文献类型：期刊文献

英文题名：Comparative N-glycoproteomics Characterization of N-glycoproteins of H3N8 Viruses Produced in Chicken Embryos versus MDCK Cells

作者：Wang, Honglin[1,2,4];Zhang, Zheng[1,2];Zhang, Xu[1,2];Zhao, Liang[1,2,3];Liu, Xuping[3];Ye, Qian[1,2];Tan, Wen-Song[1,2,3]

机构：[1]East China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]Shanghai Collaborat Innovat Ctr Biomfg, Shanghai 200237, Peoples R China;[3]Shanghai BioEngine Scitech Co Ltd, Shanghai 201203, Peoples R China;[4]Qingdao Inst Technol, Qingdao 266300, Peoples R China

年份：2025

卷号：10

期号：51

起止页码：62727

外文期刊名：ACS OMEGA

收录：;WOS:【SCI-EXPANDED(收录号:WOS:001641547000001)】；

基金：The authors would like to thank Zhiying Xiao for his help with the preparation of this paper.

语种：英文

摘要：N-linked glycosylation has been demonstrated to play a critical role in the folding and immunomodulation of influenza virus glycoproteins. Chicken embryos have historically been the predominant production host for influenza vaccines; however, Madin-Darby canine kidney (MDCK) cells have recently emerged as a significant alternative host. N-glycosylation of H3N8 viruses produced in chicken embryos and MDCK cells was comparatively characterized by mass spectrometry-based N-glycoproteomics with isotopic labeling at the molecular level of intact N-glycopeptides. A total of 3647 and 912 site- and structure-specific intact N-glycopeptides with glycosite localization and N-glycan monosaccharide sequence structure confirmation were identified from the whole N-glycoproteome and hemagglutinin N-glycoproteins, respectively, which correspond to 308 unique N-glycan sequence structures (defined by specific chemical linkages and branching patterns) and are derived from 171 distinct monosaccharide compositions. The data additionally contains N-glycosylation of the noncanonical glycosylation motif Asn-X-Cys. Ultimately, 628 intact N-glycopeptides were quantified as differentially expressed intact N-glycopeptides (DEGPs), where 425 were down-regulated and 203 were up-regulated. The results provide a global view of N-glycosylation of H3N8 viruses produced from the two systems, which has implications for virus research, including vaccine development, and the method could be extended to the N-glycosylation characterization of other viruses.