Cutting Edge: H-2Ld Class I Molecule Protects an HIV N-Extended Epitope from In Vitro Trimming by Endoplasmic Reticulum Aminopeptidase Associated with Antigen Processing

  • Infantes S
  • Samino Y
  • Lorente E
  • et al.
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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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Infantes, S., Samino, Y., Lorente, E., Jiménez, M., García, R., Del Val, M., & López, D. (2010). Cutting Edge: H-2Ld Class I Molecule Protects an HIV N-Extended Epitope from In Vitro Trimming by Endoplasmic Reticulum Aminopeptidase Associated with Antigen Processing. The Journal of Immunology, 184(7), 3351–3355. https://doi.org/10.4049/jimmunol.0901560

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