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TCR–peptide–MHC interactions in situ show accelerated kinetics and increased affinity

Author

Listed:
  • Johannes B. Huppa

    (Stanford School of Medicine, and)

  • Markus Axmann

    (Institut für Biophysik, Johannes Kepler-Universität, Altenbergerstrasse 69, A-4040 Linz, Austria)

  • Manuel A. Mörtelmaier

    (Stanford School of Medicine, and
    Institut für Biophysik, Johannes Kepler-Universität, Altenbergerstrasse 69, A-4040 Linz, Austria
    Present addresses: Agilent Technologies Austria, Mooslackengasse 17, 1190 Wien, Austria (M.A.M.); Nomis Center for Immunobiology and Microbial Pathogenesis, Waitt Advanced Biophotonics Center, The Salk Institute, 10010 North Torrey Pines Road, La Jolla, California 92037, USA (B.F.L.).)

  • Björn F. Lillemeier

    (Stanford School of Medicine, and
    Present addresses: Agilent Technologies Austria, Mooslackengasse 17, 1190 Wien, Austria (M.A.M.); Nomis Center for Immunobiology and Microbial Pathogenesis, Waitt Advanced Biophotonics Center, The Salk Institute, 10010 North Torrey Pines Road, La Jolla, California 92037, USA (B.F.L.).)

  • Evan W. Newell

    (Stanford School of Medicine, and)

  • Mario Brameshuber

    (Institut für Biophysik, Johannes Kepler-Universität, Altenbergerstrasse 69, A-4040 Linz, Austria)

  • Lawrence O. Klein

    (Stanford School of Medicine, and)

  • Gerhard J. Schütz

    (Institut für Biophysik, Johannes Kepler-Universität, Altenbergerstrasse 69, A-4040 Linz, Austria)

  • Mark M. Davis

    (Stanford School of Medicine, and
    Howard Hughes Medical Institute, Beckman Center B221, 279 Campus Drive, Stanford, California 94305-5323, USA)

Abstract

T-cell interactions The use of a novel FRET-based imaging system provides an in situ view of the kinetics of T-cell receptor (TCR) binding to peptide MHC complexes in their natural environment, the immunological synapse. Previously the mater of how containment in this environment would affect the molecular interactions that drive cell–cell interactions has been a matter of speculation. Now that they have been measured, both expected effects (enhanced association rate due to optimal orientation) and unexpected (a very active cytoskeletal component destabilizing TCR binding) are revealed. This work is of relevance to T-cell immunology and to in cell–cell interactions more generally.

Suggested Citation

  • Johannes B. Huppa & Markus Axmann & Manuel A. Mörtelmaier & Björn F. Lillemeier & Evan W. Newell & Mario Brameshuber & Lawrence O. Klein & Gerhard J. Schütz & Mark M. Davis, 2010. "TCR–peptide–MHC interactions in situ show accelerated kinetics and increased affinity," Nature, Nature, vol. 463(7283), pages 963-967, February.
    • Handle: RePEc:nat:nature:v:463:y:2010:i:7283:d:10.1038_nature08746
    DOI: 10.1038/nature08746
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    Cited by:

    1. Darren B. McAffee & Mark K. O’Dair & Jenny J. Lin & Shalini T. Low-Nam & Kiera B. Wilhelm & Sungi Kim & Shumpei Morita & Jay T. Groves, 2022. "Discrete LAT condensates encode antigen information from single pMHC:TCR binding events," Nature Communications, Nature, vol. 13(1), pages 1-18, December.
    2. Christopher Szeto & Pirooz Zareie & Rushika C. Wirasinha & Justin B. Zhang & Andrea T. Nguyen & Alan Riboldi-Tunnicliffe & Nicole L. Gruta & Stephanie Gras & Stephen R. Daley, 2022. "Covalent TCR-peptide-MHC interactions induce T cell activation and redirect T cell fate in the thymus," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    3. Muaz Nik Rushdi & Victor Pan & Kaitao Li & Hyun-Kyu Choi & Stefano Travaglino & Jinsung Hong & Fletcher Griffitts & Pragati Agnihotri & Roy A. Mariuzza & Yonggang Ke & Cheng Zhu, 2022. "Cooperative binding of T cell receptor and CD4 to peptide-MHC enhances antigen sensitivity," Nature Communications, Nature, vol. 13(1), pages 1-16, December.

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