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  Monomeric TCRs drive T cell antigen recognition.

Brameshuber, M., Kellner, F., Rossboth, B. K., BK, Ta, H., Alge, K., et al. (2018). Monomeric TCRs drive T cell antigen recognition. Nature Immunology, 19(5), 487-496. doi:10.1038/s41590-018-0092-4.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0001-4409-9 Version Permalink: http://hdl.handle.net/21.11116/0000-0003-3823-7
Genre: Journal Article

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 Creators:
Brameshuber, M., Author
Kellner, F., Author
Rossboth, B. K., Author
BK, Author
Ta, H.1, Author              
Alge, K., Author
Sevcsik, E., Author
Göhring, J., Author
Axmann, M., Author
Baumgart, F., Author
Gascoigne, N. R. J., Author
Davis, S. J., Author
Stockinger, H., Author
Schütz, G. J., Author
Huppa, J. B., Author
Affiliations:
1Department of NanoBiophotonics, MPI for biophysical chemistry, Max Planck Society, ou_578627              

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 Abstract: T cell antigen recognition requires T cell antigen receptors (TCRs) engaging MHC-embedded antigenic peptides (pMHCs) within the contact region of a T cell with its conjugated antigen-presenting cell. Despite micromolar TCR:pMHC affinities, T cells respond to even a single antigenic pMHC, and higher-order TCRs have been postulated to maintain high antigen sensitivity and trigger signaling. We interrogated the stoichiometry of TCRs and their associated CD3 subunits on the surface of living T cells through single-molecule brightness and single-molecule coincidence analysis, photon-antibunching-based fluorescence correlation spectroscopy and Förster resonance energy transfer measurements. We found exclusively monomeric TCR–CD3 complexes driving the recognition of antigenic pMHCs, which underscores the exceptional capacity of single TCR–CD3 complexes to elicit robust intracellular signaling.

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Language(s): eng - English
 Dates: 2018-04-162018-05
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/s41590-018-0092-4
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Title: Nature Immunology
Source Genre: Journal
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Pages: - Volume / Issue: 19 (5) Sequence Number: - Start / End Page: 487 - 496 Identifier: -