Functions of galectins as ‘self/non-self’-recognition and effector factors
| Autor: | Chiguang Feng, Cheyenne Palm, Justin Mancini, Lishi Yang, Graeme Frost, Nuria González-Montalbán, Kelsey Abernathy, Gerardo R. Vasta |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Microbiology (medical) Glycan Galectins Cell Biology 03 medical and health sciences Chimera (genetics) medicine Animals Humans Immunology and Allergy Receptors Immunologic Immune Evasion Galectin Innate immune system 030102 biochemistry & molecular biology General Immunology and Microbiology Effector Pattern recognition receptor Lectin General Medicine Immunity Innate Cell biology 030104 developmental biology Infectious Diseases medicine.anatomical_structure Host-Pathogen Interactions biology.protein Minireview |
| Zdroj: | Pathogens and Disease. 75 |
| ISSN: | 2049-632X |
| DOI: | 10.1093/femspd/ftx046 |
| Popis: | Carbohydrate structures on the cell surface encode complex information that through specific recognition by carbohydrate-binding proteins (lectins) modulates interactions between cells, cells and the extracellular matrix, or mediates recognition of potential microbial pathogens. Galectins are a family of ß-galactoside-binding lectins, which are evolutionary conserved and have been identified in most organisms, from fungi to invertebrates and vertebrates, including mammals. Since their discovery in the 1970s, their biological roles, initially understood as limited to recognition of endogenous carbohydrate ligands in embryogenesis and development, have expanded in recent years by the discovery of their roles in tissue repair and regulation of immune homeostasis. More recently, evidence has accumulated to support the notion that galectins can also bind glycans on the surface of potentially pathogenic microbes, and function as recognition and effector factors in innate immunity, thus establishing a new paradigm. Furthermore, some parasites ‘subvert’ the recognition roles of the vector/host galectins for successful attachment or invasion. These recent findings have revealed a striking functional diversification in this structurally conserved lectin family. |
| Databáze: | OpenAIRE |
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