Journal
JOURNAL OF IMMUNOLOGY
Volume 177, Issue 1, Pages 227-233Publisher
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.177.1.227
Keywords
-
Categories
Funding
- Intramural NIH HHS Funding Source: Medline
Ask authors/readers for more resources
There is mounting evidence that MHC class I peptide ligands are predominantly generated from defective ribosomal products and other classes of polypeptides degraded rapidly (t(1/2) < 10 min) following their synthesis. The most direct eviden supporting this conclusion is the rapid inhibition of peptide ligand generation following cyclobeximide-mediated inhibition of protein synthesis. In this study, we show that this linkage is due to depleting the pool of rapidly degraded proteins, and not to interference with other protein synthesis-dependent processes. Our findings indicate that in the model systems used in this study, MHC class I peptides are preferentially generated from rapidly degraded polypeptides relative to slowly degraded proteins. This conclusion is supported by the properties of peptide presentation from slowly degraded (t(1/2) = 4 h) defective ribosomal products generated artificially by incorporation of the amino acid analog canavanine into a model viral Ag. We propose that specialized machinery exists to link protein synthesis with class I peptide ligand generation to enable the rapid detection of viral gene expression.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available