Publication: H-2Ld class I molecule protects an HIV N-extended epitope from in vitro trimming by endoplasmic reticulum aminopeptidase associated with antigen processing.
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Publication date
2010-04-01
Authors
Lorente, Elena ISCIII
Jimenez, Mercedes ISCIII
Garcia, Ruth ISCIII
Val, Margarita del ISCIII
Lopez, Daniel ISCIII
Infantes, Susana ISCIII
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Publisher
American Association of Immunologists (AAI)
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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Bibliographic citation
J Immunol . 2010 Apr 1;184(7):3351-5.