Imperial College London
Alternate

DrMaureenTaylor

Faculty of Natural Sciences, Department of Life Sciences

Reader in Biological Chemistry
 
 
 
//

Contact

 

+44 (0)20 7594 5281m.taylor

 
 
//

Location

 

607Sir Ernst Chain BuildingSouth Kensington Campus

//

Summary

 

Publications

Citation

BibTex format

@article{Kim:2018:glycob/cwy050,
author = {Kim, J-W and Budzak, J and Liu, Y and Jégouzo, SAF and Drickamer, K and Taylor, ME},
doi = {glycob/cwy050},
journal = {Glycobiology},
pages = {592--600},
title = {Identification of serum glycoprotein ligands for the immunomodulatory receptor blood dendritic cell antigen 2.},
url = {http://dx.doi.org/10.1093/glycob/cwy050},
volume = {28},
year = {2018}
}
Download

RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Blood dendritic cell antigen 2 (BDCA-2) is a C-type lectin found on the surface of plasmacytoid dendritic cells. It functions as a glycan-binding receptor that downregulates the production of type I interferons and thus plays a role in oligosaccharide-mediated immunomodulation. The carbohydrate recognition domain in BDCA-2 binds selectively to galactose-terminated bi-antennary glycans. Because the plasmacytoid dendritic cells function in a plasma environment rich in glycoproteins, experiments have been undertaken to identify endogenous ligands for blood dendritic cell antigen 2. A combination of blotting, affinity chromatography and proteomic analysis reveals that serum glycoprotein ligands for BDCA-2 include IgG, IgA and IgM. Compared to binding of IgG, which was previously described, IgA and IgM bind with higher affinity. The association constants for the different subclasses of immunoglobulins are below and roughly proportional to the serum concentrations of these glycoprotein ligands. Binding to the other main serum glycoprotein ligand, α2-macroglobulin, is independent of whether this protease inhibitor is activated. Binding to all of these glycoprotein ligands is mediated predominantly by bi-antennary glycans in which each branch bears a terminal galactose residue. The different affinities of the glycoprotein ligands reflect the different numbers of these galactose-terminated glycans and their degree of exposure on the native glycoproteins. The results suggest that normal serum levels of immunoglobulins could downmodulate interferon stimulation of further antibody production.
AU  - Kim,J-W
AU  - Budzak,J
AU  - Liu,Y
AU  - Jégouzo,SAF
AU  - Drickamer,K
AU  - Taylor,ME
DO  - glycob/cwy050
EP  - 600
PY  - 2018///
SP  - 592
TI  - Identification of serum glycoprotein ligands for the immunomodulatory receptor blood dendritic cell antigen 2.
T2  - Glycobiology
UR  - http://dx.doi.org/10.1093/glycob/cwy050
UR  - https://www.ncbi.nlm.nih.gov/pubmed/29796630
UR  - http://hdl.handle.net/10044/1/60229
VL  - 28
ER  -
Download