Sequence variation of cytotoxic T cell epitopes in different isolates of Epstein-Barr virus

1992 ◽  
Vol 22 (1) ◽  
pp. 183-189 ◽  
Author(s):  
Ann Apolloni ◽  
Denis Moss ◽  
Robyn Stumm ◽  
Scott Burrows ◽  
Andreus Suhrbier ◽  
...  
Keyword(s):  
T Cell ◽  
Epstein Barr Virus ◽  
Sequence Variation ◽  
Cytotoxic T Cell ◽  
T Cell Epitopes ◽  
Barr Virus ◽  
Epstein Barr

scholarly journals Five new cytotoxic T cell epitopes identified within Epstein-Barr virus nuclear antigen 3

1994 ◽  
Vol 75 (9) ◽  
pp. 2489-2493 ◽  
Author(s):  
S. R. Burrows ◽  
J. Gardner ◽  
R. Khanna ◽  
T. Steward ◽  
D. J. Moss ◽  
...  
Keyword(s):  
T Cell ◽  
Epstein Barr Virus ◽  
Nuclear Antigen ◽  
Cytotoxic T Cell ◽  
T Cell Epitopes ◽  
Barr Virus ◽  
Epstein Barr

scholarly journals Conservation of Epstein-Barr Virus Cytotoxic T-Cell Epitopes in Posttransplant Lymphomas

2002 ◽  
Vol 160 (5) ◽  
pp. 1839-1845 ◽  
Author(s):  
Qian Tao ◽  
Jie Yang ◽  
He Huang ◽  
Lode J. Swinnen ◽  
Richard F. Ambinder
Keyword(s):  
T Cell ◽  
Epstein Barr Virus ◽  
Cytotoxic T Cell ◽  
T Cell Epitopes ◽  
Barr Virus ◽  
Epstein Barr

scholarly journals Helper cell-independent cytotoxic clones in man.

1982 ◽  
Vol 156 (6) ◽  
pp. 1854-1859 ◽  
Author(s):  
S L Wee ◽  
L K Chen ◽  
G Strassmann ◽  
F H Bach
Keyword(s):  
T Cell ◽  
Epstein Barr Virus ◽  
Helper Cell ◽  
Cytotoxic T Cell ◽  
Lymphoblastoid Cell Lines ◽  
Barr Virus ◽  
Mediate Cytotoxicity ◽  
Epstein Barr ◽  
And Function

We report here a class of helper cell-independent cytotoxic T cell (HITc) clones in man that can proliferate in response to antigenic stimulation as well as mediate cytotoxicity. HITc appear to be rare among clones derived from primary in vitro allosensitized culture, but constitute the majority of clones derived from cells sensitized to autologous Epstein-Barr virus-transformed lymphoblastoid cell lines. The implications of the derivation and function of HITc clones are discussed.

scholarly journals Epstein-Barr Virus Isolates Retain Their Capacity To Evade T Cell Immunity through BNLF2a despite Extensive Sequence Variation

2011 ◽  
Vol 86 (1) ◽  
pp. 572-577 ◽  
Author(s):  
D. Horst ◽  
S. R. Burrows ◽  
D. Gatherer ◽  
B. van Wilgenburg ◽  
M. J. Bell ◽  
...  
Keyword(s):  
T Cell ◽  
Epstein Barr Virus ◽  
Sequence Variation ◽  
T Cell Immunity ◽  
Extensive Sequence ◽  
Barr Virus ◽  
Cell Immunity ◽  
Epstein Barr ◽  
Virus Isolates

EPSTEIN-BARR VIRUS-SPECIFIC CYTOTOXIC T CELL RESPONSE IN CARDIAC TRANSPLANT RECIPIENTS

1994 ◽  
Vol 57 (11) ◽  
pp. 1611-1616
Author(s):  
Myat T. Kyaw-Tanner ◽  
Donald Esmore ◽  
Scott R. Burrows ◽  
Elizabeth M. Benson ◽  
Tom B. Sculley
Keyword(s):  
T Cell ◽  
Cell Response ◽  
Epstein Barr Virus ◽  
T Cell Response ◽  
Cytotoxic T Cell ◽  
Cardiac Transplant ◽  
Transplant Recipients ◽  
Barr Virus ◽  
Epstein Barr

scholarly journals Computer-Aided Design of an Epitope-Based Vaccine against Epstein-Barr Virus

2017 ◽  
Vol 2017 ◽  
pp. 1-15 ◽  
Author(s):  
Julio Alonso-Padilla ◽  
Esther M. Lafuente ◽  
Pedro A. Reche
Keyword(s):  
T Cell ◽  
B Cell ◽  
Epstein Barr Virus ◽  
Cell Epitope ◽  
T Cell Epitopes ◽  
Cell Component ◽  
B Cell Epitopes ◽  
Barr Virus ◽  
Epstein Barr ◽  
Epitope Selection

Epstein-Barr virus is a very common human virus that infects 90% of human adults. EBV replicates in epithelial and B cells and causes infectious mononucleosis. EBV infection is also linked to various cancers, including Burkitt’s lymphoma and nasopharyngeal carcinomas, and autoimmune diseases such as multiple sclerosis. Currently, there are no effective drugs or vaccines to treat or prevent EBV infection. Herein, we applied a computer-aided strategy to design a prophylactic epitope vaccine ensemble from experimentally defined T and B cell epitopes. Such strategy relies on identifying conserved epitopes in conjunction with predictions of HLA presentation for T cell epitope selection and calculations of accessibility and flexibility for B cell epitope selection. The T cell component includes 14 CD8 T cell epitopes from early antigens and 4 CD4 T cell epitopes, targeted during the course of a natural infection and providing a population protection coverage of over 95% and 81.8%, respectively. The B cell component consists of 3 experimentally defined B cell epitopes from gp350 plus 4 predicted B cell epitopes from other EBV envelope glycoproteins, all mapping in flexible and solvent accessible regions. We discuss the rationale for the formulation and possible deployment of this epitope vaccine ensemble.

scholarly journals Endogenous Presentation of CD8+ T Cell Epitopes from Epstein-Barr Virus–encoded Nuclear Antigen 1

2004 ◽  
Vol 199 (10) ◽  
pp. 1421-1431 ◽  
Author(s):  
Judy Tellam ◽  
Geoff Connolly ◽  
Katherine J. Green ◽  
John J. Miles ◽  
Denis J. Moss ◽  
...  
Keyword(s):  
T Cell ◽  
B Cells ◽  
Antigen Processing ◽  
Epstein Barr Virus ◽  
Cd8 T Cell ◽  
Nuclear Antigen ◽  
T Cell Epitopes ◽  
Barr Virus ◽  
Degradation Rates ◽  
Epstein Barr

Epstein-Barr virus (EBV)–encoded nuclear antigen (EBNA)1 is thought to escape cytotoxic T lymphocyte (CTL) recognition through either self-inhibition of synthesis or by blockade of proteasomal degradation by the glycine-alanine repeat (GAr) domain. Here we show that EBNA1 has a remarkably varied cell type–dependent stability. However, these different degradation rates do not correspond to the level of major histocompatibility complex class I–restricted presentation of EBNA1 epitopes. In spite of the highly stable expression of EBNA1 in B cells, CTL epitopes derived from this protein are efficiently processed and presented to CD8+ T cells. Furthermore, we show that EBV-infected B cells can readily activate EBNA1-specific memory T cell responses from healthy virus carriers. Functional assays revealed that processing of these EBNA1 epitopes is proteasome and transporter associated with antigen processing dependent. We also show that the endogenous presentation of these epitopes is dependent on the newly synthesized protein rather than the long-lived stable EBNA1. Based on these observations, we propose that defective ribosomal products, not the full-length antigen, are the primary source of endogenously processed CD8+ T cell epitopes from EBNA1.

Sign in / Sign up

Export Citation Format

Share Document