A spliced Epstein-Barr virus gene expressed in immortalized lymphocytes is created by circularization of the linear viral genome.

Laux, Gerhard; Perricaudet, Michel; Farrell, Paul J.

doi:10.1002/j.1460-2075.1988.tb02874.x

Cited by 192 publications

(147 citation statements)

References 49 publications

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“…CBMI-RAL-STO is a lymphoblastoid cell line (LCL) established from cord blood with the Rael strain of EBV and Jac-1 and BK are LCL from peripheral blood of healthy individuals after infection with the B-95-8 strain of EBV. The following HEK 293 (Graham et al, 1977;Shaw et al, 2002) cell lines were used: 293T, which expresses the SV40 T-antigen; 293P, which is a pLXPOP vector control (Winberg et al, 2000); C4 and IC2 express the LMP2A gene from the B95-8 strain of EBV (Laux et al, 1988), cloned in the pLXPOP vector; LMP2A2-31 stably expresses LMP2A from the pLNPOX vector, derived from the pLNCX vector (a gift of AD Miller, Genbank M28247) by insertion of the poliovirus 5 0 -UTR ribosome entry site (PO) in place of the CMV intermediate early promoter. Welsh et al, 1998;and Welsh, personal communication).…”

Section: Methodsmentioning

confidence: 99%

“…Full-length wild type (wt) and 4 Â Flag-tagged wt LMP2A (Winberg et al, 2000;Ingham et al, 2005) were based on the pSP64-23TP plasmid, a kind gift from Dr P Farrell (Laux et al, 1988). Vectors LMP2A point mutations Y64F, Y74F, Y64/74F and Y74/85F were constructed in the pLXPOP vector using overlap recombination PCR.…”

Section: Shb Interaction With Ebv Lmp2a LV Matskova Et Almentioning

confidence: 99%

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The Shb signalling scaffold binds to and regulates constitutive signals from the Epstein–Barr virus LMP2A membrane protein

et al. 2007

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The Epstein-Barr virus latency-associated membrane protein LMP2A has been shown to activate the survival kinase Akt in epithelial and B cells in a phosphoinositide 3-kinase-dependent fashion. In this study, we demonstrate that the signalling scaffold Shb associates through SH2 and PTB domain interactions with phosphorylated tyrosine motifs in the LMP2A N-terminal tail. Additionally, we show that mutation of tyrosines in these motifs as well as shRNA-mediated downregulation of Shb leads to a loss of constitutive Akt-activation in LMP2A-expressing cells. Furthermore, utilization by Shb of the LMP2A ITAM motif regulates stability of the Syk tyrosine kinase in LMP2A-expressing cells. Our data set the precedent for viral utilization of the Shb signalling scaffold and implicate Shb as a regulator of LMP2A-dependent Akt activation.

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Section: Methodsmentioning

confidence: 99%

Section: Shb Interaction With Ebv Lmp2a LV Matskova Et Almentioning

confidence: 99%

The Shb signalling scaffold binds to and regulates constitutive signals from the Epstein–Barr virus LMP2A membrane protein

et al. 2007

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“…These include the nuclear antigens, EBNAs 1, 2, 3a, 3b, 3c and -LP, whose expression is controUed from one of two transcriptional promoters in the BamHI CW region of the virus genome (Speck & Strominger, 1989), and a latent membrane protein (LMP) whose expression is under separate transcriptional control. These seven virus-encoded latent proteins can now be individually identified using monospecific or monoclonal antibody (MAb) preparations; an eight latent gene product, terminal protein or LMP2, has been predicted to exist from cDNA cloning work but has not yet been identified unequivocally (Laux et al, 1988;Sample et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

Different Epstein--Barr virus--B cell interactions in phenotypically distinct clones of a Burkitt's lymphoma cell line

Gregory

Rowe

Rickinson

1990

Journal of General Virology

308

265

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“…The majority of cells in an LCL express only the latent EB viral gene products which are compatible with continued cell proliferation. These include the EB viral nuclear antigen complex (EBNA) 1 to 6 (Dillner & Kallin, 1988;Allday et al, 1988), the latent membrane protein (LMP) and the products of the terminal protein gene (Laux et al, 1988). The functions of these proteins are for the most part unknown, but EBNA 1 is essential for maintenance of the viral episome (Yates et al, 1985).…”

Section: Introductionmentioning

confidence: 99%

Immortalization of Epstein--Barr virus-infected CD23-negative B lymphocytes by the addition of B cell growth factor

Azim

Allday

Crawford

1990

Journal of General Virology

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Epstein-Barr (EB) virus-immortalized B lymphocytes coexpress the EB viral latent gene products (EB viral nuclear antigens 1 to 6, the latent membrane protein and the terminal protein gene products) and the cellular activation antigen CD23. Immortalized B cells can be separated from those which are infected but not immortalized on the basis of CD23 expression as early as 2 days after in vitro infection. In the present report we have confirmed these data, but show that if left in culture for 7 days after infection before separation the CD23-negative cells show a donor-related ability to become CD23-positive and immortalize. CD23-negative cells separated 2 days after infection can be induced to immortalize by the addition of low Mr B cell growth factor but not by the addition of recombinant interleukin 1, 4 or soluble CD23. At 2 to 3 days after infection the EB viral nuclear antigens 1, 2 and the high Mr species 3, 4 and 6, as well as the latent membrane protein can be detected in the CD23-positive fraction. In contrast at this time only nuclear antigens 1 and 2 could be detected in the CD23-negative fraction. This difference in gene expression may account for the inability of the CD23-negative fraction to immortalize. In the light of these observations the mechanism of viral persistence in vivo is discussed.

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A spliced Epstein-Barr virus gene expressed in immortalized lymphocytes is created by circularization of the linear viral genome.

Cited by 192 publications

References 49 publications

The Shb signalling scaffold binds to and regulates constitutive signals from the Epstein–Barr virus LMP2A membrane protein

The Shb signalling scaffold binds to and regulates constitutive signals from the Epstein–Barr virus LMP2A membrane protein

Different Epstein--Barr virus--B cell interactions in phenotypically distinct clones of a Burkitt's lymphoma cell line

Immortalization of Epstein--Barr virus-infected CD23-negative B lymphocytes by the addition of B cell growth factor

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