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Structural Basis for Selective Recognition of Endogenous and Microbial Polysaccharides by Macrophage Receptor SIGN-R1

Authors
 Noella Silva-Martín  ;  Sergio G. Bartual  ;  Erney Ramírez-Aportela  ;  Pablo Chacón  ;  Chae Gyu Park 
Citation
 STRUCTURE, Vol.22(11) : 1595-1606, 2014 
Journal Title
 STRUCTURE 
ISSN
 0969-2126 
Issue Date
2014
MeSH
Animals ; Binding Sites ; CHO Cells ; Cell Adhesion Molecules/chemistry* ; Cell Adhesion Molecules/metabolism* ; Cricetulus ; Crystallography, X-Ray ; Dextran Sulfate/metabolism* ; Humans ; Immunoglobulin Fc Fragments/metabolism* ; Lectins, C-Type/chemistry* ; Lectins, C-Type/metabolism* ; Mice ; Models, Molecular ; N-Acetylneuraminic Acid/metabolism* ; Protein Structure, Secondary ; Receptors, Cell Surface/chemistry* ; Receptors, Cell Surface/metabolism*
Abstract
SIGN-R1 is a principal receptor for microbial polysaccharides uptake and is responsible for C3 fixation via an unusual complement activation pathway on splenic marginal zone macrophages. In these macrophages, SIGN-R1 is also involved in anti-inflammatory activity of intravenous immunoglobulin by direct interaction with sialylated Fcs. The high-resolution crystal structures of SIGN-R1 carbohydrate recognition domain and its complexes with dextran sulfate or sialic acid, and of the sialylated Fc antibody provide insights into SIGN-R1's selective recognition of α-2,6-sialylated glycoproteins. Unexpectedly, an additional binding site has been found in the SIGN-R1 carbohydrate recognition domain, structurally separate from the calcium-dependent carbohydrate-binding site. This secondary binding site could bind repetitive molecular patterns, as observed in microbial polysaccharides, in a calcium-independent manner. These two binding sites may allow SIGN-R1 to simultaneously bind both immune glycoproteins and microbial polysaccharide components, accommodating SIGN-R1's ability to relate the recognition of microbes to the activation of the classical complement pathway.
Full Text
http://www.sciencedirect.com/science/article/pii/S0969212614002871
DOI
10.1016/j.str.2014.09.001
Appears in Collections:
1. College of Medicine (의과대학) > BioMedical Science Institute (의생명과학부) > 1. Journal Papers
Yonsei Authors
Park, Chae Gyu(박채규) ORCID logo https://orcid.org/0000-0003-1906-1308
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/100307
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