ArticleInternational journal of molecular sciences2022
BST2, a Novel Inhibitory Receptor, Is Involved in NK Cell Cytotoxicity through Its Cytoplasmic Tail Domain.
Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 9 citations in OpenAlex.
- Bone Marrow Stromal Cell Antigen 2 Promotes Esophageal Squamous Cell Carcinoma Progression by Mediating the Cell-Cell Interaction between Cancer Cells and Cancer-Associated Fibroblasts.The American journal of pathology · 2026Article
- CD317 stabilizes TNFR1 and confers the anti-inflammatory functions of MSCs via NF-κB/TSG6 pathway.Stem cell research & therapy · 2025Article
- Machine learning-driven identification of exosome- related biomarkers in head and neck squamous cell carcinoma.Frontiers in immunology · 2025Article
- Lentinan enhances CAR-T cell potency in solid tumors by optimizing T cell differentiation.Frontiers in immunology · 2025Article
- The Role of Bone Marrow Stromal Cell Antigen 2 (BST2) in the Migration of Dendritic Cells to Lymph Nodes.International journal of molecular sciences · 2024Article
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
Bone Marrow Stromal Cell Antigen 2 (BST2) is a type II transmembrane protein expressed on various cell types that tethers the release of viruses. Natural killer (NK) cells express low levels of BST2 under normal conditions but exhibit increased expression of BST2 upon activation. In this study, we show for the first time that murine BST2 can control the cytotoxicity of NK cells. The cytoplasmic tail of murine BST2 contains an immunoreceptor tyrosine-based inhibitory motif (ITIM). The absence of BST2 on NK cells can enhance their cytotoxicity against tumor cells compared to wild type NK cells. NK cells isolated from NZW mice, which express ITIM-deficient BST2, also showed higher cytotoxicity than wild type NK cells. In addition, we found that galectin-8 and galectin-9 were ligands of BST2, since blocking galectin-8 or -9 with monoclonal antibodies enhanced the cytotoxicity of NK cells. These results suggested that BST2 might be a novel NK cell inhibitory receptor as it was involved in regulating NK cell cytotoxicity through its interaction with galectins.
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