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  1. Article ; Online: Molecular recognition of

    Nieto-Fabregat, Ferran / Marseglia, Angela / Thépaut, Michel / Kleman, Jean-Philippe / Abbas, Massilia / Le Roy, Aline / Ebel, Christine / Maalej, Meriem / Simorre, Jean-Pierre / Laguri, Cedric / Molinaro, Antonio / Silipo, Alba / Fieschi, Franck / Marchetti, Roberta

    iScience

    2024  Volume 27, Issue 2, Page(s) 108792

    Abstract: Due to their ability to recognize carbohydrate structures, lectins emerged as potential receptors for bacterial lipopolysaccharides (LPS). Despite growing interest in investigating the association between host receptor lectins and exogenous glycan ... ...

    Abstract Due to their ability to recognize carbohydrate structures, lectins emerged as potential receptors for bacterial lipopolysaccharides (LPS). Despite growing interest in investigating the association between host receptor lectins and exogenous glycan ligands, the molecular mechanisms underlying bacterial recognition by human lectins are still not fully understood. We contributed to fill this gap by unveiling the molecular basis of the interaction between the lipooligosaccharide of
    Language English
    Publishing date 2024-01-04
    Publishing country United States
    Document type Journal Article
    ISSN 2589-0042
    ISSN (online) 2589-0042
    DOI 10.1016/j.isci.2024.108792
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: The unique 3D arrangement of macrophage galactose lectin enables

    Abbas, Massilia / Maalej, Meriem / Nieto-Fabregat, Ferran / Thépaut, Michel / Kleman, Jean-Philippe / Ayala, Isabel / Molinaro, Antonio / Simorre, Jean-Pierre / Marchetti, Roberta / Fieschi, Franck / Laguri, Cedric

    PNAS nexus

    2023  Volume 2, Issue 9, Page(s) pgad310

    Abstract: Lipopolysaccharides are a hallmark of gram-negative bacteria, and their presence at the cell surface is key for bacterial integrity. As surface-exposed components, they are recognized by immunity C-type lectin receptors present on antigen-presenting ... ...

    Abstract Lipopolysaccharides are a hallmark of gram-negative bacteria, and their presence at the cell surface is key for bacterial integrity. As surface-exposed components, they are recognized by immunity C-type lectin receptors present on antigen-presenting cells. Human macrophage galactose lectin binds
    Language English
    Publishing date 2023-09-20
    Publishing country England
    Document type Journal Article
    ISSN 2752-6542
    ISSN (online) 2752-6542
    DOI 10.1093/pnasnexus/pgad310
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  3. Article ; Online: Human Macrophage Galactose-Type Lectin (MGL) Recognizes the Outer Core of Escherichia coli Lipooligosaccharide.

    Maalej, Meriem / Forgione, Rosa Ester / Marchetti, Roberta / Bulteau, François / Thépaut, Michel / Lanzetta, Rosa / Laguri, Cedric / Simorre, Jean-Pierre / Fieschi, Franck / Molinaro, Antonio / Silipo, Alba

    Chembiochem : a European journal of chemical biology

    2019  Volume 20, Issue 14, Page(s) 1778–1782

    Abstract: Carbohydrate-lectin interactions intervene in and mediate most biological processes, including a crucial modulation of immune responses to pathogens. Despite growing interest in investigating the association between host receptor lectins and exogenous ... ...

    Abstract Carbohydrate-lectin interactions intervene in and mediate most biological processes, including a crucial modulation of immune responses to pathogens. Despite growing interest in investigating the association between host receptor lectins and exogenous glycan ligands, the molecular mechanisms underlying bacterial recognition by human lectins are still not fully understood. Herein, a novel molecular interaction between the human macrophage galactose-type lectin (MGL) and the lipooligosaccharide (LOS) of Escherichia coli strain R1 is described. Saturation transfer difference NMR spectroscopy analysis, supported by computational studies, demonstrated that MGL bound to the purified deacylated LOS
    MeSH term(s) Binding Sites ; Escherichia coli/chemistry ; Humans ; Lectins, C-Type/chemistry ; Lectins, C-Type/metabolism ; Lipopolysaccharides/chemistry ; Lipopolysaccharides/metabolism ; Molecular Docking Simulation ; Nuclear Magnetic Resonance, Biomolecular ; Protein Binding
    Chemical Substances Lectins, C-Type ; Lipopolysaccharides ; MGL lectin, human ; lipid-linked oligosaccharides
    Language English
    Publishing date 2019-06-24
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2020469-3
    ISSN 1439-7633 ; 1439-4227
    ISSN (online) 1439-7633
    ISSN 1439-4227
    DOI 10.1002/cbic.201900087
    Database MEDical Literature Analysis and Retrieval System OnLINE

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