| Online-Ressource |
Verfasst von: | Raddrizzani, Laura [VerfasserIn]  |
| Kropshofer, Harald [VerfasserIn]  |
| Hämmerling, Günter J. [VerfasserIn]  |
Titel: | Identification of destabilizing residues in HLA class II-selected bacteriophage display libraries edited by HLA-DM |
Verf.angabe: | Laura Raddrizzani, Elisa Bono, Anne B. Vogt, Harald Kropshofer, Fabio Gallazzi, Tiziana Sturniolo, Günter J. Hämmerling, Francesco Sinigaglia and Juergen Hammer |
E-Jahr: | 2006 |
Jahr: | 28 March 2006 |
Jahr des Originals: | 1999 |
Umfang: | 9 S. |
Fussnoten: | First published: 28 March 2006 ; Elektronische Reproduktion der Druck-Ausgabe ; Gesehen am 16.02.2021 |
Titel Quelle: | Enthalten in: European journal of immunology |
Ort Quelle: | Weinheim : Wiley-VCH, 1971 |
Jahr Quelle: | 1999 |
Band/Heft Quelle: | 29(1999), 2, Seite 660-668 |
ISSN Quelle: | 1521-4141 |
Abstract: | HLA-DM (DM) functions as a peptide editor by catalyzing the release of class II-associated invariant chain peptides (CLIP) and other unstable peptides, thus supporting the formation of stable class II-peptide complexes for presentation. To investigate the general features that determine the DM susceptibility of HLA-DR1/peptide complexes, we generated a large DM-ensitive peptide repertoire from an M13 bacteriophage display library using a novel double selection protocol: we selected bacteriophage capable of binding to DR1 molecules and, subsequently, we enriched DR1-bound bacteriophage susceptible to elution by purified DM molecules. Sequence and mutational analyses of the DR1/DM double-selected peptides revealed that the amino acids Gly and Pro play a destabilizing role in the dissociation kinetics of DR1 ligands. This observation was confirmed also in natural peptide sequences such as CLIP 89 - 101, HA 307 - 319 and bovine collagen II (CII) 261-273. Our results demonstrate that DM susceptibility does not only depend on the number and nature of anchor residues, or the peptide length. Instead, less obvious sequence characteristics play a major role in the DM editing process and ultimately in the composition of peptide repertoires presented to T cells. |
DOI: | doi:10.1002/(SICI)1521-4141(199902)29:02<660::AID-IMMU660>3.0.CO;2-I |
URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext ; Verlag: https://doi.org/10.1002/(SICI)1521-4141(199902)29:02<660::AID-IMMU660>3.0.CO;2-I |
| Volltext: https://onlinelibrary.wiley.com/doi/abs/10.1002/%28SICI%291521-4141%28199902%2929%3A02%3C660%3A%3AAID-IMMU660%3E3.0.CO%3 ... |
| DOI: https://doi.org/10.1002/(SICI)1521-4141(199902)29:02<660::AID-IMMU660>3.0.CO;2-I |
Datenträger: | Online-Ressource |
Sprache: | eng |
Sach-SW: | HLA-DM |
| HLA-DR |
| Peptide binding |
| Peptide editing |
| Phage display |
K10plus-PPN: | 1748435140 |
Verknüpfungen: | → Zeitschrift |
Identification of destabilizing residues in HLA class II-selected bacteriophage display libraries edited by HLA-DM / Raddrizzani, Laura [VerfasserIn]; 28 March 2006 (Online-Ressource)