Allergy Associated With N-glycans on Glycoprotein Allergens
10.16476/j.pibb.2023.0292
- VernacularTitle:糖蛋白过敏原N-糖链与过敏的相关性研究
- Author:
Yu-Xin ZHANG
1
;
Rui-Jie LIU
1
;
Shao-Xing ZHANG
1
;
Shu-Ying YUAN
2
;
Yan-Wen CHEN
3
;
Yi-Lin YE
1
;
Qian-Ge LIN
1
;
Xin-Rong LU
4
;
Yong-Liang TONG
4
;
Li CHEN
4
;
Gui-Qin SUN
1
Author Information
1. School of Medical Technology and Information Engineering, Zhejiang Chinese Medical University, Hangzhou 310053, China
2. Department of Clinical Laboratory, Jiaxing Maternity and Child Health Care Hospital, Jiaxing 314009, China
3. Department of Central Laboratory, Renji Hospital Shanghai Jiaotong University School of Medical, Ningbo Hangzhou Bay Hospital, Ningbo 315336, China
4. Department of Medical Microbiology and Parasitology, Key Laboratory of Medical Molecular Virology of Ministries of Education and National Health Committee, School of Basic Medical Sciences, Fudan University, Shanghai 200032, China
- Publication Type:Journal Article
- Keywords:
allergic reaction;
N-glycosylation;
N-sugar chain structures;
glycosylation-related enzymes;
allergy mechanism
- From:
Progress in Biochemistry and Biophysics
2024;51(5):1023-1033
- CountryChina
- Language:Chinese
-
Abstract:
Protein as the allergens could lead to allergy. In addition, a widespread class of allergens were known as glycans of N-glycoprotein. N-glycoprotein contained oligosaccharide linked by covalent bonds with protein. Recently,studies implicated that allergy was associated with glycans of heterologous N-glycoprotein found in food, inhalants, insect toxins, etc. The N-glycan structure of N-glycoprotein allergen has exerted an influence on the binding between allergens and IgE, while the recognition and presentation of allergens by antigen-presenting cells (APCs) were also affected. Some researches showed thatN-glycan structure of allergen was remodeled by N-glycosidase, such as cFase I, gpcXylase, as binding of allergen and IgE partly decreased. Thus, allergic problems caused by N-glycoproteins could potentially be solved by modifying or altering the structure ofN-glycoprotein allergens, addressing the root of the issue. Mechanism of N-glycans associated allergy could also be elaborated through glycosylation enzymes, alterations of host glycosylation. This article hopes to provide a separate insight for glycoimmunology perspective, and an alternative strategy for clinical prevention or therapy of allergic diseases.
