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Updated: Jun 15, 2026

A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes
Published on: March 25, 2014
H-2Ld class I molecule protects an HIV N-extended epitope from in vitro trimming by endoplasmic reticulum
Susana Infantes1, Yolanda Samino, Elena Lorente
1Unidad de Proteómica, Centro Nacional de Microbiología, Instituto de Salud Carlos III, Consejo Superior de Investigaciones Científicas/Universidad Autónoma de Madrid, Madrid, Spain.
Abstract:
In the classical MHC class I Ag presentation pathway, antigenic peptides derived from viral proteins by multiple proteolytic cleavages are transported to the endoplasmic reticulum lumen and are then exposed to ami-nopeptidase activity. In the current study, a long MHC class I natural ligand recognized by cytotoxic T lymphocytes was used to study the kinetics of degradation by aminopeptidase. The in vitro data indicate that this N-extended peptide is efficiently trimmed to a 9-mer, unless its binding to the MHC molecules protects the full-length peptide.
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