Imperial College London
Alternate

DrMariaPanico

Faculty of Natural Sciences, Department of Life Sciences

Laboratory Manager
 
 
 
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Contact

 

+44 (0)20 7594 5204m.panico

 
 
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Location

 

102Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Wu:2015:10.1007/s10719-015-9638-y,
author = {Wu, G and Hitchen, PG and Panico, M and North, SJ and Barbouche, MR and Binet, D and Morris, HR and Dell, A and Haslam, SM},
doi = {10.1007/s10719-015-9638-y},
journal = {Glycoconjugate Journal},
pages = {447--456},
title = {Glycoproteomic studies of IgE from a novel hyper IgE syndrome linked to PGM3 mutation},
url = {http://dx.doi.org/10.1007/s10719-015-9638-y},
volume = {33},
year = {2015}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Glycans serve as important regulators of antibody activities and half-lives. IgE is the most heavily glycosylated antibody, but in comparison to other antibodies little is known about its glycan structure function relationships. We therefore describe the site specific IgE glycosylation from a patient with a novel hyper IgE syndrome linked to mutations in PGM3, which is an enzyme involved in synthesizing UDP-GlcNAc, a sugar donor widely required for glycosylation. A two-step method was developed to prepare two IgE samples from less than 1 mL of serum collected from a patient with PGM3 mutation and a patient with atopic dermatitis as a control subject. Then, a glycoproteomic strategy was used to study the site-specific glycosylation. No glycosylation was found at Asn264, whilst high mannose glycans were only detected at Asn275, tri-antennary glycans were exclusively observed at Asn99 and Asn252, and non-fucosylated complex glycans were detected at Asn99. The results showed similar glycosylation profiles between the two IgE samples. These observations, together with previous knowledge of IgE glycosylation, imply that IgE glycosylation is similarly regulated among healthy control, allergy and PGM3 related hyper IgE syndrome.
AU  - Wu,G
AU  - Hitchen,PG
AU  - Panico,M
AU  - North,SJ
AU  - Barbouche,MR
AU  - Binet,D
AU  - Morris,HR
AU  - Dell,A
AU  - Haslam,SM
DO  - 10.1007/s10719-015-9638-y
EP  - 456
PY  - 2015///
SN  - 1573-4986
SP  - 447
TI  - Glycoproteomic studies of IgE from a novel hyper IgE syndrome linked to PGM3 mutation
T2  - Glycoconjugate Journal
UR  - http://dx.doi.org/10.1007/s10719-015-9638-y
UR  - http://hdl.handle.net/10044/1/31886
VL  - 33
ER  -
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