Authors
Olivia Jacobs, Tanja Menche, Cindy Höper, Frédéric Gerhards, Ivica Fucek, Fulvia Vascotto, Marina S Dietz, Mike Heilemann, Robert Tampé
Published in
Proceedings of the National Academy of Sciences of the United States of America. Volume 123. Issue 35. Pages e2615838123. Epub Aug 25, 2026.
Abstract
Major histocompatibility complex class I (MHC I) molecules present antigenic peptides to cytotoxic T cells, a process central to immune surveillance. However, the nanoscale spatial organization of peptide-MHC I (pMHC I) on human dendritic cells (DCs), key initiators of cytotoxic T cell responses, remains largely unexplored. Here, we combine high-affinity soluble T cell receptors with DNA-based point accumulation for imaging in nanoscale topography (DNA-PAINT) to quantitatively map and count defined pMHC I complexes at single-molecule resolution on HLA-A*02:01-expressing cells and primary human monocyte-derived DCs. We found no evidence for higher-order pMHC I nanoclusters under conditions of extracellular peptide exchange or physiological intracellular loading. Instead, detected signals correspond to individual pMHC I complexes. Notably, DC differentiation and activation modulate pMHC I surface abundance and spatial compartmentalization. These findings refine current models of antigen presentation by emphasizing regulation through surface density and spatial distribution, and establish a quantitative framework for epitope-specific, single-molecule quantification of antigen presentation in human immune cells.
PMID:
42640805
Bibliographic data and abstract were imported from PubMed on 26 Aug 2026.
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