Samino, YolandaLorente, ElenaJimenez, MercedesGarcia, RuthVal, Margarita delLopez, DanielInfantes, Susana2020-07-062020-07-062010-04-01J Immunol . 2010 Apr 1;184(7):3351-5.0022-1767http://hdl.handle.net/20.500.12105/10655In 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.engAMhttp://creativecommons.org/licenses/by-nc-sa/4.0/AnimalsAntigen PresentationCells, CulturedEndoplasmic ReticulumEpitopes, T-LymphocyteH-2 AntigensHIV Envelope Protein gp120Histocompatibility Antigen H-2DHumansLeucyl AminopeptidaseMiceRecombinant ProteinsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationH-2Ld class I molecule protects an HIV N-extended epitope from in vitro trimming by endoplasmic reticulum aminopeptidase associated with antigen processingAtribución-NoComercial-CompartirIgual 4.0 Internacional2020027818473351-510.4049/jimmunol.09015601550-6606Journal of immunology (Baltimore, Md. : 1950)open access