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  1. Article ; Online: Structure of the murine CD94-NKG2A receptor in complex with Qa-1

    MacLachlan, Bruce J / Sullivan, Lucy C / Brooks, Andrew G / Rossjohn, Jamie / Vivian, Julian P

    The FEBS journal

    2024  Volume 291, Issue 7, Page(s) 1530–1544

    Abstract: The heterodimeric natural killer cells antigen CD94 (CD94)-NKG2-A/NKG2-B type II integral membrane protein (NKG2A) receptor family expressed on human and mouse natural killer (NK) cells monitors global major histocompatibility complex (MHC) class I cell ... ...

    Abstract The heterodimeric natural killer cells antigen CD94 (CD94)-NKG2-A/NKG2-B type II integral membrane protein (NKG2A) receptor family expressed on human and mouse natural killer (NK) cells monitors global major histocompatibility complex (MHC) class I cell surface expression levels through binding to MHC class Ia-derived leader sequence peptides presented by HLA class I histocompatibility antigen, alpha chain E (HLA-E; in humans) or H-2 class I histocompatibility antigen, D-37 (Qa-1
    MeSH term(s) Animals ; Humans ; Mice ; Histocompatibility Antigens Class I/genetics ; Histocompatibility Antigens Class I/metabolism ; HLA Antigens/genetics ; HLA Antigens/metabolism ; HLA-E Antigens ; Killer Cells, Natural ; NK Cell Lectin-Like Receptor Subfamily C/genetics ; NK Cell Lectin-Like Receptor Subfamily C/metabolism ; NK Cell Lectin-Like Receptor Subfamily D/genetics ; NK Cell Lectin-Like Receptor Subfamily D/chemistry ; Peptides/metabolism ; Protein Sorting Signals ; Receptors, Natural Killer Cell/metabolism
    Chemical Substances Histocompatibility Antigens Class I ; HLA Antigens ; HLA-E Antigens ; NK Cell Lectin-Like Receptor Subfamily C ; NK Cell Lectin-Like Receptor Subfamily D ; Peptides ; Protein Sorting Signals ; Receptors, Natural Killer Cell
    Language English
    Publishing date 2024-01-10
    Publishing country England
    Document type Journal Article
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/febs.17050
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Production of Recombinant Killer Immunoglobulin-Like Receptors for Crystallography and Luminex-Based Assays.

    Pymm, Phillip / Vivian, Julian P

    Methods in molecular biology (Clifton, N.J.)

    2017  Volume 1725, Page(s) 281–299

    Abstract: The killer immunoglobulin-like receptors (KIR) are a highly diverse family of cell-surface receptors that are of importance to the effector function of Natural Killer cells. KIR have been implicated in the detection and clearance of malignantly ... ...

    Abstract The killer immunoglobulin-like receptors (KIR) are a highly diverse family of cell-surface receptors that are of importance to the effector function of Natural Killer cells. KIR have been implicated in the detection and clearance of malignantly transformed cells and in the immune-control of viruses including HIV, HCV and CMV. Recently, the mismatching of donor and recipient KIR has been demonstrated to improve success of hematopoietic stem cell transplantation treatments of leukemias. Due to the high degree of diversity amongst the KIR, a number of strategies are required for the production of recombinant protein for medical, biochemical and structural applications. Each of these strategies has advantages and limitations and is suitable for different subsets of the KIR and their intended use. Here we describe the preparation of these proteins for crystallography and the novel adaptation of tetramer production for this protein family that is suitable for a number of assays including single-antigen bead binding by Luminex. These methods are intended to provide comprehensive details for the production and characterization of each KIR and to be broadly applicable to other cell surface receptors of the immune system.
    MeSH term(s) Animals ; Baculoviridae/genetics ; Baculoviridae/metabolism ; Biological Assay ; Cells, Cultured ; Crystallography, X-Ray ; HEK293 Cells ; Histocompatibility Antigens Class I ; Humans ; Luminescent Measurements ; Receptors, KIR/genetics ; Receptors, KIR/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Sf9 Cells
    Chemical Substances Histocompatibility Antigens Class I ; Receptors, KIR ; Recombinant Proteins
    Language English
    Publishing date 2017-12-28
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-7568-6_22
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Structural integrity with functional plasticity: what type I IFN receptor polymorphisms reveal.

    de Weerd, Nicole A / Vivian, Julian P / Lim, San S / Huang, Stephanie U-Shane / Hertzog, Paul J

    Journal of leukocyte biology

    2021  Volume 108, Issue 3, Page(s) 909–924

    Abstract: The type I IFNs activate an array of signaling pathways, which are initiated after IFNs bind their cognate receptors, IFNα/β receptor (IFNAR)1 and IFNAR2. These signals contribute to many aspects of human health including defense against pathogens, ... ...

    Abstract The type I IFNs activate an array of signaling pathways, which are initiated after IFNs bind their cognate receptors, IFNα/β receptor (IFNAR)1 and IFNAR2. These signals contribute to many aspects of human health including defense against pathogens, cancer immunosurveillance, and regulation of inflammation. How these cytokines interact with their receptors influences the quality of these signals. As such, the integrity of receptor structure is pivotal to maintaining human health and the response to immune stimuli. This review brings together genome wide association studies and clinical reports describing the association of nonsynonymous IFNAR1 and IFNAR2 polymorphisms with clinical disease, including altered susceptibility to viral and bacterial pathogens, autoimmune diseases, cancer, and adverse reactions to live-attenuated vaccines. We describe the amino acid substitutions or truncations induced by these polymorphisms and, using the knowledge of IFNAR conformational changes, IFNAR-IFN interfaces and overall structure-function relationship of the signaling complexes, we hypothesize the effect of these polymorphisms on receptor structure. That these predicted changes to IFNAR structure are associated with clinical manifestations of human disease, highlights the importance of IFNAR structural integrity to maintaining functional quality of these receptor-mediated responses. Type I IFNs are pivotal to innate immune responses and ultimately, to human health. Understanding the consequences of altered structure on the actions of these clinically significant cell receptors provides important information on the roles of IFNARs in health and disease.
    MeSH term(s) Alternative Splicing ; Amino Acid Sequence ; Animals ; Codon, Nonsense/genetics ; Crystallography, X-Ray ; Disease Susceptibility ; Humans ; Immunity, Innate ; Immunogenicity, Vaccine ; Ligands ; Macrophages/immunology ; Mammals/genetics ; Mice ; Models, Molecular ; Polymorphism, Single Nucleotide ; Protein Binding ; Protein Conformation ; Protein Domains ; Receptor, Interferon alpha-beta/chemistry ; Receptor, Interferon alpha-beta/genetics ; Receptor, Interferon alpha-beta/physiology ; Sequence Alignment ; Sequence Homology, Amino Acid ; Signal Transduction ; Structure-Activity Relationship ; Tuberculosis/immunology
    Chemical Substances Codon, Nonsense ; Ligands ; Receptor, Interferon alpha-beta (156986-95-7)
    Language English
    Publishing date 2021-01-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 605722-6
    ISSN 1938-3673 ; 0741-5400
    ISSN (online) 1938-3673
    ISSN 0741-5400
    DOI 10.1002/JLB.2MR0420-152R
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: A pocket guide on how to structure SARS-CoV-2 drugs and therapies.

    Littler, Dene R / MacLachlan, Bruce J / Watson, Gabrielle M / Vivian, Julian P / Gully, Benjamin S

    Biochemical Society transactions

    2020  Volume 48, Issue 6, Page(s) 2625–2641

    Abstract: The race to identify a successful treatment for COVID19 will be defined by fundamental research into the replication cycle of the SARS-CoV-2 virus. This has identified five distinct stages from which numerous vaccination and clinical trials have emerged ... ...

    Abstract The race to identify a successful treatment for COVID19 will be defined by fundamental research into the replication cycle of the SARS-CoV-2 virus. This has identified five distinct stages from which numerous vaccination and clinical trials have emerged alongside an innumerable number of drug discovery studies currently in development for disease intervention. Informing every step of the viral replication cycle has been an unprecedented 'call-to-arms' by the global structural biology community. Of the 20 main SARS-CoV-2 proteins, 13 have been resolved structurally for SARS-CoV-2 with most having a related SARS-CoV and MERS-CoV structural homologue totalling some 300 structures currently available in public repositories. Herein, we review the contribution of structural studies to our understanding of the virus and their role in structure-based development of therapeutics.
    MeSH term(s) Antiviral Agents/chemical synthesis ; Antiviral Agents/chemistry ; Antiviral Agents/therapeutic use ; COVID-19/immunology ; COVID-19/therapy ; Drug Development/methods ; Drug Discovery/methods ; Genome, Viral ; Humans ; Models, Molecular ; Protein Structural Elements ; SARS-CoV-2/chemistry ; SARS-CoV-2/drug effects ; SARS-CoV-2/immunology ; SARS-CoV-2/physiology ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/physiology ; Structure-Activity Relationship ; Viral Structural Proteins/chemistry ; Viral Structural Proteins/physiology ; Virus Replication/drug effects ; Virus Replication/physiology ; COVID-19 Drug Treatment
    Chemical Substances Antiviral Agents ; Spike Glycoprotein, Coronavirus ; Viral Structural Proteins ; spike protein, SARS-CoV-2
    Language English
    Publishing date 2020-11-30
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 184237-7
    ISSN 1470-8752 ; 0300-5127
    ISSN (online) 1470-8752
    ISSN 0300-5127
    DOI 10.1042/BST20200396
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Engineering Cell Lines for Specific Human Leukocyte Antigen Presentation.

    Jin, Dongbin / Loh, Khai Lee / Shamekhi, Tima / Ting, Yi Tian / Lim Kam Sian, Terry C C / Roest, James / Ooi, Joshua D / Vivian, Julian P / Faridi, Pouya

    Methods in molecular biology (Clifton, N.J.)

    2023  Volume 2691, Page(s) 351–369

    Abstract: Epitope-specific immunotherapies have enabled the targeted treatment of a variety of diseases, ranging from cancer, infection, and autoimmune disorders. For ... ...

    Abstract Epitope-specific immunotherapies have enabled the targeted treatment of a variety of diseases, ranging from cancer, infection, and autoimmune disorders. For CD8
    MeSH term(s) Humans ; Antigens, Neoplasm ; Histocompatibility Antigens Class I/genetics ; HLA Antigens/genetics ; Histocompatibility Antigens Class II ; Cell Line, Tumor ; Epitopes, T-Lymphocyte ; Antigen Presentation
    Chemical Substances Antigens, Neoplasm ; Histocompatibility Antigens Class I ; HLA Antigens ; Histocompatibility Antigens Class II ; Epitopes, T-Lymphocyte
    Language English
    Publishing date 2023-06-24
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-3331-1_25
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Complimentary electrostatics dominate T-cell receptor binding to a psoriasis-associated peptide antigen presented by human leukocyte antigen C∗06:02.

    Anand, Sushma / Littler, Dene R / Mobbs, Jesse I / Braun, Asolina / Baker, Daniel G / Tennant, Luke / Purcell, Anthony W / Vivian, Julian P / Rossjohn, Jamie

    The Journal of biological chemistry

    2023  Volume 299, Issue 7, Page(s) 104930

    Abstract: Psoriasis is a chronic skin disease characterized by hyperproliferative epidermal lesions infiltrated by autoreactive T cells. Individuals expressing the human leukocyte antigen (HLA) C∗06:02 allele are at highest risk for developing psoriasis. An ... ...

    Abstract Psoriasis is a chronic skin disease characterized by hyperproliferative epidermal lesions infiltrated by autoreactive T cells. Individuals expressing the human leukocyte antigen (HLA) C∗06:02 allele are at highest risk for developing psoriasis. An autoreactive T cell clone (termed Vα3S1/Vβ13S1) isolated from psoriatic plaques is selective for HLA-C∗06:02, presenting a peptide derived from the melanocyte-specific autoantigen ADAMTSL5 (VRSRRCLRL). Here we determine the crystal structure of this psoriatic TCR-HLA-C∗06:02 ADAMTSL5 complex with a stabilized peptide. Docking of the TCR involves an extensive complementary charge network formed between negatively charged TCR residues interleaving with exposed arginine residues from the self-peptide and the HLA-C∗06:02 α1 helix. We probed these interactions through mutagenesis and activation assays. The charged interface spans the polymorphic region of the C1/C2 HLA group. Notably the peptide-binding groove of HLA-C∗06:02 appears exquisitely suited for presenting highly charged Arg-rich epitopes recognized by this acidic psoriatic TCR. Overall, we provide a structural basis for understanding the engagement of melanocyte antigen-presenting cells by a TCR implicated in psoriasis while simultaneously expanding our knowledge of how TCRs engage HLA-C.
    MeSH term(s) Humans ; HLA-C Antigens ; Static Electricity ; Peptides/chemistry ; Psoriasis/pathology ; Receptors, Antigen, T-Cell/genetics ; ADAMTS Proteins
    Chemical Substances HLA-C Antigens ; Peptides ; Receptors, Antigen, T-Cell ; ADAMTSL5 protein, human (EC 3.4.24.-) ; ADAMTS Proteins (EC 3.4.24.-)
    Language English
    Publishing date 2023-06-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2023.104930
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Characterization of Monoclonal Antibodies to Measure Cell Surface Protein Levels of Human Interferon-Lambda Receptor 1.

    de Weerd, Nicole A / Ogungbola, Olamide / Liu, Xinyun / Matthews, Antony Y / Ismail, Amina / Vivian, Julian P / Lim, San S / Tyrrell, D Lorne / Putcha, Niru / Skawinski, Mike / Dickensheets, Harold / Lavoie, Thomas B / Donnelly, Raymond P / Hertzog, Paul J / Santer, Deanna M

    Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research

    2023  Volume 43, Issue 9, Page(s) 403–413

    Abstract: Type III interferons (IFN-lambdas, IFN-λs) are important antiviral cytokines that can also modulate immune responses by acting through a heterodimeric receptor composed of the specific and limited expressed IFN-λR1 chain and the ubiquitous IL-10R2 chain, ...

    Abstract Type III interferons (IFN-lambdas, IFN-λs) are important antiviral cytokines that can also modulate immune responses by acting through a heterodimeric receptor composed of the specific and limited expressed IFN-λR1 chain and the ubiquitous IL-10R2 chain, which is shared with IL-10 family cytokines. Conflicting data have been reported regarding which cells express the IFN-λR1 subunit and directly respond to IFN-λs. This is, in part, owing to transcript levels of the IFN-λR1 gene,
    MeSH term(s) Humans ; Interferons ; Receptors, Interferon/genetics ; Interferon Lambda ; Membrane Proteins ; Antibodies, Monoclonal ; Cytokines
    Chemical Substances Interferons (9008-11-1) ; Receptors, Interferon ; Interferon Lambda ; Membrane Proteins ; Antibodies, Monoclonal ; Cytokines
    Language English
    Publishing date 2023-07-27
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1226675-9
    ISSN 1557-7465 ; 1079-9907
    ISSN (online) 1557-7465
    ISSN 1079-9907
    DOI 10.1089/jir.2023.0040
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Reply.

    Brooks, Andrew J / Ishikawa, Mayumi / Fernández-Rojo, Manuel A / Vivian, Julian P / Rossjohn, Jamie / Waters, Michael J

    Hepatology (Baltimore, Md.)

    2020  Volume 73, Issue 3, Page(s) 1239

    Language English
    Publishing date 2020-08-25
    Publishing country United States
    Document type Letter ; Comment
    ZDB-ID 604603-4
    ISSN 1527-3350 ; 0270-9139
    ISSN (online) 1527-3350
    ISSN 0270-9139
    DOI 10.1002/hep.31531
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Carbamazepine Induces Focused T Cell Responses in Resolved Stevens-Johnson Syndrome and Toxic Epidermal Necrolysis Cases But Does Not Perturb the Immunopeptidome for T Cell Recognition.

    Mifsud, Nicole A / Illing, Patricia T / Lai, Jeffrey W / Fettke, Heidi / Hensen, Luca / Huang, Ziyi / Rossjohn, Jamie / Vivian, Julian P / Kwan, Patrick / Purcell, Anthony W

    Frontiers in immunology

    2021  Volume 12, Page(s) 653710

    Abstract: Antiseizure medications (ASMs) are frequently implicated in T cell-mediated drug hypersensitivity reactions and cause skin tropic pathologies that range in severity from mild rashes to life-threatening systemic syndromes. During the acute stages of the ... ...

    Abstract Antiseizure medications (ASMs) are frequently implicated in T cell-mediated drug hypersensitivity reactions and cause skin tropic pathologies that range in severity from mild rashes to life-threatening systemic syndromes. During the acute stages of the more severe manifestations of these reactions, drug responsive proinflammatory CD8
    MeSH term(s) Anticonvulsants/adverse effects ; CD8-Positive T-Lymphocytes/drug effects ; CD8-Positive T-Lymphocytes/immunology ; CD8-Positive T-Lymphocytes/metabolism ; Carbamazepine/adverse effects ; Case-Control Studies ; Cell Line, Tumor ; Clonal Selection, Antigen-Mediated/drug effects ; Clonal Selection, Antigen-Mediated/genetics ; Female ; HLA-B15 Antigen/analysis ; HLA-B15 Antigen/metabolism ; Healthy Volunteers ; Humans ; Immunologic Memory/drug effects ; Male ; Peptides/analysis ; Peptides/metabolism ; Primary Cell Culture ; Proteomics ; Receptors, Antigen, T-Cell/genetics ; Receptors, Antigen, T-Cell/metabolism ; Stevens-Johnson Syndrome/blood ; Stevens-Johnson Syndrome/immunology
    Chemical Substances Anticonvulsants ; HLA-B*15:02 antigen ; HLA-B15 Antigen ; Peptides ; Receptors, Antigen, T-Cell ; Carbamazepine (33CM23913M)
    Language English
    Publishing date 2021-04-12
    Publishing country Switzerland
    Document type Journal Article ; Observational Study ; Research Support, Non-U.S. Gov't
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2021.653710
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: The Role of the HLA Class I α2 Helix in Determining Ligand Hierarchy for the Killer Cell Ig-like Receptor 3DL1.

    Saunders, Philippa M / MacLachlan, Bruce J / Widjaja, Jacqueline / Wong, Shu Cheng / Oates, Clare V L / Rossjohn, Jamie / Vivian, Julian P / Brooks, Andrew G

    Journal of immunology (Baltimore, Md. : 1950)

    2021  Volume 206, Issue 4, Page(s) 849–860

    Abstract: HLA class I molecules that represent ligands for the inhibitory killer cell Ig-like receptor (KIR) 3DL1 found on NK cells are categorically defined as those HLA-A and HLA-B allotypes containing the Bw4 motif, yet KIR3DL1 demonstrates hierarchical ... ...

    Abstract HLA class I molecules that represent ligands for the inhibitory killer cell Ig-like receptor (KIR) 3DL1 found on NK cells are categorically defined as those HLA-A and HLA-B allotypes containing the Bw4 motif, yet KIR3DL1 demonstrates hierarchical recognition of these HLA-Bw4 ligands. To better understand the molecular basis underpinning differential KIR3DL1 recognition, the HLA-A
    MeSH term(s) HLA-A Antigens/chemistry ; HLA-A Antigens/immunology ; Humans ; Killer Cells, Natural/chemistry ; Killer Cells, Natural/immunology ; Protein Conformation, alpha-Helical ; Protein Domains ; Receptors, KIR3DL1/chemistry ; Receptors, KIR3DL1/immunology
    Chemical Substances HLA-A Antigens ; HLA-A*32 antigen ; KIR3DL1 protein, human ; Receptors, KIR3DL1
    Language English
    Publishing date 2021-01-13
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 3056-9
    ISSN 1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
    ISSN (online) 1550-6606
    ISSN 0022-1767 ; 1048-3233 ; 1047-7381
    DOI 10.4049/jimmunol.2001109
    Database MEDical Literature Analysis and Retrieval System OnLINE

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