LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 3 of total 3

Search options

  1. Article ; Online: The MHC-E peptide ligands for checkpoint CD94/NKG2A are governed by inflammatory signals, whereas LILRB1/2 receptors are peptide indifferent.

    Middelburg, Jim / Ghaffari, Soroush / Schoufour, Tom A W / Sluijter, Marjolein / Schaap, Gaby / Göynük, Büsra / Sala, Benedetta M / Al-Tamimi, Lejla / Scheeren, Ferenc / Franken, Kees L M C / Akkermans, Jimmy J L L / Cabukusta, Birol / Joosten, Simone A / Derksen, Ian / Neefjes, Jacques / van der Burg, Sjoerd H / Achour, Adnane / Wijdeven, Ruud H M / Weidanz, Jon /
    van Hall, Thorbald

    Cell reports

    2023  Volume 42, Issue 12, Page(s) 113516

    Abstract: The immune checkpoint NKG2A/CD94 is a promising target for cancer immunotherapy, and its ligand major histocompatibility complex E (MHC-E) is frequently upregulated in cancer. NKG2A/CD94-mediated inhibition of lymphocytes depends on the presence of ... ...

    Abstract The immune checkpoint NKG2A/CD94 is a promising target for cancer immunotherapy, and its ligand major histocompatibility complex E (MHC-E) is frequently upregulated in cancer. NKG2A/CD94-mediated inhibition of lymphocytes depends on the presence of specific leader peptides in MHC-E, but when and where they are presented in situ is unknown. We apply a nanobody specific for the Qdm/Qa-1
    MeSH term(s) Mice ; Animals ; Histocompatibility Antigens Class I/metabolism ; Leukocyte Immunoglobulin-like Receptor B1/metabolism ; Killer Cells, Natural ; Ligands ; Peptides/metabolism ; Neoplasms/metabolism ; NK Cell Lectin-Like Receptor Subfamily C/metabolism
    Chemical Substances Histocompatibility Antigens Class I ; Leukocyte Immunoglobulin-like Receptor B1 ; Ligands ; Peptides ; NK Cell Lectin-Like Receptor Subfamily C
    Language English
    Publishing date 2023-12-03
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2023.113516
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  2. Article ; Online: Thermal-exchange HLA-E multimers reveal specificity in HLA-E and NKG2A/CD94 complex interactions.

    Ruibal, Paula / Derksen, Ian / van Wolfswinkel, Marjolein / Voogd, Linda / Franken, Kees L M C / El Hebieshy, Angela F / van Hall, Thorbald / Schoufour, Tom A W / Wijdeven, Ruud H / Ottenhoff, Tom H M / Scheeren, Ferenc A / Joosten, Simone A

    Immunology

    2022  Volume 168, Issue 3, Page(s) 526–537

    Abstract: There is growing interest in HLA-E-restricted T-cell responses as a possible novel, highly conserved, vaccination targets in the context of infectious and malignant diseases. The developing field of HLA multimers for the detection and study of peptide- ... ...

    Abstract There is growing interest in HLA-E-restricted T-cell responses as a possible novel, highly conserved, vaccination targets in the context of infectious and malignant diseases. The developing field of HLA multimers for the detection and study of peptide-specific T cells has allowed the in-depth study of TCR repertoires and molecular requirements for efficient antigen presentation and T-cell activation. In this study, we developed a method for efficient peptide thermal exchange on HLA-E monomers and multimers allowing the high-throughput production of HLA-E multimers. We optimized the thermal-mediated peptide exchange, and flow cytometry staining conditions for the detection of TCR and NKG2A/CD94 receptors, showing that this novel approach can be used for high-throughput identification and analysis of HLA-E-binding peptides which could be involved in T-cell and NK cell-mediated immune responses. Importantly, our analysis of NKG2A/CD94 interaction in the presence of modified peptides led to new molecular insights governing the interaction of HLA-E with this receptor. In particular, our results reveal that interactions of HLA-E with NKG2A/CD94 and the TCR involve different residues. Altogether, we present a novel HLA-E multimer technology based on thermal-mediated peptide exchange allowing us to investigate the molecular requirements for HLA-E/peptide interaction with its receptors.
    MeSH term(s) Killer Cells, Natural ; Protein Binding ; Histocompatibility Antigens Class I/metabolism ; Peptides ; Receptors, Antigen, T-Cell ; NK Cell Lectin-Like Receptor Subfamily D/chemistry ; NK Cell Lectin-Like Receptor Subfamily D/metabolism ; NK Cell Lectin-Like Receptor Subfamily C ; HLA-E Antigens
    Chemical Substances Histocompatibility Antigens Class I ; Peptides ; Receptors, Antigen, T-Cell ; NK Cell Lectin-Like Receptor Subfamily D ; NK Cell Lectin-Like Receptor Subfamily C
    Language English
    Publishing date 2022-10-20
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 80124-0
    ISSN 1365-2567 ; 0019-2805 ; 0953-4954
    ISSN (online) 1365-2567
    ISSN 0019-2805 ; 0953-4954
    DOI 10.1111/imm.13591
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  3. Article ; Online: Identification of HLA-E Binding

    Ruibal, Paula / Franken, Kees L M C / van Meijgaarden, Krista E / van Wolfswinkel, Marjolein / Derksen, Ian / Scheeren, Ferenc A / Janssen, George M C / van Veelen, Peter A / Sarfas, Charlotte / White, Andrew D / Sharpe, Sally A / Palmieri, Fabrizio / Petrone, Linda / Goletti, Delia / Abeel, Thomas / Ottenhoff, Tom H M / Joosten, Simone A

    Journal of immunology (Baltimore, Md. : 1950)

    2022  Volume 209, Issue 8, Page(s) 1555–1565

    Abstract: Tuberculosis (TB) remains one of the deadliest infectious diseases worldwide, posing great social and economic burden to affected countries. Novel vaccine approaches are needed to increase protective immunity against the causative ... ...

    Abstract Tuberculosis (TB) remains one of the deadliest infectious diseases worldwide, posing great social and economic burden to affected countries. Novel vaccine approaches are needed to increase protective immunity against the causative agent
    MeSH term(s) Antigens, Bacterial ; CD8-Positive T-Lymphocytes ; Epitopes, T-Lymphocyte ; Histocompatibility Antigens Class I ; Humans ; Mycobacterium tuberculosis ; Peptides ; Tuberculosis ; HLA-E Antigens
    Chemical Substances Antigens, Bacterial ; Epitopes, T-Lymphocyte ; Histocompatibility Antigens Class I ; Peptides
    Language English
    Publishing date 2022-09-12
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    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.2200122
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

To top