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Curr Top Microbiol Immunol. 2019;423:77-93. doi: 10.1007/82_2019_151.

IgE Glycosylation in Health and Disease.

Author information

1
Massachusetts General Hospital, Center for Immunology and Inflammatory Diseases, Harvard Medical School, 149 13th Street, Room 8.321, Boston, MA, 02129, USA.
2
Massachusetts General Hospital, Center for Immunology and Inflammatory Diseases, Harvard Medical School, 149 13th Street, Room 8.321, Boston, MA, 02129, USA. Robert.Anthony@mgh.harvard.edu.

Abstract

IgE are absolutely required for initiation of allergy reactions, which affect over 20% of the world's population. IgE are the least prevalent immunoglobulins in circulation with 12-h and 2-day half-lives in mouse and human serum, respectively, but an extended tissue half-life of 3-weeks bound to the surface of mast cells by the high affinity IgE receptor, FcεRI (Gould and Sutton 2008). Although the importance of glycosylation to IgG biology is well established, less is known regarding the contribution of IgE glycosylation to allergic inflammation. IgE has seven and nine N-linked glycosylation sites distributed across human and murine constant chains, respectively. Here we discuss studies that have analyzed IgE glycosylation and its function, and how IgE glycosylation contributions to health and disease.

PMID:
30820668
PMCID:
PMC6750212
[Available on 2020-01-01]
DOI:
10.1007/82_2019_151
[Indexed for MEDLINE]

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