Biological differences between epstein-barr virus (EBV) strains with regard to lymphocyte transforming ability, superinfection and antigen induction

Menezes, José; Leibold, W.; Klein, George

doi:10.1016/0014-4827(75)90404-8

Cited by 140 publications

(89 citation statements)

References 10 publications

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“…All CD19ϩ preparations contained Ͻ3% of other PBMCs. Viral preparations of EBV strains from the B95.8 marmoset cell line were produced by the standard procedure (27). Cells were infected with EBV (10 5 transforming units) and cultured in complete medium in 75-cm 2 tissue culture flasks.…”

Section: Methodsmentioning

confidence: 99%

Deiminated Epstein‐Barr virus nuclear antigen 1 is a target of anti–citrullinated protein antibodies in rheumatoid arthritis

Pratesi

Tommasi

Anzilotti

et al. 2006

Arthritis & Rheumatism

120

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Objective. To test the hypothesis that deimination of viral sequences containing Arg-Gly repeats could generate epitopes recognized by anti-citrullinated protein antibodies (ACPAs) that are present in rheumatoid arthritis (RA) sera.Methods. Multiple antigen peptides derived from Epstein-Barr virus (EBV)-encoded Epstein-Barr nuclear antigen 1 (EBNA-1) were synthesized, substituting the arginines with citrulline, and were used to screen RA sera. Anti-cyclic citrullinated peptide antibodies were purified by affinity chromatography and tested on a panel of in vitro deiminated proteins. Their ability to bind in vivo deiminated proteins was evaluated by immunoprecipitation, using EBV-infected cell lines.Results. Antibodies specific for a peptide corresponding to the EBNA-1 35-58 sequence containing citrulline in place of arginine (viral citrullinated peptide [VCP]) were detected in 50% of RA sera and in <5% of normal and disease control sera. In addition, affinitypurified anti-VCP antibodies from RA sera reacted with filaggrin-derived citrullinated peptides, with deiminated fibrinogen, and with deiminated recombinant EBNA-1. Moreover, anti-VCP antibodies immunoprecipitated, from the lysate of calcium ionophore-stimulated lymphoblastoid cell lines, an 80-kd band that was reactive with a monoclonal anti-EBNA-1 antibody and with anti-modified citrulline antibodies.Conclusion. These data indicate that ACPAs react with a viral deiminated protein and suggest that EBV infection may play a role in the induction of these RA-specific antibodies.

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Section: Methodsmentioning

confidence: 99%

Deiminated Epstein‐Barr virus nuclear antigen 1 is a target of anti–citrullinated protein antibodies in rheumatoid arthritis

Pratesi

Tommasi

Anzilotti

et al. 2006

Arthritis & Rheumatism

120

View full text Add to dashboard Cite

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“…Viral particles were resuspended in RPMI 1640 medium and kept at Ϫ80°C until use. Viral titers were evaluated and adjusted to 10 7 transforming units (TFU/ml), as previously described (21). For every experiment, cell-free supernatants collected from B95-8 cells that have not been exposed to PMA were processed as described above and served for mock-infected controls.…”

Section: Viral Preparationsmentioning

confidence: 99%

EBV Suppresses Prostaglandin E2 Biosynthesis in Human Monocytes

Savard

Bélanger

Tremblay

et al. 2000

The Journal of Immunology

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It is well known that EBV has developed strategies to evade immune surveillance. Previously, EBV was shown to bind specifically to monocytes and regulate expression of proinflammatory mediators such as IL-1, IL-6, TNF-α, and leukotrienes. EBV was also found to affect phagocytosis of monocytes. In this study, we show that in addition to these effects, EBV suppresses the biosynthesis of PGE2, a pleiotropic immunomodulatory molecule that is synthesized by the dioxygenation of arachidonic acid via the cyclooxygenase (COX) pathway. This down-regulation of PGE2 formation involved the inhibition of the inducible COX-2 isoform expression both at the transcriptional and translational levels, whereas expression of the constitutive COX-1 isoform was unaltered. Furthermore, exposure of monocytes to EBV was found to impact on the NF-κB activation pathway, which plays an essential role in the induction of COX-2 in monocytes. The inhibition of PGE2 biosynthesis was relieved when the experiments were conducted in presence of phosphonoacetic acid, an inhibitor of herpesviruses DNA polymerase, indicating that viral replication and/or neosynthesized viral proteins were involved in this process. Thus, inhibition of PGE2 biosynthesis in monocytes may represent an additional mechanism underlying EBV pathogenicity.

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“…LCL#3 (Sinclair et al, 1994), B95-8PF (Farrell et al, 1991) and IB4 (King et al, 1980) were established by immortalization of primary B-cells with the B95-8 strain of EBV. BJAB was originally derived from an EBV-negative B-lymphoma and does not harbour any of the c-myc/immunoglobulin translocations that are characteristic of Burkitt's lymphoma (Clements et al, 1975;Menezes et al, 1975). SAOS (Diller et al, 1990) and U2OS (Ponten and Saksela, 1967) were originally derived from osteosarcomas.…”

Section: Cell Culturementioning

confidence: 99%

Loss of functional pRB is not a ubiquitous feature of B-cell malignancies

Sinclair

Frost

1999

Br J Cancer

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Summary Human cancers frequently sustain genetic mutations that alter the function of their G1 cell cycle control check point. These include changes to the retinoblastoma gene and to the genes that regulate its phosphorylation, such as the cyclin-dependent kinase inhibitor p16 INK4a . Altered expression of retinoblastoma protein (pRb) is associated with non-Hodgkin's lymphoma, particularly centroblastic and Burkitt's lymphomas. pRb is expressed in normal B-cells and its regulatory phosphorylation pathway is activated in response to a variety of stimuli. Since human B-lymphoma-derived cell lines are often used as in vitro model systems to analyse the downstream effects of signal transduction, we examined the functional status of pRb in a panel of human B-cell lines. We identified eleven cell lines which express the hyperphosphorylated forms of pRb. Furthermore, we suggest that the pRb protein appears to be functional in these cell lines.

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Biological differences between epstein-barr virus (EBV) strains with regard to lymphocyte transforming ability, superinfection and antigen induction

Cited by 140 publications

References 10 publications

Deiminated Epstein‐Barr virus nuclear antigen 1 is a target of anti–citrullinated protein antibodies in rheumatoid arthritis

Deiminated Epstein‐Barr virus nuclear antigen 1 is a target of anti–citrullinated protein antibodies in rheumatoid arthritis

EBV Suppresses Prostaglandin E2 Biosynthesis in Human Monocytes

Loss of functional pRB is not a ubiquitous feature of B-cell malignancies

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