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Identification of destabilizing residues in HLA class II-selected bacteriophage display libraries edited by HLA-DM

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 susce...

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Bibliographic Details
Main Authors: Raddrizzani, Laura (Author) , Kropshofer, Harald (Author) , Hämmerling, Günter J. (Author)
Format: Article (Journal)
Language:English
Published: 28 March 2006
In: European journal of immunology
Year: 1999, Volume: 29, Issue: 2, Pages: 660-668
ISSN:1521-4141
DOI:10.1002/(SICI)1521-4141(199902)29:02<660::AID-IMMU660>3.0.CO;2-I
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1002/(SICI)1521-4141(199902)29:02<660::AID-IMMU660>3.0.CO;2-I
Verlag, lizenzpflichtig, Volltext: https://onlinelibrary.wiley.com/doi/abs/10.1002/%28SICI%291521-4141%28199902%2929%3A02%3C660%3A%3AAID-IMMU660%3E3.0.CO%3B2-I
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Author Notes:Laura Raddrizzani, Elisa Bono, Anne B. Vogt, Harald Kropshofer, Fabio Gallazzi, Tiziana Sturniolo, Günter J. Hämmerling, Francesco Sinigaglia and Juergen Hammer
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Summary: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.
Item Description:First published: 28 March 2006
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Physical Description:Online Resource
ISSN:1521-4141
DOI:10.1002/(SICI)1521-4141(199902)29:02<660::AID-IMMU660>3.0.CO;2-I

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