Kinetic analysis of peptide loading onto HLA-DR molecules mediated by HLA-DM.
The nonclassical major histocompatibility complex class II molecule HLA-DM (DM) has recently been shown to play a central role in the class II-associated antigen presentation pathway: DM releases invariant chain-derived CLIP peptides (class II-associated invariant chain protein peptide) from HLA-DR...
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| Main Authors: | , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
September 3, 1996
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| In: |
Proceedings of the National Academy of Sciences of the United States of America
Year: 1996, Volume: 93, Issue: 18, Pages: 9724-9729 |
| ISSN: | 1091-6490 |
| DOI: | 10.1073/pnas.93.18.9724 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1073/pnas.93.18.9724 Verlag, lizenzpflichtig, Volltext: https://www.pnas.org/doi/10.1073/pnas.93.18.9724 
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| Author Notes: | Anne B. Vogt, Harald Kropshofer, Gerhard Moldenhauer, and Günter J. Hämmerling |
MARC
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| 245 | 1 | 0 | |a Kinetic analysis of peptide loading onto HLA-DR molecules mediated by HLA-DM. |c Anne B. Vogt, Harald Kropshofer, Gerhard Moldenhauer, and Günter J. Hämmerling |
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| 520 | |a The nonclassical major histocompatibility complex class II molecule HLA-DM (DM) has recently been shown to play a central role in the class II-associated antigen presentation pathway: DM releases invariant chain-derived CLIP peptides (class II-associated invariant chain protein peptide) from HLA-DR (DR) molecules and thereby facilitates loading with antigenic peptides. Some observations have led to the suggestion that DM acts in a catalytic manner, but so far direct proof is missing. Here, we investigated in vitro the kinetics of exchange of endogenously bound CLIP for various peptides on DR1 and DR2a molecules: we found that in the presence of DM the peptide loading process follows Michaelis-Menten kinetics with turnover numbers of 3-12 DR molecules per minute per DM molecule, and with KM values of 500-1000 nM. In addition, surface plasmon resonance measurements showed that DM interacts efficiently with DR-CLIP complexes but only weakly with DR-peptide complexes isolated from DM-positive cells. Taken together, our data provide evidence that DM functions as an enzyme-like catalyst of peptide exchange and favors the generation of long-lived DR-peptide complexes that are no longer substrates for DM. | ||
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