H-2Ld class I molecule protects an HIV N-extended epitope from in vitro trimming by endoplasmic reticulum aminopeptidase associated with antigen processing

J Immunol. 2010 Apr 1;184(7):3351-5. doi: 10.4049/jimmunol.0901560. Epub 2010 Mar 3.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antigen Presentation / immunology*
  • Cells, Cultured
  • Endoplasmic Reticulum / immunology
  • Endoplasmic Reticulum / metabolism
  • Epitopes, T-Lymphocyte / immunology
  • Epitopes, T-Lymphocyte / metabolism*
  • H-2 Antigens / immunology
  • H-2 Antigens / metabolism*
  • HIV Envelope Protein gp120 / immunology
  • HIV Envelope Protein gp120 / metabolism*
  • Histocompatibility Antigen H-2D
  • Humans
  • Leucyl Aminopeptidase / immunology
  • Leucyl Aminopeptidase / metabolism*
  • Mice
  • Recombinant Proteins / immunology
  • Recombinant Proteins / metabolism
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Substances

  • Epitopes, T-Lymphocyte
  • H-2 Antigens
  • HIV Envelope Protein gp120
  • Histocompatibility Antigen H-2D
  • Recombinant Proteins
  • Leucyl Aminopeptidase
  • puromycin-insensitive leucyl-specific aminopeptidase