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  1. Article ; Online: The B7:CD28 family and friends: Unraveling coinhibitory interactions.

    Burke, Kelly P / Chaudhri, Apoorvi / Freeman, Gordon J / Sharpe, Arlene H

    Immunity

    2024  Volume 57, Issue 2, Page(s) 223–244

    Abstract: Immune responses must be tightly regulated to ensure both optimal protective immunity and tolerance. Costimulatory pathways within the B7:CD28 family provide essential signals for optimal T cell activation and clonal expansion. They provide crucial ... ...

    Abstract Immune responses must be tightly regulated to ensure both optimal protective immunity and tolerance. Costimulatory pathways within the B7:CD28 family provide essential signals for optimal T cell activation and clonal expansion. They provide crucial inhibitory signals that maintain immune homeostasis, control resolution of inflammation, regulate host defense, and promote tolerance to prevent autoimmunity. Tumors and chronic pathogens can exploit these pathways to evade eradication by the immune system. Advances in understanding B7:CD28 pathways have ushered in a new era of immunotherapy with effective drugs to treat cancer, autoimmune diseases, infectious diseases, and transplant rejection. Here, we discuss current understanding of the mechanisms underlying the coinhibitory functions of CTLA-4, PD-1, PD-L1:B7-1 and PD-L2:RGMb interactions and less studied B7 family members, including HHLA2, VISTA, BTNL2, and BTN3A1, as well as their overlapping and unique roles in regulating immune responses, and the therapeutic potential of these insights.
    MeSH term(s) Humans ; CD28 Antigens/metabolism ; Friends ; T-Lymphocytes ; CTLA-4 Antigen/metabolism ; Immunotherapy ; Autoimmune Diseases ; B7-1 Antigen/metabolism ; Immunoglobulins/metabolism ; Butyrophilins/metabolism ; Antigens, CD/metabolism
    Chemical Substances CD28 Antigens ; CTLA-4 Antigen ; B7-1 Antigen ; HHLA2 protein, human ; Immunoglobulins ; BTNL2 protein, human ; Butyrophilins ; BTN3A1 protein, human ; Antigens, CD
    Language English
    Publishing date 2024-02-12
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 1217235-2
    ISSN 1097-4180 ; 1074-7613
    ISSN (online) 1097-4180
    ISSN 1074-7613
    DOI 10.1016/j.immuni.2024.01.013
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 4227: Show issues Location:
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  2. Article ; Online: Novel Antimurine Thyroid-Stimulating Hormone Receptor Monoclonal Antibodies.

    Klee, Alyssa N / Torchia, James A / Freeman, Gordon J

    Monoclonal antibodies in immunodiagnosis and immunotherapy

    2023  Volume 42, Issue 3, Page(s) 109–114

    Abstract: Autoantibodies against thyroid proteins are present in several thyroid diseases. Thyroid-stimulating hormone receptor (TSHR) is a G-protein-coupled receptor (GPCR) that binds to thyroid-stimulating hormone (TSH) and stimulates production of thyroxine (T4) ...

    Abstract Autoantibodies against thyroid proteins are present in several thyroid diseases. Thyroid-stimulating hormone receptor (TSHR) is a G-protein-coupled receptor (GPCR) that binds to thyroid-stimulating hormone (TSH) and stimulates production of thyroxine (T4) and triiodothyronine (T3). When agonized by anti-TSHR autoantibodies, aberrant production of thyroid hormone can lead to Graves' Disease (GD). In Hashimoto's thyroiditis (HT), anti-TSHR autoantibodies target the thyroid for immune attack. To better understand the role of anti-TSHR antibodies in thyroid disease, we generated a set of rat antimouse (m)TSHR monoclonal antibodies with a range of affinities, blocking of TSH, and agonist activity. These antibodies could be used to investigate the etiology and therapy of thyroid disease in mouse models and as building blocks in protein therapeutics that target the thyroid for treatment in either HT or GD.
    MeSH term(s) Mice ; Rats ; Animals ; Antibodies, Monoclonal ; Graves Disease/drug therapy ; Graves Disease/etiology ; Receptors, Thyrotropin/metabolism ; Hashimoto Disease/complications ; Autoantibodies ; Thyrotropin
    Chemical Substances Antibodies, Monoclonal ; Receptors, Thyrotropin ; Autoantibodies ; Thyrotropin (9002-71-5)
    Language English
    Publishing date 2023-06-01
    Publishing country United States
    Document type Journal Article
    ISSN 2167-9436
    ISSN (online) 2167-9436
    DOI 10.1089/mab.2022.0037
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: A Comparison of Murine PD-1 and PD-L1 Monoclonal Antibodies.

    Bu, Melissa T / Yuan, Long / Klee, Alyssa N / Freeman, Gordon J

    Monoclonal antibodies in immunodiagnosis and immunotherapy

    2022  Volume 41, Issue 4, Page(s) 202–209

    Abstract: Blockade of the PD-L1/PD-1 pathway has proven to be a broadly effective cancer immunotherapy. FDA-approved therapeutic monoclonal antibodies (mAbs) targeting the pathway have high affinity, blocking capacity, and low antibody effector activity. A number ... ...

    Abstract Blockade of the PD-L1/PD-1 pathway has proven to be a broadly effective cancer immunotherapy. FDA-approved therapeutic monoclonal antibodies (mAbs) targeting the pathway have high affinity, blocking capacity, and low antibody effector activity. A number of rat antimouse mAbs have been used to model cancer immunotherapy in mouse models. We set forth the amino acid sequences of mAbs specific for mouse PD-1 (29F.1A12) and PD-L1 (10F.9G2) and compare their avidities, blocking capacities, biological activities, and epitope recognition with other commonly used mAbs. Further manipulation of these sequences should facilitate better modeling of immunotherapy in mouse models and the generation of novel agents.
    MeSH term(s) Animals ; Antibodies, Monoclonal ; Antineoplastic Agents, Immunological ; B7-H1 Antigen ; Immunotherapy ; Mice ; Neoplasms ; Programmed Cell Death 1 Receptor ; Rats
    Chemical Substances Antibodies, Monoclonal ; Antineoplastic Agents, Immunological ; B7-H1 Antigen ; Programmed Cell Death 1 Receptor
    Language English
    Publishing date 2022-08-04
    Publishing country United States
    Document type Journal Article
    ISSN 2167-9436
    ISSN (online) 2167-9436
    DOI 10.1089/mab.2021.0068
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  4. Article ; Online: Acidity changes immunology: a new VISTA pathway.

    Mahoney, Kathleen M / Freeman, Gordon J

    Nature immunology

    2019  Volume 21, Issue 1, Page(s) 13–16

    MeSH term(s) Animals ; Antibodies, Monoclonal/immunology ; Antibodies, Monoclonal/therapeutic use ; B7 Antigens/immunology ; B7 Antigens/metabolism ; Cell Hypoxia/physiology ; Humans ; Hydrogen-Ion Concentration ; Immunotherapy ; Lymphocyte Activation ; Membrane Glycoproteins/metabolism ; Membrane Proteins ; Mice ; Neoplasms/immunology ; Neoplasms/therapy ; Tumor Microenvironment/physiology
    Chemical Substances Antibodies, Monoclonal ; B7 Antigens ; Membrane Glycoproteins ; Membrane Proteins ; P-selectin ligand protein ; VSIR protein, human
    Language English
    Publishing date 2019-12-10
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2016987-5
    ISSN 1529-2916 ; 1529-2908
    ISSN (online) 1529-2916
    ISSN 1529-2908
    DOI 10.1038/s41590-019-0563-2
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    Zs.A 5294: Show issues Location:
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    Zs.MG 42: Show issues

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  5. Article ; Online: Preclinical models for development of immune-oncology therapies.

    Wang, Yufei / Shelton, Sarah E / Kastrunes, Gabriella / Barbie, David A / Freeman, Gordon J / Marasco, Wayne A

    Immuno-oncology insights

    2022  Volume 3, Issue 8, Page(s) 379–398

    Abstract: Immunotherapy has demonstrated great success in clinical treatment, especially for cancer care. Here we review preclinical models, including cell lines, three dimensional (3D) cultures, and mouse models to support the need for tools enabling the ... ...

    Abstract Immunotherapy has demonstrated great success in clinical treatment, especially for cancer care. Here we review preclinical models, including cell lines, three dimensional (3D) cultures, and mouse models to support the need for tools enabling the development of novel immune-oncology (I-O) therapies. While
    Language English
    Publishing date 2022-09-26
    Publishing country England
    Document type Journal Article
    ISSN 2634-5099
    ISSN (online) 2634-5099
    DOI 10.18609/ioi.2022.41
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  6. Article ; Online: mTORC1 upregulates B7-H3/CD276 to inhibit antitumor T cells and drive tumor immune evasion.

    Liu, Heng-Jia / Du, Heng / Khabibullin, Damir / Zarei, Mahsa / Wei, Kevin / Freeman, Gordon J / Kwiatkowski, David J / Henske, Elizabeth P

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 1214

    Abstract: Identifying the mechanisms underlying the regulation of immune checkpoint molecules and the therapeutic impact of targeting them in cancer is critical. Here we show that high expression of the immune checkpoint B7-H3 (CD276) and high mTORC1 activity ... ...

    Abstract Identifying the mechanisms underlying the regulation of immune checkpoint molecules and the therapeutic impact of targeting them in cancer is critical. Here we show that high expression of the immune checkpoint B7-H3 (CD276) and high mTORC1 activity correlate with immunosuppressive phenotypes and worse clinical outcomes in 11,060 TCGA human tumors. We find that mTORC1 upregulates B7-H3 expression via direct phosphorylation of the transcription factor YY2 by p70 S6 kinase. Inhibition of B7-H3 suppresses mTORC1-hyperactive tumor growth via an immune-mediated mechanism involving increased T-cell activity and IFN-γ responses coupled with increased tumor cell expression of MHC-II. CITE-seq reveals strikingly increased cytotoxic CD38
    MeSH term(s) Humans ; Tumor Escape ; T-Lymphocytes ; Genes, Regulator ; Transcription Factors ; Mechanistic Target of Rapamycin Complex 1 ; B7 Antigens
    Chemical Substances Transcription Factors ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1) ; CD276 protein, human ; B7 Antigens ; YY2 protein, human
    Language English
    Publishing date 2023-03-03
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-36881-7
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  7. Article ; Online: VISTA: A Mediator of Quiescence and a Promising Target in Cancer Immunotherapy.

    Yuan, Long / Tatineni, Jahnavi / Mahoney, Kathleen M / Freeman, Gordon J

    Trends in immunology

    2021  Volume 42, Issue 3, Page(s) 209–227

    Abstract: V-domain Ig suppressor of T cell activation (VISTA) is a B7 family member that maintains T cell and myeloid quiescence and is a promising target for combination cancer immunotherapy. During inflammatory challenges, VISTA activity reprograms macrophages ... ...

    Abstract V-domain Ig suppressor of T cell activation (VISTA) is a B7 family member that maintains T cell and myeloid quiescence and is a promising target for combination cancer immunotherapy. During inflammatory challenges, VISTA activity reprograms macrophages towards reduced production of proinflammatory cytokines and increased production of interleukin (IL)-10 and other anti-inflammatory mediators. The interaction of VISTA with its ligands is regulated by pH, and the acidic pH ~6.0 in the tumor microenvironment (TME) facilitates VISTA binding to P-selectin glycoprotein ligand 1 (PSGL-1). Targeting intratumoral pH might be a way to reduce the immunoinhibitory activity of the VISTA pathway and enhance antitumor immune responses. We review differences among VISTA therapeutics under development as candidate immunotherapies, focusing on VISTA binding partners and the unique structural features of this interaction.
    MeSH term(s) B7 Antigens ; Humans ; Immunotherapy ; Lymphocyte Activation ; Neoplasms/therapy ; T-Lymphocytes ; Tumor Microenvironment
    Chemical Substances B7 Antigens
    Language English
    Publishing date 2021-01-23
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2036831-8
    ISSN 1471-4981 ; 1471-4906
    ISSN (online) 1471-4981
    ISSN 1471-4906
    DOI 10.1016/j.it.2020.12.008
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    Zs.A 1601: Show issues Location:
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    Zs.MG 2: Show issues

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  8. Article ; Online: The importance of exosomal PDL1 in tumour immune evasion.

    Daassi, Dhouha / Mahoney, Kathleen M / Freeman, Gordon J

    Nature reviews. Immunology

    2020  Volume 20, Issue 4, Page(s) 209–215

    Abstract: The interaction of programmed cell death 1 ligand 1 (PDL1) with its receptor programmed cell death 1 (PD1) inhibits T cell responses, and blockade of this interaction has proven to be an effective immunotherapy for several different cancers. PDL1 can be ... ...

    Abstract The interaction of programmed cell death 1 ligand 1 (PDL1) with its receptor programmed cell death 1 (PD1) inhibits T cell responses, and blockade of this interaction has proven to be an effective immunotherapy for several different cancers. PDL1 can be expressed on the surface of tumour cells, immune cells and other cells in the tumour microenvironment but is also found in extracellular forms. Recent studies have explored the importance of different forms of extracellular PDL1, such as on exosomes or as a freely soluble protein, and have shown that PDL1-expressing exosomes can inhibit antitumour immune responses. In patients with melanoma, exosomal PDL1 is also a marker of immune activation early after initiation of therapy with PD1-blocking antibodies and predicts a clinical response to PD1 blockade. In this Progress article, we highlight recent insights into the role of exosomal PDL1 in immune oncology and how it may be useful as a biomarker for the management of cancer or to define a subset of patients who would benefit from therapeutics that block exosome production.
    MeSH term(s) Animals ; B7-H1 Antigen/immunology ; Humans ; Immunotherapy/methods ; Neoplasms/immunology ; Neoplasms/therapy ; T-Lymphocytes/immunology ; Tumor Escape/immunology
    Chemical Substances B7-H1 Antigen ; CD274 protein, human
    Language English
    Publishing date 2020-01-21
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ZDB-ID 2062776-2
    ISSN 1474-1741 ; 1474-1733
    ISSN (online) 1474-1741
    ISSN 1474-1733
    DOI 10.1038/s41577-019-0264-y
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  9. Article ; Online: PRMT1 mediated methylation of cGAS suppresses anti-tumor immunity.

    Liu, Jing / Bu, Xia / Chu, Chen / Dai, Xiaoming / Asara, John M / Sicinski, Piotr / Freeman, Gordon J / Wei, Wenyi

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 2806

    Abstract: Activation of the cGAS/STING innate immunity pathway is essential and effective for anti-tumor immunotherapy. However, it remains largely elusive how tumor-intrinsic cGAS signaling is suppressed to facilitate tumorigenesis by escaping immune surveillance. ...

    Abstract Activation of the cGAS/STING innate immunity pathway is essential and effective for anti-tumor immunotherapy. However, it remains largely elusive how tumor-intrinsic cGAS signaling is suppressed to facilitate tumorigenesis by escaping immune surveillance. Here, we report that the protein arginine methyltransferase, PRMT1, methylates cGAS at the conserved Arg133 residue, which prevents cGAS dimerization and suppresses the cGAS/STING signaling in cancer cells. Notably, genetic or pharmaceutical ablation of PRMT1 leads to activation of cGAS/STING-dependent DNA sensing signaling, and robustly elevates the transcription of type I and II interferon response genes. As such, PRMT1 inhibition elevates tumor-infiltrating lymphocytes in a cGAS-dependent manner, and promotes tumoral PD-L1 expression. Thus, combination therapy of PRMT1 inhibitor with anti-PD-1 antibody augments the anti-tumor therapeutic efficacy in vivo. Our study therefore defines the PRMT1/cGAS/PD-L1 regulatory axis as a critical factor in determining immune surveillance efficacy, which serves as a promising therapeutic target for boosting tumor immunity.
    MeSH term(s) B7-H1 Antigen/genetics ; B7-H1 Antigen/metabolism ; Methylation ; Immunity, Innate/genetics ; Nucleotidyltransferases/metabolism ; Signal Transduction/genetics ; Methyltransferases/metabolism
    Chemical Substances B7-H1 Antigen ; Nucleotidyltransferases (EC 2.7.7.-) ; Methyltransferases (EC 2.1.1.-)
    Language English
    Publishing date 2023-05-17
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-38443-3
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  10. Article ; Online: Publisher Correction: Targeting PD-L2-RGMb overcomes microbiome-related immunotherapy resistance.

    Park, Joon Seok / Gazzaniga, Francesca S / Wu, Meng / Luthens, Amalia K / Gillis, Jacob / Zheng, Wen / LaFleur, Martin W / Johnson, Sarah B / Morad, Golnaz / Park, Elizabeth M / Zhou, Yifan / Watowich, Stephanie S / Wargo, Jennifer A / Freeman, Gordon J / Kasper, Dennis L / Sharpe, Arlene H

    Nature

    2023  Volume 618, Issue 7966, Page(s) E27

    Language English
    Publishing date 2023-05-31
    Publishing country England
    Document type Published Erratum
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/s41586-023-06237-8
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