PMID: 9551364Apr 29, 1998Paper

TAP-independent delivery of antigenic peptides to the endoplasmic reticulum: therapeutic potential and insights into TAP-dependent antigen processing

Journal of Immunotherapy
J W YewdellJ R Bennink

Abstract

We have taken several approaches to investigate the capacity of the secretory pathway to liberate major histocompatibility complex (MHC) class I-restricted antigenic peptides from precursor polypeptides. Cells lacking the peptide transporter (TAP) are unable to deliver peptides from cytosolic antigens to class I molecules. TAP can be bypassed by targeting peptides directly to the endoplasmic reticulum (ER) using NH2-terminal signal sequences. This results in the generation of enormous numbers of MHC class I complexes (50,000 peptides/cell), and recombinant vaccinia viruses expressing such peptides are highly immunogenic. In contrast to signal sequence-targeted peptides, peptides are liberated very inefficiently from internal locations in ER-targeted full-length proteins, indicating that the secretory pathway has a limited capacity for generating antigenic peptides from most polypeptide contexts. We have, however, identified a location in proteins from which peptides can be liberated in numerous contexts in the secretory pathway. Placing a number of different peptides at the COOH termini of a secreted protein and two proteins with type II membrane anchors resulted in their TAP-independent presentation. These findings demonstrate...Continue Reading

Citations

Sep 22, 2001·International Journal for Parasitology·C G Lüder, F Seeber
Feb 27, 1999·Current Opinion in Immunology·P M van Endert
May 30, 2009·Bioinformatics·Tal Vider-ShalitYoram Louzoun
Apr 21, 2005·PLoS Biology·Nathalie E BlachèreMatthew L Albert
Jul 5, 2005·Expert Opinion on Investigational Drugs·L L An, A Sette
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Dec 3, 1999·Biochimica Et Biophysica Acta·R Abele, R Tampé

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