Please use this identifier to cite or link to this item:http://hdl.handle.net/20.500.12105/10655
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.
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.
Animals | Antigen Presentation | Cells, Cultured | Endoplasmic Reticulum | Epitopes, T-Lymphocyte | H-2 Antigens | HIV Envelope Protein gp120 | Histocompatibility Antigen H-2D | Humans | Leucyl Aminopeptidase | Mice | Recombinant Proteins | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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