The Journal of Experimental Medicine
VeriKine-HS Human IFN-Beta
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© The Rockefeller University Press, 0022-1007/1998/8/773/ $5.00
The Journal of Experimental Medicine, Volume 188, Number 4, August 17, 1998 773-778

Brief Definitive Reports

Glycan-regulated Antigen Processing of a Protein in the Endoplasmic Reticulum Can Uncover Cryptic Cytotoxic T Cell Epitopes

Philip Wood and Tim Elliott

From the Institute for Molecular Medicine and Nuffield Department of Clinical Medicine, University of Oxford, John Radcliffe Hospital, Oxford OX3 9DU, United Kingdom

We and others have shown that influenza A nucleoprotein (NP) targeted to the secretory pathway cannot be processed to yield several cytotoxic T lymphocyte (CTL) epitopes in cell lines that lack the transporter associated with antigen processing (TAP). However, a large COOH-terminal fragment of NP is processed and presented in these cells. Full-length NP is cotranslationally glycosylated in the lumen of the endoplasmic reticulum at two sites distal to the major H2-Kk and H2-Db restricted CTL epitopes, and we show here that pharmacological or genetic inhibition of N-linked glycosylation, leads to the processing and presentation of both these epitopes in a TAP-independent way.

Key Words: cytotoxic T lymphocyte • antigen processing • endoplasmic reticulum • transporter associated with antigen processing • class I major histocompatibility complex

Address correspondence to Tim Elliott, Institute for Molecular Medicine and Nuffield Department of Clinical Medicine, University of Oxford, John Radcliffe Hospital, Oxford OX3 9DU, UK. Phone: 44-1865-221949; Fax: 44-1865-222901; E-mail: tim.elliott{at}ndm.ox.ac.uk


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