Cutting Edge: H-2Ld Class I Molecule Protects an HIV N-Extended Epitope from In Vitro Trimming by Endoplasmic Reticulum Aminopeptidase Associated with Antigen Processing
Author(s) -
Susana Infantes,
Yolanda Samino,
Elena Lorente,
Mercedes Jiménez,
Ruth García,
Margarita Del Val,
Daniel López
Publication year - 2010
Publication title -
the journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.737
H-Index - 372
eISSN - 1550-6606
pISSN - 0022-1767
DOI - 10.4049/jimmunol.0901560
Subject(s) - endoplasmic reticulum , mhc class i , antigen processing , aminopeptidase , antigen presentation , transporter associated with antigen processing , major histocompatibility complex , cytotoxic t cell , epitope , in vitro , mhc restriction , antigen , biology , peptide , chemistry , microbiology and biotechnology , biochemistry , immunology , amino acid , leucine
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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