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  1. Article ; Online: Immune evasion by oncogenic proteins of acute myeloid leukemia.

    Elias, Shlomo / Yamin, Rachel / Golomb, Lior / Tsukerman, Pinchas / Stanietsky-Kaynan, Noah / Ben-Yehuda, Dina / Mandelboim, Ofer

    Blood

    2014  Volume 123, Issue 10, Page(s) 1535–1543

    Abstract: PML-RARA and AML1-ETO are important oncogenic fusion proteins that play a central role in transformation to acute myeloid leukemia (AML). Whether these fusion proteins render the tumor cells with immune evasion properties is unknown. Here we show that ... ...

    Abstract PML-RARA and AML1-ETO are important oncogenic fusion proteins that play a central role in transformation to acute myeloid leukemia (AML). Whether these fusion proteins render the tumor cells with immune evasion properties is unknown. Here we show that both oncogenic proteins specifically downregulate the expression of CD48, a ligand of the natural killer (NK) cell activating receptor 2B4, thereby leading to decreased killing by NK cells. We demonstrate that this process is histone deacetylase (HDAC)-dependent, that it is mediated through the downregulation of CD48 messenger RNA, and that treatment with HDAC inhibitors (HDACi) restores the expression of CD48. Furthermore, by using chromatin immunoprecepitation (ChIP) experiments, we show that AML1-ETO directly interacts with CD48. Finally, we show that AML patients who are carrying these specific translocations have low expression of CD48.
    MeSH term(s) Antigens, CD/chemistry ; Antigens, CD/genetics ; Antigens, CD/metabolism ; Base Sequence ; CD48 Antigen ; Cell Line, Tumor ; Core Binding Factor Alpha 2 Subunit/genetics ; Core Binding Factor Alpha 2 Subunit/immunology ; Cytotoxicity, Immunologic ; Gene Expression ; Gene Expression Regulation ; Histone Deacetylases/metabolism ; Humans ; Killer Cells, Natural/immunology ; Killer Cells, Natural/metabolism ; Leukemia, Myeloid, Acute/genetics ; Leukemia, Myeloid, Acute/immunology ; Leukemia, Myeloid, Acute/metabolism ; Molecular Sequence Data ; Oncogene Proteins, Fusion/genetics ; Oncogene Proteins, Fusion/immunology ; Oncogene Proteins, Fusion/metabolism ; RUNX1 Translocation Partner 1 Protein ; Tumor Escape/genetics ; Tumor Escape/immunology
    Chemical Substances AML1-ETO fusion protein, human ; Antigens, CD ; CD48 Antigen ; CD48 protein, human ; Core Binding Factor Alpha 2 Subunit ; Oncogene Proteins, Fusion ; RUNX1 Translocation Partner 1 Protein ; promyelocytic leukemia-retinoic acid receptor alpha fusion oncoprotein ; Histone Deacetylases (EC 3.5.1.98)
    Language English
    Publishing date 2014-01-21
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80069-7
    ISSN 1528-0020 ; 0006-4971
    ISSN (online) 1528-0020
    ISSN 0006-4971
    DOI 10.1182/blood-2013-09-526590
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Binding of the Fap2 protein of Fusobacterium nucleatum to human inhibitory receptor TIGIT protects tumors from immune cell attack.

    Gur, Chamutal / Ibrahim, Yara / Isaacson, Batya / Yamin, Rachel / Abed, Jawad / Gamliel, Moriya / Enk, Jonatan / Bar-On, Yotam / Stanietsky-Kaynan, Noah / Coppenhagen-Glazer, Shunit / Shussman, Noam / Almogy, Gideon / Cuapio, Angelica / Hofer, Erhard / Mevorach, Dror / Tabib, Adi / Ortenberg, Rona / Markel, Gal / Miklić, Karmela /
    Jonjic, Stipan / Brennan, Caitlin A / Garrett, Wendy S / Bachrach, Gilad / Mandelboim, Ofer

    Immunity

    2015  Volume 42, Issue 2, Page(s) 344–355

    Abstract: Bacteria, such as Fusobacterium nucleatum, are present in the tumor microenvironment. However, the immunological consequences of intra-tumoral bacteria remain unclear. Here, we have shown that natural killer (NK) cell killing of various tumors is ... ...

    Abstract Bacteria, such as Fusobacterium nucleatum, are present in the tumor microenvironment. However, the immunological consequences of intra-tumoral bacteria remain unclear. Here, we have shown that natural killer (NK) cell killing of various tumors is inhibited in the presence of various F. nucleatum strains. Our data support that this F. nucleatum-mediated inhibition is mediated by human, but not by mouse TIGIT, an inhibitory receptor present on all human NK cells and on various T cells. Using a library of F. nucleatum mutants, we found that the Fap2 protein of F. nucleatum directly interacted with TIGIT, leading to the inhibition of NK cell cytotoxicity. We have further demonstrated that tumor-infiltrating lymphocytes expressed TIGIT and that T cell activities were also inhibited by F. nucleatum via Fap2. Our results identify a bacterium-dependent, tumor-immune evasion mechanism in which tumors exploit the Fap2 protein of F. nucleatum to inhibit immune cell activity via TIGIT.
    MeSH term(s) Adenocarcinoma/immunology ; Adenocarcinoma/microbiology ; Animals ; Bacterial Outer Membrane Proteins/immunology ; Cell Line ; Cell Proliferation ; Colonic Neoplasms/immunology ; Colonic Neoplasms/microbiology ; Fusobacterium nucleatum/immunology ; Humans ; Killer Cells, Natural/immunology ; Lymphocytes, Tumor-Infiltrating/immunology ; Mice ; Protein Binding ; Receptors, Immunologic/immunology ; Tumor Escape/immunology ; Tumor Microenvironment/immunology
    Chemical Substances Bacterial Outer Membrane Proteins ; Receptors, Immunologic ; TIGIT protein, human
    Language English
    Publishing date 2015-02-10
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1217235-2
    ISSN 1097-4180 ; 1074-7613
    ISSN (online) 1097-4180
    ISSN 1074-7613
    DOI 10.1016/j.immuni.2015.01.010
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.MG 69: Show issues

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