期刊
BIOPHYSICAL JOURNAL
卷 103, 期 2, 页码 L17-L19出版社
CELL PRESS
DOI: 10.1016/j.bpj.2012.06.019
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资金
- Austrian Federal Ministry for Science and Research
- Austrian Science Fund (FWF) [Y250-B10]
- Max Planck Society
- Schrodinger Fellowship program [J3086]
- National Institutes of Health [RO1 AI52211]
- Howard Hughes Medical Institute
- Immunology Frontier Research Center consortium
- Austrian Science Fund (FWF) [Y 250, J 3086] Funding Source: researchfish
- Austrian Science Fund (FWF) [J3086] Funding Source: Austrian Science Fund (FWF)
The binding of peptide-loaded major histocompatibility complex (pMHC) to the T cell receptor (TCR) represents the central step in T cell antigen recognition. It proceeds in the cell contact area between a T cell and an antigen-presenting cell termed the immunological synapse. An important and unresolved issue is how T cells discriminate between potentially harmful and harmless antigens. One limitation has been the difficulty to measure interaction parameters directly, that is, as they occur in the immunological synapse. Here we present a single-molecule approach to determine pMHC-TCR interaction kinetics in situ based on diffusion analysis of dye-labeled pMHC. We find synaptic off-rates >10-fold accelerated when compared to the dissociation of purified proteins measured in vitro.
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