Journal
CELL DISCOVERY
Volume 1, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/celldisc.2015.36
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Funding
- European Research Council under the European Union's Seventh Framework Programme/ERC [320473-BacNK]
- I-CORE Program of the Planning and Budgeting Committee
- Israel Science Foundation
- I-Core on Chromatin and RNA in Gene Regulation
- GIF foundation
- Lewis family foundation
- ICRF
- Helmholtz Israel
- Rosetrees Trust
- ERC [322693]
- European Research Council (ERC) [322693] Funding Source: European Research Council (ERC)
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Natural killer (NK) cells kill tumor and virus-infected cells using activating NK cell receptors. One of the major NK-activating receptors is NKp46 and its mouse ortholog Ncr1. NKp46/Ncr1 is expressed exclusively on NK cells and on a subset of innate lymphoid cells. NKp46/Ncr1 was shown to be involved in a myriad of pathologies and immunological settings. Specifically, NKp46/Ncr1 was shown to interact with the viral hemagglutinin (HA) protein and with an unknown tumor/cellular ligand. NKp46 and Ncr1 are structurally similar; however, they are substantially different in their glycosylation patterns. Although the human NKp46 carries both O- and N-glycosylations that are essential for its activity, the mouse Ncr1 was predicted to have N-linked glycosylations only. Here we discovered using prediction algorithms and high-performance liquid chromatography analysis that Ncr1 carries two putative novel O-glycosylations, one of which (Thr 225) is conserved in NKp46. We next used surface plasmon resonance, biochemical, mutational and functional in vitro and in vivo assays to demonstrate that the putative O-glycosylations of Ncr1 are critical for its function.
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