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Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
biochemistry, genetics and molecular biology
Glycosylation influences the lectin activities of the macrophage mannose receptor
Journal of Biological Chemistry, Volume 280, No. 38, Year 2005
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Description
The mannose receptor (MR) is a heavily glycosylated endocytic receptor that recognizes both mannosylated and sulfated ligands through its C-type lectin domains and cysteine-rich (CR) domain, respectively. Differential binding properties have been described for MR isolated from different sources, and we hypothesized that this could be due to altered glycosylation. Using MR transductants and purified MR, we demonstrate that glycosylation differentially affects both MR lectin activities. MR transductants generated in glycosylation mutant cell lines lacked most mannose internalization activity, but could internalize sulfated glycans. Accordingly, purified MR bearing truncated Man5-GlcNAc2 glycans (Man5-MR) or non-sialylated complex glycans (SA0-MR) did not bind mannosylated glycans, but could recognize SO4-S-Gal in vitro. Additional studies showed that, although mannose recognition was largely independent of the oligomerization state of the protein, recognition of sulfated carbohydrates was mostly mediated by self-associated MR and that, in SA0-MR, there was a higher proportion of oligomeric MR. These results suggest that self-association could lead to multiple presentation of CR domains and enhanced avidity for sulfated sugars and that non-sialylated MR is predisposed to oligomerize. Therefore, the glycosylation of MR, terminal sialylation in particular, could influence its binding properties at two levels, (i) It is required for mannose recognition; and (ii) it modulates the tendency of MR to self-associate, effectively regulating the avidity of the CR domain for sulfated sugar ligands. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.
Authors & Co-Authors
Su, Yunpeng
United Kingdom, Oxford
University of Oxford Medical Sciences Division
United Kingdom, Oxford
Sir William Dunn School of Pathology
United States, Cambridge
Whitehead Institute
Bakker, Talitha
United Kingdom, Oxford
Sir William Dunn School of Pathology
Harris, James
United Kingdom, Oxford
Sir William Dunn School of Pathology
United States, Albuquerque
Unm Health Sciences Center
Tsang, Clarence
United Kingdom, Oxford
Sir William Dunn School of Pathology
Brown, Gordon D.A.
United Kingdom, Oxford
Sir William Dunn School of Pathology
South Africa, Cape Town
Faculty of Health Sciences
Wormald, Mark R.
United Kingdom, Oxford
Sir William Dunn School of Pathology
Gordon, Siamon
United Kingdom, Oxford
Sir William Dunn School of Pathology
Dwek, Raymond A.
United Kingdom, Oxford
University of Oxford Medical Sciences Division
Rudd, Pauline Mary
United Kingdom, Oxford
University of Oxford Medical Sciences Division
Martinez-Pomares Luisa, Luisa
United Kingdom, Oxford
Sir William Dunn School of Pathology
Statistics
Citations: 72
Authors: 10
Affiliations: 5
Identifiers
Doi:
10.1074/jbc.M503457200
ISSN:
00219258