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|Title:||Collectins and ficolins: Sugar pattern recognition molecules of the mammalian innate immune system||Authors:||Lu, J.
|Issue Date:||19-Sep-2002||Citation:||Lu, J., Teh, C., Kishore, U., Reid, K.B.M (2002-09-19). Collectins and ficolins: Sugar pattern recognition molecules of the mammalian innate immune system. Biochimica et Biophysica Acta - General Subjects 1572 (2-3) : 387-400. ScholarBank@NUS Repository. https://doi.org/10.1016/S0304-4165(02)00320-3||Abstract:||Collectins and ficolins represent two important groups of pattern recognition molecules, which bind to oligosaccharide structures on the surface of microorganisms, leading to the killing of bound microbes through complement activation and phagocytosis. Collectins and ficolins bear no significant sequence homology except for the presence of collagen-like sequences over the N-terminal halves of the polypeptides that enable the assembly of these molecules into oligomeric structures. Collectins and ficolins both contain lectin activities within the C-terminal halves of their polypeptides, the C-type carbohydrate recognition domain (CRDs) and fibrinogen β/γ (homology) (FBG) domain, respectively. These domains form trimeric clusters at the ends of the collagen triple helices emanating from a central hub, where the N-terminal ends of the polypeptides merge. The collectins and ficolins seem to have evolved to recognize the surface sugar codes of microbes and their binding, to these arrays of cell surface carbohydrate molecules, targets the microbe for subsequent clearance by phagocytic cells. © 2002 Elsevier Science B.V. All rights reserved.||Source Title:||Biochimica et Biophysica Acta - General Subjects||URI:||http://scholarbank.nus.edu.sg/handle/10635/112824||ISSN:||03044165||DOI:||10.1016/S0304-4165(02)00320-3|
|Appears in Collections:||Staff Publications|
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