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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.

Original publication

DOI

10.1084/jem.188.4.773

Type

Journal article

Journal

The Journal of experimental medicine

Publication Date

08/1998

Volume

188

Pages

773 - 778

Addresses

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

Keywords

T-Lymphocytes, Cytotoxic, Cell Line, COS Cells, Endoplasmic Reticulum, Animals, Humans, Polysaccharides, Proteins, Epitopes, T-Lymphocyte, Antigen Presentation, Glycosylation