chloroquine. Both phagocytosis and EBV nuclear-antigen (EBNA) expression can be observed in one and the same cell. Ms 28 cells might be useful to study immunologic activities like antigen processing and presentation.

scholarly journals The Late Lytic LMP-1 Protein of Epstein-Barr Virus Can Negatively Regulate LMP-1 Signaling

2000 ◽  
Vol 74 (2) ◽  
pp. 1057-1060 ◽  
Author(s):  
Kimberly D. Erickson ◽  
Jennifer M. Martin
Keyword(s):  
Epstein Barr Virus ◽  
Lytic Cycle ◽  
Dependent Manner ◽  
Reading Frame ◽  
Barr Virus ◽  
Tetradecanoyl Phorbol Acetate ◽  
Human B Cells ◽  
Negative Effect ◽  
Epstein Barr ◽  
Related Proteins

ABSTRACT The BNLF-1 open reading frame of Epstein-Barr virus (EBV) encodes two related proteins, latent membrane protein-1 (LMP-1) and lytic LMP-1 (lyLMP-1). LMP-1 is a latent protein required for immortalization of human B cells by EBV, whereas lyLMP-1 is expressed during the lytic cycle and is found in the EBV virion. We show here that, in contrast to LMP-1, lyLMP-1 is stable, with a half-life of >20 h in tetradecanoyl phorbol acetate- and butyrate-treated B95-8 cells. Although lyLMP-1 itself has negligible effects on NF-κB activity, it inhibits NF-κB activation by LMP-1 in a dose-dependent manner. The lyLMP-1 protein does not oligomerize with LMP-1, and the negative effect of lyLMP-1 on NF-κB activation by LMP-1 does not result from lyLMP-1-mediated disruption of LMP-1 oligomers. Modulation of LMP-1-activated signaling pathways is the first identified biological activity associated with lyLMP-1, and this activity may contribute to the progression of EBV's lytic cycle.

scholarly journals A novel cis-acting element required for lipopolysaccharide-induced transcription of the murine interleukin-1 beta gene.

1995 ◽  
Vol 15 (1) ◽  
pp. 112-119 ◽  
Author(s):  
S A Godambe ◽  
D D Chaplin ◽  
T Takova ◽  
L M Read ◽  
C J Bellone
Keyword(s):  
Binding Site ◽  
Binding Sites ◽  
Competitive Inhibition ◽  
Interleukin 1 ◽  
Sodium Dodecyl ◽  
Regulatory Elements ◽  
Nuclear Factor ◽  
Interleukin 1 Beta ◽  
Factor Binding ◽  
Beta Gene

Regulatory elements important for transcription of the murine interleukin-1 beta (IL-1 beta) gene lie within a DNase I-hypersensitive region located > 2,000 bp upstream from the transcription start site. We have identified within this region a novel positive regulatory element that is required for activation of an IL-1 beta promoter-chloramphenicol acetyltransferase (CAT) fusion gene in the murine macrophage line RAW264.7. Electrophoretic mobility shift analysis of the 3' portion (-2315 to -2106) of the hypersensitive region revealed at least two nuclear factor binding sites, one of which is located between positions -2285 and -2256. Competitive inhibition studies localized the binding site to a 15-bp sequence between -2285 and -2271. Nuclear factor binding was lost by mutation of the 6-bp sequence from -2280 to -2275. The specific retarded complex formed with RAW264.7 nuclear extract was not detected under similar conditions with nuclear extracts from RLM-11, a murine T-cell line which does not express IL-1 beta RNA. Mutation of the 6-bp sequence (-2280 to -2275) in the chimeric IL-1 beta promoter -4093 +I CAT plasmid virtually eliminated the activation of this reporter gene by lipopolysaccharide (LPS) in transfected RAW264.7 cells. Multimerization of the 15-bp sequence containing the core wild-type 6-bp sequence 5' of minimal homologous or heterologous promoters in CAT reporter plasmids resulted in significant enhancement of CAT expression compared with parallel constructs containing the mutant 6-bp core sequence. This element was LPS independent and position and orientation dependent. The multimerized 15-bp sequence did not enhance expression in RLM-11 cells. Methylation interference revealed contact residues from -2281 to -2271, CCAAAAAGGAA. Because a search of the NIH TFD data bank with the 11-bp binding site sequence found no homology to known nuclear factor binding sites, we have designated this sequence the IL1 beta -upstream nuclear factor 1 (IL1 beta -UNF1) target. UV cross-linking and sodium dodecyl sulfate-polyacrylamide electrophoresis identified an IL1 beta -UNF1-specific binding factor approximately 85 to 90 kDa in size.

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