Functions of galectins as 'self/non-self'-recognition and effector factors. Issue 5 (25th April 2017)

• Record Type: Journal Article
• Authors: Vasta, Gerardo R.; Feng, Chiguang; González-Montalbán, Nuria; Mancini, Justin; Yang, Lishi; Abernathy, Kelsey; Frost, Graeme; Palm, Cheyenne
• Is Part Of: Pathogens and disease. Volume 75:Issue 5(2017:Jul.)
• Publication Date: 2017-04-25
• Subjects: pattern recognition receptors -- galectins, ß-galactoside -- carbohydrate recognition domain: glycans -- structure -- function -- proto-type -- chimera -- tandem repeat; Medical microbiology -- Periodicals; Pathogenic microorganisms -- Periodicals; Communicable diseases -- Microbiology -- Periodicals; Communicable diseases -- Pathogenesis -- Periodicals; Host-parasite relationships -- Periodicals; Systems biology -- Periodicals; 616.904105
• DOI: 10.1093/femspd/ftx046
• Languages: English
• ISSNs: 2049-632X

Abstract

Abstract: 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. Abstract : In this minireview, we discuss the structural basis of carbohydrate recognition by galectins, an evolutionary conserved family of ß-galactoside-binding lectins, and their binding and effector properties for endogenous ('self') and exogenous ('non-self') glycosylated ligands.