ArticleJournal of immunology (Baltimore, Md. : 1950)2014
The MHC class II cofactor HLA-DM interacts with Ig in B cells.
Article in Journal of immunology (Baltimore, Md. : 1950), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Article
- Lysosomes and lysosome-related organelles in immune responses.FEBS open bio · 2022Review
- Immunoglobulin somatic hypermutation has clinical impact in DLBCL and potential implications for immune checkpoint blockade and neoantigen-based immunotherapies.Journal for immunotherapy of cancer · 2019Article
- Synergy between B cell receptor/antigen uptake and MHCII peptide editing relies on HLA-DO tuning.Scientific reports · 2019Article
- Structural aspects of chaperone-mediated peptide loading in the MHC-I antigen presentation pathway.Critical reviews in biochemistry and molecular biology · 2019Review
- A Missing Switch in Peptide Exchange for MHC Class II Molecules.Frontiers in immunology · 2019Review
- The immunobiology of ubiquitin-dependent B cell receptor functions.Molecular immunology · 2018Review
- The Other Function: Class II-Restricted Antigen Presentation by B Cells.Frontiers in immunology · 2017Review
- Novel Phospholipid-Protein Conjugates Allow Improved Detection of Antibodies in Patients with Autoimmune Diseases.PloS one · 2016Article
- Antigen-B Cell Receptor Complexes Associate with Intracellular major histocompatibility complex (MHC) Class II Molecules.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
B cells internalize extracellular Ag into endosomes using the Ig component of the BCR. In endosomes, Ag-derived peptides are loaded onto MHC class II proteins. How these pathways intersect remains unclear. We find that HLA-DM (DM), a catalyst for MHC class II peptide loading, coprecipitates with Ig in lysates from human tonsillar B cells and B cell lines. The molecules in the Ig/DM complexes have mature glycans, and the complexes colocalize with endosomal markers in intact cells. A larger fraction of Ig precipitates with DM after BCR crosslinking, implying that complexes can form when DM meets endocytosed Ig. In vitro, in the endosomal pH range, soluble DM directly binds the Ig Fab domain and increases levels of free Ag released from immune complexes. Taken together, these results argue that DM and Ig intersect in the endocytic pathway of B cells with potential functional consequences.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.