In vitro stimulation of human lymphocytes by Epstein-Barr virus

Studies have been performed on in vitro infection by Epstein-Barr virus (EBV) of subpopulations of human lymphocytes. B cells of adult peripheral or fetal cord blood transform with equal efficiency, whether assayed by DNA synthesis induction or by outgrowth of transformed lymphocytes. In contrast, unfractionated adult lymphocytes transform much less efficiently than those from fetal cord. Reconstitution experiments of different cell preparations indicated that this difference was due to a suppression of B-cell proliferation by adult Ig-negative lymphocytes which fetal Ig-negative lymphocytes were unable to perform. Separation of Ig-negative lymphocytes into various subpopulations revealed that the suppression was performed by T cells. Macrophages and null cells play little or no role in suppression. The relevance of this phenomenon to infection and recovery from EBV infection during and after infectious mononucleosis is discussed.

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Antiviral specificities of immunoglobulins secreted by human lymphocytes immortalized in vitro with Epstein-Barr virus

Annales de l Institut Pasteur Virologie ◽

10.1016/s0769-2617(81)80003-2 ◽

1981 ◽

Vol 132 (3) ◽

pp. 323-335

Author(s):

J.M. Seigneurin ◽

C. Desgranges ◽

J.C. Renversez ◽

M. Baccard ◽

C. Micouin

Keyword(s):

Epstein Barr Virus ◽

Human Lymphocytes ◽

Barr Virus ◽

Epstein Barr

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Stimulation of human lymphocytes with irradiated cells of the autologous Epstein-Barr virus-transformed cell line

Cellular Immunology ◽

10.1016/0008-8749(82)90205-2 ◽

1982 ◽

Vol 67 (1) ◽

pp. 129-140 ◽

Cited By ~ 44

Author(s):

L.E. Wallace ◽

A.B. Rickinson ◽

M. Rowe ◽

D.J. Moss ◽

D.J. Allen ◽

...

Keyword(s):

Cell Line ◽

Epstein Barr Virus ◽

Human Lymphocytes ◽

Transformed Cell ◽

Barr Virus ◽

Transformed Cell Line ◽

Epstein Barr ◽

Stimulation Of

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Immunization of human lymphocytes with Epstein-Barr virus capsid antigens in vitro

Bulletin of Experimental Biology and Medicine ◽

10.1007/bf00841248 ◽

1991 ◽

Vol 111 (1) ◽

pp. 83-86

Author(s):

V. V. Kulikov ◽

A. V. Krivonos ◽

M. E. Krasheninnikov ◽

O. V. Borisova ◽

S. L. Kal'nov

Keyword(s):

Epstein Barr Virus ◽

Human Lymphocytes ◽

Virus Capsid ◽

Barr Virus ◽

Epstein Barr

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Polyclonal Ig production after Epstein-Barr virus infection of human lymphocytes in vitro

Nature ◽

10.1038/267052a0 ◽

1977 ◽

Vol 267 (5606) ◽

pp. 52-54 ◽

Cited By ~ 258

Author(s):

ANDERS ROSÉN ◽

PETER GERGELY ◽

MIKAEL JONDAL ◽

GEORGE KLEIN ◽

SVEN BRITTON

Keyword(s):

Virus Infection ◽

Epstein Barr Virus ◽

Human Lymphocytes ◽

Epstein Barr Virus Infection ◽

Barr Virus ◽

Epstein Barr ◽

Barr Virus Infection

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Dissociation of patching by latent membrane protein-1 of Epstein–Barr virus from its stimulation of NF-κB activity

Journal of General Virology ◽

10.1099/0022-1317-80-12-3227 ◽

1999 ◽

Vol 80 (12) ◽

pp. 3227-3232 ◽

Cited By ~ 5

Author(s):

Tim Bloss ◽

Ajamete Kaykas ◽

Bill Sugden

Keyword(s):

Membrane Protein ◽

Epstein Barr Virus ◽

Latent Membrane Protein ◽

Latent Membrane Protein 1 ◽

Binding Motifs ◽

Mutant Proteins ◽

Barr Virus ◽

Epstein Barr ◽

Stimulation Of

Alterations were made in the amino terminus and the first two transmembrane-spanning regions of the latent membrane protein-1 (LMP-1) of Epstein–Barr virus. These mutant proteins were tested for their abilities to patch and to stimulate NF-κB activity. A subset of these derivatives retains the wild-type topology of LMP-1 in the plasma membrane, but has lost the ability to patch. Deletion of residues 9–20 of LMP-1, which contain potential SH3-binding motifs, abrogates patching of LMP-1. However, mutation of the prolines within these motifs, which eliminates binding of LMP-1 to SH3 domains in vitro, does not prevent patching by LMP-1. Deletion of the first two transmembrane regions of LMP-1 does prevent it patching. Some of the derivatives of LMP-1 which do not patch do stimulate NF-κB activity. Patching by LMP-1 appears to be a higher-order assemblage of protein that is compatible with the stimulation of NF-κB activity but is not necessary for this signalling.

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