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Quality control of MHC class II associated peptides by HLA-DM H2-M

For many years the crucial components involved in MHC class II mediated antigen presentation have been thought to be known: polymorphic MHC class II molecules, the monomorphic invariant chain (li) and a set of conventional proteases that cleave antigenic proteins thereby generating ligands able to a...

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Hauptverfasser: Vogt, Anne B. (VerfasserIn) , Hämmerling, Günter J. (VerfasserIn) , Kropshofer, Harald (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 25 May 2002
In: Seminars in immunology
Year: 1999, Jahrgang: 11, Heft: 6, Pages: 391-403
ISSN:1096-3618
DOI:10.1006/smim.1999.0197
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1006/smim.1999.0197
Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S1044532399901975
Volltext
Verfasserangaben:Anne B. Vogt, S. Oliver Arndt, Günter J. Hämmerling and Harald Kropshofer

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520 |a For many years the crucial components involved in MHC class II mediated antigen presentation have been thought to be known: polymorphic MHC class II molecules, the monomorphic invariant chain (li) and a set of conventional proteases that cleave antigenic proteins thereby generating ligands able to associate with MHC class II molecules. However, in 1994 it was found that without an additional molecule, HLA-DM (DM), efficient presentation of protein antigens cannot be achieved. Biochemical studies showed that DM acts as a molecular chaperone protecting empty MHC class II molecules from functional inactivation. In addition, it serves as a peptide editor: DM catalyzes not only the release of the invariant chain remnant CLIP, but of all sorts of low-stability peptides, and simultaneously favors binding of high-stability peptides. Through this quality control of peptide loading, DM enables APCs to optimize MHC restriction and to display their antigenic peptide cargo on the surface for prolonged periods of time to be scrutinized by T cells. 
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