Molecular recognition of Escherichia coli R1-type core lipooligosaccharide by DC-SIGN
Summary: 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 underlyin...
| Main Authors: | , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2024-02-01
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| Series: | iScience |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2589004224000130 |
| _version_ | 1797351576640159744 |
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| author | Ferran Nieto-Fabregat Angela Marseglia Michel Thépaut Jean-Philippe Kleman Massilia Abbas Aline Le Roy Christine Ebel Meriem Maalej Jean-Pierre Simorre Cedric Laguri Antonio Molinaro Alba Silipo Franck Fieschi Roberta Marchetti |
| author_facet | Ferran Nieto-Fabregat Angela Marseglia Michel Thépaut Jean-Philippe Kleman Massilia Abbas Aline Le Roy Christine Ebel Meriem Maalej Jean-Pierre Simorre Cedric Laguri Antonio Molinaro Alba Silipo Franck Fieschi Roberta Marchetti |
| author_sort | Ferran Nieto-Fabregat |
| collection | DOAJ |
| description | Summary: 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 Escherichia coli and the dendritic cell-specific intracellular adhesion molecules (ICAM)-3 grabbing non-integrin (DC-SIGN). Specifically, a combination of different techniques, including fluorescence microscopy, surface plasmon resonance, NMR spectroscopy, and computational studies, demonstrated that DC-SIGN binds to the purified deacylated R1 lipooligosaccharide mainly through the recognition of its outer core pentasaccharide, which acts as a crosslinker between two different tetrameric units of DC-SIGN. Our results contribute to a better understanding of DC-SIGN-LPS interaction and may support the development of pharmacological and immunostimulatory strategies for bacterial infections, prevention, and therapy. |
| first_indexed | 2024-03-08T13:02:28Z |
| format | Article |
| id | doaj.art-b0db4208477b44db88da22e26245f019 |
| institution | Directory Open Access Journal |
| issn | 2589-0042 |
| language | English |
| last_indexed | 2024-03-08T13:02:28Z |
| publishDate | 2024-02-01 |
| publisher | Elsevier |
| record_format | Article |
| series | iScience |
| spelling | doaj.art-b0db4208477b44db88da22e26245f0192024-01-19T05:01:52ZengElsevieriScience2589-00422024-02-01272108792Molecular recognition of Escherichia coli R1-type core lipooligosaccharide by DC-SIGNFerran Nieto-Fabregat0Angela Marseglia1Michel Thépaut2Jean-Philippe Kleman3Massilia Abbas4Aline Le Roy5Christine Ebel6Meriem Maalej7Jean-Pierre Simorre8Cedric Laguri9Antonio Molinaro10Alba Silipo11Franck Fieschi12Roberta Marchetti13Department of Chemical Science, University of Naples Federico II Via Cinthia 4, 80126 Naples, ItalyDepartment of Chemical Science, University of Naples Federico II Via Cinthia 4, 80126 Naples, ItalyUniversity Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, 41 Avenue des Martyrs, 38000 Grenoble, FranceUniversity Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, 41 Avenue des Martyrs, 38000 Grenoble, FranceUniversity Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, 41 Avenue des Martyrs, 38000 Grenoble, FranceUniversity Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, 41 Avenue des Martyrs, 38000 Grenoble, FranceUniversity Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, 41 Avenue des Martyrs, 38000 Grenoble, FranceDepartment of Chemical Science, University of Naples Federico II Via Cinthia 4, 80126 Naples, Italy; University Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, 41 Avenue des Martyrs, 38000 Grenoble, FranceUniversity Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, 41 Avenue des Martyrs, 38000 Grenoble, FranceUniversity Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, 41 Avenue des Martyrs, 38000 Grenoble, FranceDepartment of Chemical Science, University of Naples Federico II Via Cinthia 4, 80126 Naples, ItalyDepartment of Chemical Science, University of Naples Federico II Via Cinthia 4, 80126 Naples, ItalyUniversity Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, 41 Avenue des Martyrs, 38000 Grenoble, France; Institut Universitaire de France (IUF), Paris, FranceDepartment of Chemical Science, University of Naples Federico II Via Cinthia 4, 80126 Naples, Italy; Corresponding authorSummary: 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 Escherichia coli and the dendritic cell-specific intracellular adhesion molecules (ICAM)-3 grabbing non-integrin (DC-SIGN). Specifically, a combination of different techniques, including fluorescence microscopy, surface plasmon resonance, NMR spectroscopy, and computational studies, demonstrated that DC-SIGN binds to the purified deacylated R1 lipooligosaccharide mainly through the recognition of its outer core pentasaccharide, which acts as a crosslinker between two different tetrameric units of DC-SIGN. Our results contribute to a better understanding of DC-SIGN-LPS interaction and may support the development of pharmacological and immunostimulatory strategies for bacterial infections, prevention, and therapy.http://www.sciencedirect.com/science/article/pii/S2589004224000130MicrobiologyStructural biology |
| spellingShingle | Ferran Nieto-Fabregat Angela Marseglia Michel Thépaut Jean-Philippe Kleman Massilia Abbas Aline Le Roy Christine Ebel Meriem Maalej Jean-Pierre Simorre Cedric Laguri Antonio Molinaro Alba Silipo Franck Fieschi Roberta Marchetti Molecular recognition of Escherichia coli R1-type core lipooligosaccharide by DC-SIGN iScience Microbiology Structural biology |
| title | Molecular recognition of Escherichia coli R1-type core lipooligosaccharide by DC-SIGN |
| title_full | Molecular recognition of Escherichia coli R1-type core lipooligosaccharide by DC-SIGN |
| title_fullStr | Molecular recognition of Escherichia coli R1-type core lipooligosaccharide by DC-SIGN |
| title_full_unstemmed | Molecular recognition of Escherichia coli R1-type core lipooligosaccharide by DC-SIGN |
| title_short | Molecular recognition of Escherichia coli R1-type core lipooligosaccharide by DC-SIGN |
| title_sort | molecular recognition of escherichia coli r1 type core lipooligosaccharide by dc sign |
| topic | Microbiology Structural biology |
| url | http://www.sciencedirect.com/science/article/pii/S2589004224000130 |
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