H-2Ld class I molecule protects an HIV N-extended epitope from in vitro trimming by endoplasmic reticulum aminopeptidase associated with antigen processing
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 recogniz...
| Authors: | , , , , , , |
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| Format: | article |
| Publication Date: | 2010 |
| Country: | España |
| Institution: | Instituto de Salud Carlos III (ISCIII) |
| Repository: | Repisalud |
| Language: | English |
| OAI Identifier: | oai:repisalud.isciii.es:20.500.12105/10655 |
| Online Access: | http://hdl.handle.net/20.500.12105/10655 |
| Access Level: | Open access |
| Keyword: | 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 |
| Summary: | 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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