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Recognition of host Clr-b by the inhibitory NKR-P1B receptor provides a basis for missing-self recognition

Author

Listed:
  • Gautham R. Balaji

    (Monash University
    Monash University)

  • Oscar A. Aguilar

    (University of Toronto
    Sunnybrook Research Institute
    University of California
    University of California)

  • Miho Tanaka

    (University of Toronto
    Sunnybrook Research Institute)

  • Miguel A. Shingu-Vazquez

    (Monash University
    Monash University)

  • Zhihui Fu

    (Monash University
    Monash University)

  • Benjamin S. Gully

    (Monash University
    Monash University)

  • Lewis L. Lanier

    (University of California
    University of California)

  • James R. Carlyle

    (University of Toronto
    Sunnybrook Research Institute)

  • Jamie Rossjohn

    (Monash University
    Monash University
    Cardiff University School of Medicine, Heath Park)

  • Richard Berry

    (Monash University
    Monash University)

Abstract

The interaction between natural killer (NK) cell inhibitory receptors and their cognate ligands constitutes a key mechanism by which healthy tissues are protected from NK cell-mediated lysis. However, self-ligand recognition remains poorly understood within the prototypical NKR-P1 receptor family. Here we report the structure of the inhibitory NKR-P1B receptor bound to its cognate host ligand, Clr-b. NKR-P1B and Clr-b interact via a head-to-head docking mode through an interface that includes a large array of polar interactions. NKR-P1B:Clr-b recognition is extremely sensitive to mutations at the heterodimeric interface, with most mutations severely impacting both Clr-b binding and NKR-P1B receptor function to implicate a low affinity interaction. Within the structure, two NKR-P1B:Clr-b complexes are cross-linked by a non-classic NKR-P1B homodimer, and the disruption of homodimer formation abrogates Clr-b recognition. These data provide an insight into a fundamental missing-self recognition system and suggest an avidity-based mechanism underpins NKR-P1B receptor function.

Suggested Citation

  • Gautham R. Balaji & Oscar A. Aguilar & Miho Tanaka & Miguel A. Shingu-Vazquez & Zhihui Fu & Benjamin S. Gully & Lewis L. Lanier & James R. Carlyle & Jamie Rossjohn & Richard Berry, 2018. "Recognition of host Clr-b by the inhibitory NKR-P1B receptor provides a basis for missing-self recognition," Nature Communications, Nature, vol. 9(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-06989-2
    DOI: 10.1038/s41467-018-06989-2
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    Cited by:

    1. Jan Bláha & Tereza Skálová & Barbora Kalousková & Ondřej Skořepa & Denis Cmunt & Valéria Grobárová & Samuel Pazicky & Edita Poláchová & Celeste Abreu & Jan Stránský & Tomáš Kovaľ & Jarmila Dušková & Y, 2022. "Structure of the human NK cell NKR-P1:LLT1 receptor:ligand complex reveals clustering in the immune synapse," Nature Communications, Nature, vol. 13(1), pages 1-18, December.
    2. Michal Scur & Ahmad Bakur Mahmoud & Sayanti Dey & Farah Abdalbarri & Iona Stylianides & Daniel Medina-Luna & Gayani S. Gamage & Aaron Woblistin & Alexa N. M. Wilson & Haggag S. Zein & Ashley Stueck & , 2022. "Alveolar macrophage metabolic programming via a C-type lectin receptor protects against lipo-toxicity and cell death," Nature Communications, Nature, vol. 13(1), pages 1-20, December.

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