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000296018 1001_ $$0P:(DE-He78)63f0928851cb60021a60e05e4c196aae$$aGünther, Matthias$$b0$$eFirst author$$udkfz
000296018 245__ $$aAntigen presentation by MHC-II is shaped by competitive and cooperative allosteric mechanisms of peptide exchange.
000296018 260__ $$aCambridge, Mass.$$bCell Press$$c2025
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000296018 500__ $$a#EA:B086#LA:B086# / 2025 Feb 6;33(2):389-400.e13
000296018 520__ $$aMajor histocompatibility complex class II (MHC-II) presents antigens to T helper cells. The spectrum of presented peptides is regulated by the exchange catalyst human leukocyte antigen DM (HLA-DM), which dissociates peptide-MHC-II complexes in the endosome. How susceptible a peptide is to HLA-DM is mechanistically not understood. Here, we present a data-driven mathematical model for the conformational landscape of MHC-II that explains the wide range of measured HLA-DM susceptibilities and predicts why some peptides are largely HLA-DM-resistant. We find that the conformational plasticity of MHC-II mediates both allosteric competition and cooperation between peptide and HLA-DM. Competition causes HLA-DM susceptibility to be proportional to the intrinsic peptide off-rate. Remarkably, diverse MHC-II allotypes with conserved HLA-DM interactions show a universal linear susceptibility function. However, HLA-DM-resistant peptides deviate from this susceptibility function; we predict resistance to be caused by fast peptide association with MHC-II. Thus, our study provides quantitative insight into peptide and MHC-II allotype parameters that shape class-II antigen presentation.
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000296018 650_7 $$2Other$$aHLA-DM
000296018 650_7 $$2Other$$aHLA-DM susceptibility
000296018 650_7 $$2Other$$aMHC class-II
000296018 650_7 $$2Other$$aantigen presentation
000296018 650_7 $$2Other$$aimmunopeptidome prediction
000296018 650_7 $$2Other$$amathematical model
000296018 7001_ $$aSticht, Jana$$b1
000296018 7001_ $$aFreund, Christian$$b2
000296018 7001_ $$0P:(DE-He78)9dbe272aaadbdc810ab0bb291eae428e$$aHöfer, Thomas$$b3$$eLast author$$udkfz
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