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Structural basis for selective recognition of endogenous and microbial polysaccharides by macrophage receptor SIGN-R1

AuthorsSilva-Martín, Noella; Bartual, Sergio G. ; Ramirez-Aportela, E.; Chacón, Pablo ; Park, C.G.; Hermoso, Juan A.
Issue Date2014
CitationStructure 22: 1595- 1606 (2014)
Abstract© 2014 Elsevier Ltd. 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.
Identifiersdoi: 10.1016/j.str.2014.09.001
issn: 1878-4186
Appears in Collections:(IQFR) Artículos
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