Imperial College London
Alternate

ProfessorTenFeizi

Faculty of Medicine, Department of Metabolism, Digestion and Reproduction

Professor and Director of the Glycosciences Laboratory
 
 
 
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Contact

 

+44 (0)20 7594 7207t.feizi

 
 
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Location

 

E518Burlington DanesHammersmith Campus

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Summary

 

Publications

Citation

BibTex format

@article{Zhang:2016:glycob/cww041,
author = {Zhang, H and Palma, AS and Zhang, Y and Childs, RA and Liu, Y and Mitchell, DA and Guidolin, LS and Weigel, W and Mulloy, B and Ciocchini, AE and Feizi, T and Chai, W},
doi = {glycob/cww041},
journal = {Glycobiology},
pages = {1086--1096},
title = {Generation and characterization of β1,2-gluco-oligosaccharide probes from Brucella abortus cyclic β-glucan and their recognition by C-type lectins of the immune system},
url = {http://dx.doi.org/10.1093/glycob/cww041},
volume = {26},
year = {2016}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - The β1,2-glucans produced by bacteria are important in invasion, survival andimmunomodulation in infected hosts be they mammals or plants. However, there has been alack of information on proteins which recognize these molecules. This is partly due to theextremely limited availability of the sequence-defined oligosaccharides and derived probesfor use in the study of their interactions. Here we have used the cyclic β1,2-glucan (CβG) ofthe bacterial pathogen Brucella abortus, after removal of succinyl side chains, to preparelinearized oligosaccharides which were used to generate microarrays. We describe optimizedconditions for partial depolymerization of the cyclic glucan by acid hydrolysis and conversionof the β1,2-gluco-oligosaccharides, with degrees of polymerization 2-13, to neoglycolipids forthe purpose of generating microarrays. By microarray analyses we show that the C-type lectinreceptor DC-SIGNR, like the closely related DC-SIGN we investigated earlier, binds to theβ1,2-gluco-oligosaccharides, as does the soluble immune effector serum mannose-bindingprotein. Exploratory studies with DC-SIGN are suggestive of the recognition also of the intactCβG by this receptor. These findings open the way to unravelling mechanisms ofimmunomodulation mediated by β1,2-glucans in mammalian systems.
AU  - Zhang,H
AU  - Palma,AS
AU  - Zhang,Y
AU  - Childs,RA
AU  - Liu,Y
AU  - Mitchell,DA
AU  - Guidolin,LS
AU  - Weigel,W
AU  - Mulloy,B
AU  - Ciocchini,AE
AU  - Feizi,T
AU  - Chai,W
DO  - glycob/cww041
EP  - 1096
PY  - 2016///
SN  - 1460-2423
SP  - 1086
TI  - Generation and characterization of β1,2-gluco-oligosaccharide probes from Brucella abortus cyclic β-glucan and their recognition by C-type lectins of the immune system
T2  - Glycobiology
UR  - http://dx.doi.org/10.1093/glycob/cww041
UR  - http://hdl.handle.net/10044/1/30458
VL  - 26
ER  -
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