IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v463y2010i7283d10.1038_nature08746.html
   My bibliography  Save this article

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
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature08746
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/nature08746?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. 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.
    2. 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.
    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.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:463:y:2010:i:7283:d:10.1038_nature08746. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.