ArticleProtein science : a publication of the Protein Society2022
Fast peptide exchange on major histocompatibility complex class I molecules by acidic stabilization of a peptide-empty intermediate.
Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 6 citations in OpenAlex.
- Peptide exchange-competent class I MHC molecules produced in eukaryotic cells for rapid production of MHC multimers.Journal of immunology (Baltimore, Md. : 1950) · 2026Article
- Empty MHC Class I Protein Production.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Major histocompatibility complex class I assembly within endolysosomal pathways.Current opinion in immunology · 2023Review
- Fast peptide exchange on major histocompatibility complex class I molecules by acidic stabilization of a peptide-empty intermediate.Protein science : a publication of the Protein Society · 2022Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cell biology and biochemistry of peptide exchange on major histocompatibility complex class I (MHC-I) proteins are of great interest in the study of immunodominance, which requires iterative optimization of peptide affinity, and cross-presentation of pathogen and tumor antigens, in which endogenous peptides are exchanged for exogenous ones. Even though several methods exist to catalyze peptide exchange on recombinant MHC-I proteins, the cellular conditions and mechanisms allowing for peptide exchange in vivo remain unclear. Here, we demonstrate that low pH, as present in endosomes, indeed triggers peptide exchange, and we dissect the individual steps of the exchange reaction. We find that low pH stabilizes the peptide-empty forms of MHC-I that occur as intermediates of the exchange reaction, and that is synergizes with dipeptides and with disulfide-mediated stabilization of MHC-I.
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