Identification by surface plasmon resonance of the mycobacterial lipomannan and lipoarabinomannan domains involved in binding to CD14 and LPS-binding protein
| Autor: | Bernadette Coddeville, Laurent Kremer, Joël Mazurier, Dominique Legrand, Emmanuel Maes, Elisabeth Elass, Yann Guérardel |
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| Přispěvatelé: | Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Dynamique des interactions membranaires normales et pathologiques (DIMNP), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université Montpellier 1 (UM1), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Université de Lille-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2007 |
| Předmět: |
Lipopolysaccharides
MESH: Membrane Glycoproteins Lipopolysaccharide Receptors Matrix metalloproteinase 9 Biochemistry MESH: Protein Structure Tertiary 0302 clinical medicine Structural Biology hemic and lymphatic diseases Surface plasmon resonance Receptor Cells Cultured 0303 health sciences Toll-like receptor Membrane Glycoproteins Chemistry MESH: Antigens CD14 Pattern recognition receptor MESH: Toll-Like Receptor 2 MESH: Toll-Like Receptor 1 MESH: Surface Plasmon Resonance Mycobacterium kansasii lipids (amino acids peptides and proteins) MESH: Mycobacterium kansasii MESH: Acute-Phase Proteins CD14 MESH: Cells Cultured Lipoarabinomannan Biophysics LPS-binding protein MESH: Carrier Proteins 03 medical and health sciences Glycolipid Genetics Humans [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Lipomannan Binding site Molecular Biology 030304 developmental biology MESH: Humans Macrophages Mycobacteria MESH: Macrophages MESH: Matrix Metalloproteinase 9 Cell Biology Surface Plasmon Resonance bacterial infections and mycoses Toll-Like Receptor 1 Toll-Like Receptor 2 Protein Structure Tertiary MESH: Lipopolysaccharides Carrier Proteins 030215 immunology Acute-Phase Proteins |
| Zdroj: | FEBS Letters FEBS Letters, Wiley, 2007, 581 (7), pp.1383-90. ⟨10.1016/j.febslet.2007.02.056⟩ FEBS Letters, 2007, 581 (7), pp.1383-90. ⟨10.1016/j.febslet.2007.02.056⟩ |
| ISSN: | 0014-5793 1873-3468 |
| DOI: | 10.1016/j.febslet.2007.02.056⟩ |
| Popis: | International audience; The mycobacterial lipoglycans, lipomannan (LM) and lipoarabinomannan (LAM), regulate host defence mechanisms through their interaction with pattern recognition receptors such as Toll-like receptors (TLRs). We have developed a surface plasmon resonance assay to analyse the molecular basis for the recognition of Mycobacterium kansasii LM or LAM, by immobilized CD14 and LPS-binding protein (LBP) both being capable to promote presentation of bacterial glycolipids to TLRs. The affinity of either LM/LAM was higher to CD14 than to LBP. Kinetic and Scatchard analyses were consistent with a model involving a single class of binding sites. These interactions required the lipidic anchor, but not the carbohydrate domains, of LM or LAM. We also provide evidence that addition of recombinant LBP enhanced the stimulatory effect of LM or LAM on matrix metalloproteinase-9 expression and secretion in macrophages, through a TLR1/TLR2-dependent mechanism. |
| Databáze: | OpenAIRE |
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