Sialylation of immunoglobulin E is a determinant of allergic pathogenicity

doi:10.1038/s41586-020-2311-z

GSTDTAP > 地球科学

DOI	10.1038/s41586-020-2311-z
	Sialylation of immunoglobulin E is a determinant of allergic pathogenicity
	Abdul-Masih, Michael 1; Banyard, Gareth 1; Bodensteiner, Julia 1; Bordier, Emma 1; Bowman, Dominic M.1; Dsilva, Karan 1; Fabry, Matthias 1; Hawcroft, Calum 1; Mahy, Laurent 1; Marchant, Pablo 1; Raskin, Gert 1; Reggiani, Maddalena 1; Shenar, Tomer 1; Tkachenko, Andrew 1; Van Winckel, Hans 1; Vermeylen, Lore 2; Sana, Hugues 1
	2020-04-01
发表期刊	NATURE
ISSN	0028-0836
EISSN	1476-4687
出版年	2020
卷号	582 期号:7811 页码:265-+
文章类型	Article
语种	英语
国家	USA
英文关键词	A specific type of glycosylation-sialylation-is more common on immunoglobulin E from individuals with a peanut allergys than from non-atopic people, suggesting that it has a role in regulating anaphylaxis. Approximately one-third of the world' s population suffers from allergies(1). Exposure to allergens crosslinks immunoglobulin E (IgE) antibodies that are bound to mast cells and basophils, triggering the release of inflammatory mediators, including histamine(2). Although IgE is absolutely required for allergies, it is not understood why total and allergen-specific IgE concentrations do not reproducibly correlate with allergic disease(3-5). It is well-established that glycosylation of IgG dictates its effector function and has disease-specific patterns. However, whether IgE glycans differ in disease states or affect biological activity is completely unknown(6). Here we perform an unbiased examination of glycosylation patterns of total IgE from individuals with a peanut allergy and from non-atopic individuals without allergies. Our analysis reveals an increase in sialic acid content on total IgE from individuals with a peanut allergy compared with non-atopic individuals. Removal of sialic acid from IgE attenuates effector-cell degranulation and anaphylaxis in several functional models of allergic disease. Therapeutic interventions-including removing sialic acid from cell-bound IgE with a neuraminidase enzyme targeted towards the IgE receptor Fc epsilon RI, and administering asialylated IgE-markedly reduce anaphylaxis. Together, these results establish IgE glycosylation, and specifically sialylation, as an important regulator of allergic disease.
领域	地球科学 ; 气候变化 ; 资源环境
收录类别	SCI-E
WOS记录号	WOS:000535225300005
WOS关键词	FOOD ALLERGY ; GLYCOSYLATION ; IGE ; ANTIBODIES ; ANAPHYLAXIS ; CELLS
WOS类目	Multidisciplinary Sciences
WOS研究方向	Science & Technology - Other Topics
引用统计
文献类型	期刊论文
条目标识符	http://119.78.100.173/C666/handle/2XK7JSWQ/281430
专题	地球科学资源环境科学气候变化
作者单位	1.Katholieke Univ Leuven, Inst Astron, Leuven, Belgium; 2.Royal Observ Belgium, Brussels, Belgium
推荐引用方式 GB/T 7714	Abdul-Masih, Michael,Banyard, Gareth,Bodensteiner, Julia,et al. Sialylation of immunoglobulin E is a determinant of allergic pathogenicity[J]. NATURE,2020,582(7811):265-+.
APA	Abdul-Masih, Michael.,Banyard, Gareth.,Bodensteiner, Julia.,Bordier, Emma.,Bowman, Dominic M..,...&Sana, Hugues.(2020).Sialylation of immunoglobulin E is a determinant of allergic pathogenicity.NATURE,582(7811),265-+.
MLA	Abdul-Masih, Michael,et al."Sialylation of immunoglobulin E is a determinant of allergic pathogenicity".NATURE 582.7811(2020):265-+.