ArticleResearch and practice in thrombosis and haemostasis2026
Immunopeptidomics of blood coagulation factor IX: a core peptide derived from the protease domain is promiscuously presented on HLA-DR.
Article in Research and practice in thrombosis and haemostasis, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Background: Hemophilia B is an X-linked bleeding disorder that results in a qualitative or quantitative factor IX (FIX) deficiency. A subset of hemophilia B patients treated with FIX replacement therapy develop antibodies against FIX. The development of FIX inhibitors can present as allergic or anaphylactic reactions in some patients. It is currently unknown why a subset of hemophilia B patients develop inhibitors. CD4 Objectives: In this study, we explored MHC class II presentation of FIX-derived peptides by antigen presenting cells. Methods: We incubated purified FIX with monocyte derived dendritic cells of healthy, human leukocyte antigen-typed donors. MHCII peptide complexes were immunopurified, followed by peptide elution and mass spectrometry-based analysis of eluted peptides. Results: We analyzed 12 healthy donors; of them, 8 presented FIX-derived peptides. The majority of FIX peptides were derived from the serine protease domain of FIX. With the exception of 1 donor, all of them presented at least one peptide containing the same core sequence, "NVIRIIPHHN" (residues 295-306 of FIX). Conclusions: Taken together, we identified a promiscuously presented peptide derived from the protease domain of FIX. Based on its frequent presentation in multiple donors, we speculate that this peptide may be recognized by FIX-specific CD4
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