Galectin-3 binds Neisseria meningitidis and increases interaction with phagocytic cells
Galectin-3 is expressed and secreted by immune cells and has been implicated in multiple aspects of the inflammatory response. It is a glycan binding protein which can exert its functions within cells or exogenously by binding cell surface ligands, acting as a molecular bridge or activating signalli...
| Main Authors: | , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2012
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| _version_ | 1826293695141380096 |
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| author | Quattroni, P Li, Y Lucchesi, D Lucas, S Hood, D Herrmann, M Gabius, H Tang, C Exley, R |
| author_facet | Quattroni, P Li, Y Lucchesi, D Lucas, S Hood, D Herrmann, M Gabius, H Tang, C Exley, R |
| author_sort | Quattroni, P |
| collection | OXFORD |
| description | Galectin-3 is expressed and secreted by immune cells and has been implicated in multiple aspects of the inflammatory response. It is a glycan binding protein which can exert its functions within cells or exogenously by binding cell surface ligands, acting as a molecular bridge or activating signalling pathways. In addition, this lectin has been shown to bind to microorganisms. In this study we investigated the interaction between galectin-3 and Neisseria meningitidis, an important extracellular human pathogen, which is a leading cause of septicaemia and meningitis. Immunohistochemical analysis indicated that galectin-3 is expressed during meningococcal disease and colocalizes with bacterial colonies in infected tissues from patients. We show that galectin-3 binds to N.meningitidis and we demonstrate that this interaction requiresfull-length, intact lipopolysaccharide molecules. We found that neither exogenous nor endogenous galectin-3 contributes to phagocytosis of N.meningitidis; instead exogenous galectin-3 increases adhesion to monocytes and macrophages but not epithelial cells. Finally we used galectin-3 deficient (Gal-3-/-) mice to evaluate the contribution of galectin-3 to meningococcal bacteraemia. We found that Gal-3-/- mice had significantly lower levels of bacteraemia compared with wild-type mice after challenge with live bacteria, indicating that galectin-3 confers an advantage to N. meningitidis during systemic infection. © 2012 Blackwell Publishing Ltd. |
| first_indexed | 2024-03-07T03:34:07Z |
| format | Journal article |
| id | oxford-uuid:bbb7d39a-c458-4bb2-9907-705dd564a904 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T03:34:07Z |
| publishDate | 2012 |
| record_format | dspace |
| spelling | oxford-uuid:bbb7d39a-c458-4bb2-9907-705dd564a9042022-03-27T05:18:58ZGalectin-3 binds Neisseria meningitidis and increases interaction with phagocytic cellsJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:bbb7d39a-c458-4bb2-9907-705dd564a904EnglishSymplectic Elements at Oxford2012Quattroni, PLi, YLucchesi, DLucas, SHood, DHerrmann, MGabius, HTang, CExley, RGalectin-3 is expressed and secreted by immune cells and has been implicated in multiple aspects of the inflammatory response. It is a glycan binding protein which can exert its functions within cells or exogenously by binding cell surface ligands, acting as a molecular bridge or activating signalling pathways. In addition, this lectin has been shown to bind to microorganisms. In this study we investigated the interaction between galectin-3 and Neisseria meningitidis, an important extracellular human pathogen, which is a leading cause of septicaemia and meningitis. Immunohistochemical analysis indicated that galectin-3 is expressed during meningococcal disease and colocalizes with bacterial colonies in infected tissues from patients. We show that galectin-3 binds to N.meningitidis and we demonstrate that this interaction requiresfull-length, intact lipopolysaccharide molecules. We found that neither exogenous nor endogenous galectin-3 contributes to phagocytosis of N.meningitidis; instead exogenous galectin-3 increases adhesion to monocytes and macrophages but not epithelial cells. Finally we used galectin-3 deficient (Gal-3-/-) mice to evaluate the contribution of galectin-3 to meningococcal bacteraemia. We found that Gal-3-/- mice had significantly lower levels of bacteraemia compared with wild-type mice after challenge with live bacteria, indicating that galectin-3 confers an advantage to N. meningitidis during systemic infection. © 2012 Blackwell Publishing Ltd. |
| spellingShingle | Quattroni, P Li, Y Lucchesi, D Lucas, S Hood, D Herrmann, M Gabius, H Tang, C Exley, R Galectin-3 binds Neisseria meningitidis and increases interaction with phagocytic cells |
| title | Galectin-3 binds Neisseria meningitidis and increases interaction with phagocytic cells |
| title_full | Galectin-3 binds Neisseria meningitidis and increases interaction with phagocytic cells |
| title_fullStr | Galectin-3 binds Neisseria meningitidis and increases interaction with phagocytic cells |
| title_full_unstemmed | Galectin-3 binds Neisseria meningitidis and increases interaction with phagocytic cells |
| title_short | Galectin-3 binds Neisseria meningitidis and increases interaction with phagocytic cells |
| title_sort | galectin 3 binds neisseria meningitidis and increases interaction with phagocytic cells |
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