Application of StrucGP in medical immunology:site-specific N-glycoproteomic analysis of macrophages  

作　　者：Pengfei Li Zexuan Chen Shanshan You Yintai Xu Zhifang Hao Didi Liu Jiechen Shen Bojing Zhu Wei Dan Shisheng Sun 

机构地区：[1]College of Life Sciences,Northwest University,Xi’an 710069,China

出　　处：《Frontiers of Medicine》2023年第2期304-316,共13页医学前沿（英文版）

基　　金：supported by the National Key Research and Development Program of China(No.2019YFA0905200);the National Natural Science Foundation of China(Nos.91853123,81773180,and 21705127).

摘　　要：The structure of N-glycans on specific proteins can regulate innate and adaptive immunity via sensing environmental signals.Meanwhile,the structural diversity of N-glycans poses analytical challenges that limit the exploration of specific glycosylation functions.In this work,we used THP-1-derived macrophages as examples to show the vast potential of a N-glycan structural interpretation tool StrucGP in N-glycoproteomic analysis.The intact glycopeptides of macrophages were enriched and analyzed using mass spectrometry(MS)-based glycoproteomic approaches,followed by the large-scale mapping of site-specific glycan structures via StrucGP.Results revealed that bisected GlcNAc,core fucosylated,and sialylated glycans(e.g.,HexNAc4Hex5Fuc1Neu5Ac1,N4H5F1S1)were increased in M1 and M2 macrophages,especially in the latter.The findings indicated that these structures may be closely related to macrophage polarization.In addition,a high level of glycosylated PD-L1 was observed in M1 macrophages,and the LacNAc moiety was detected at Asn-192 and Asn-200 of PD-L1,and Asn-200 contained Lewis epitopes.The precision structural interpretation of site-specific glycans and subsequent intervention of target glycoproteins and related glycosyltransferases are of great value for the development of new diagnostic and therapeutic approaches for different diseases.

关 键 词：macrophage GLYCOPROTEOME GLYCOPEPTIDES N-glycan structures PD-L1 

分 类 号：R392[医药卫生—免疫学]