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Recognition of haemagglutinins on virus-infected cells by NKp46 activates lysis by human NK cells

Author

Listed:
  • Ofer Mandelboim

    (The Lautenberg Center for General and Tumor Immunology, The Hebrew University-Hadassha Medical School)

  • Niva Lieberman

    (The Lautenberg Center for General and Tumor Immunology, The Hebrew University-Hadassha Medical School)

  • Marianna Lev

    (Faculty of Health Sciences, and the Cancer Research Center, Ben Gurion University of the Negev)

  • Lada Paul

    (Faculty of Health Sciences, and the Cancer Research Center, Ben Gurion University of the Negev)

  • Tal I. Arnon

    (The Lautenberg Center for General and Tumor Immunology, The Hebrew University-Hadassha Medical School)

  • Yuri Bushkin

    (Laboratory of Molecular Immunology, Public Health Research Institute)

  • Daniel M. Davis

    (Imperial College of Science, Technology and Medicine)

  • Jack L. Strominger

    (Harvard University)

  • Jonathan W. Yewdell

    (Laboratory of Viral Diseases, National Institute of Allergy and Infectious diseases, National Institutes of Health)

  • Angel Porgador

    (Faculty of Health Sciences, and the Cancer Research Center, Ben Gurion University of the Negev)

Abstract

Natural killer (NK) cells destroy virus-infected and tumour cells, apparently without the need for previous antigen stimulation1. In part, target cells are recognized by their diminished expression of major histocompatibility complex (MHC) class I molecules, which normally interact with inhibitory receptors on the NK cell surface2,3,4,5,6,7,8. NK cells also express triggering receptors that are specific for non-MHC ligands; but the nature of the ligands recognized on target cells is undefined9,10,11,12,13,14. NKp46 is thought to be the main activating receptor for human NK cells9,15. Here we show that a soluble NKp46–immunoglobulin fusion protein binds to both the haemagglutinin of influenza virus and the haemagglutinin–neuraminidase of parainfluenza virus. In a substantial subset of NK cells, recognition by NKp46 is required to lyse cells expressing the corresponding viral glycoproteins. The binding requires the sialylation of NKp46 oligosaccharides, which is consistent with the known sialic binding capacity of the viral glycoproteins. These findings indicate how NKp46-expressing NK cells may recognize target cells infected by influenza or parainfluenza without the decreased expression of target-cell MHC class I protein.

Suggested Citation

  • Ofer Mandelboim & Niva Lieberman & Marianna Lev & Lada Paul & Tal I. Arnon & Yuri Bushkin & Daniel M. Davis & Jack L. Strominger & Jonathan W. Yewdell & Angel Porgador, 2001. "Recognition of haemagglutinins on virus-infected cells by NKp46 activates lysis by human NK cells," Nature, Nature, vol. 409(6823), pages 1055-1060, February.
    • Handle: RePEc:nat:nature:v:409:y:2001:i:6823:d:10.1038_35059110
    DOI: 10.1038/35059110
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    Cited by:

    1. Yoav Charpak-Amikam & Tom Lapidus & Batya Isaacson & Alexandra Duev-Cohen & Tal Levinson & Adi Elbaz & Francesca Levi-Schaffer & Nir Osherov & Gilad Bachrach & Lois L. Hoyer & Maya Korem & Ronen Ben-A, 2022. "Candida albicans evades NK cell elimination via binding of Agglutinin-Like Sequence proteins to the checkpoint receptor TIGIT," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    2. Qiong-Fang Zhang & Jian-Ying Shao & Wen-Wei Yin & Yang Xia & Ling Chen & Xing Wang & Huai-Dong Hu & Peng Hu & Hong Ren & Da-Zhi Zhang, 2016. "Altered Immune Profiles of Natural Killer Cells in Chronic Hepatitis B Patients: A Systematic Review and Meta-Analysis," PLOS ONE, Public Library of Science, vol. 11(8), pages 1-16, August.

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