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

Tellam, J., Connolly, G., Green, K. J., Miles, J. J., Moss, D. J., Burrows, S. R. and Khanna, R. (2004) Endogenous Presentation of CD8+ T Cell Epitopes from Epstein-Barr Virus–encoded Nuclear Antigen 1. Journal of Experimental Medicine, 199 10: 1421-1431. doi:10.1084/jem.20040191

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Author Tellam, J.
Connolly, G.
Green, K. J.
Miles, J. J.
Moss, D. J.
Burrows, S. R.
Khanna, R.
Title Endogenous Presentation of CD8+ T Cell Epitopes from Epstein-Barr Virus–encoded Nuclear Antigen 1
Journal name Journal of Experimental Medicine   Check publisher's open access policy
ISSN 0022-1007
Publication date 2004
Sub-type Article (original research)
DOI 10.1084/jem.20040191
Open Access Status File (Publisher version)
Volume 199
Issue 10
Start page 1421
End page 1431
Total pages 11
Editor P. L. Bernstein
Place of publication New York, U.S.A.
Publisher Rockefeller University Press
Collection year 2004
Language eng
Subject C1
320202 Cellular Immunology
730102 Immune system and allergy
Abstract 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 front EBNA1.
Keyword Immunology
Medicine, Research & Experimental
Cd8(+) T Cell
Antigen Processing
Ala Repeat Domain
Q-Index Code C1

Document type: Journal Article
Sub-type: Article (original research)
Collections: 2005 Higher Education Research Data Collection
School of Medicine Publications
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Citation counts: TR Web of Science Citation Count  Cited 106 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 112 times in Scopus Article | Citations
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Created: Wed, 15 Aug 2007, 03:06:49 EST