Destructive cleavage of antigenic peptides either by the immunoproteasome or by the standard proteasome results in differential antigen presentation

Détails

ID Serval
serval:BIB_295276F73668
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Destructive cleavage of antigenic peptides either by the immunoproteasome or by the standard proteasome results in differential antigen presentation
Périodique
Journal of Immunology
Auteur⸱e⸱s
Chapiro  J., Claverol  S., Piette  F., Ma  W., Stroobant  V., Guillaume  B., Gairin  J. E., Morel  S., Burlet-Schiltz  O., Monsarrat  B., Boon  T., Van den Eynde  B. J.
ISSN
0022-1767 (Print)
Statut éditorial
Publié
Date de publication
01/2006
Volume
176
Numéro
2
Pages
1053-61
Notes
Comparative Study
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Jan 15
Résumé
The immunoproteasome (IP) is usually viewed as favoring the production of antigenic peptides presented by MHC class I molecules, mainly because of its higher cleavage activity after hydrophobic residues, referred to as the chymotrypsin-like activity. However, some peptides have been found to be better produced by the standard proteasome. The mechanism of this differential processing has not been described. By studying the processing of three tumor antigenic peptides of clinical interest, we demonstrate that their differential processing mainly results from differences in the efficiency of internal cleavages by the two proteasome types. Peptide gp100(209-217) (ITDQVPSFV) and peptide tyrosinase369-377 (YMDGTMSQV) are destroyed by the IP, which cleaves after an internal hydrophobic residue. Conversely, peptide MAGE-C2(336-344) (ALKDVEERV) is destroyed by the standard proteasome by internal cleavage after an acidic residue, in line with its higher postacidic activity. These results indicate that the IP may destroy some antigenic peptides due to its higher chymotrypsin-like activity, rather than favor their production. They also suggest that the sets of peptides produced by the two proteasome types differ more than expected. Considering that mature dendritic cells mainly contain IPs, our results have implications for the design of immunotherapy strategies.
Mots-clé
Amino Acid Sequence *Antigen Presentation Antigens/genetics/*metabolism Antigens, Neoplasm Binding Sites Cell Line Dendritic Cells/enzymology/immunology Humans Membrane Glycoproteins/genetics/metabolism Molecular Sequence Data Monophenol Monooxygenase/genetics/metabolism Neoplasm Proteins/genetics/metabolism Oligopeptides/genetics/*immunology/*metabolism Peptide Fragments/genetics/immunology/metabolism Proteasome Endopeptidase Complex/*immunology/*metabolism
Pubmed
Web of science
Création de la notice
28/01/2008 9:36
Dernière modification de la notice
20/08/2019 13:09
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