作者
Hsiang-Chi Huang, Yun-Ju Lai, Chun-Che Liao, Feng-Yang Wang, Ke-Bin Huang, I-Jung Lee, Wen-Cheng Chou, Shih-Han Wang, Ling-Hui Wang, Jung-Mao Hsu, Cheng-Pu Sun, Chun-Tse Kuo, Jyun Wang, Tzu-Chun Hsiao, Po-Jiun Yang, Te-An Lee, Wilson Huang, Fu-An Li, Chen-Yang Shen, Yi-Ling Lin, Mi-Hua Tao, Chia-Wei Li
发表日期
2021/12/1
期刊
EBioMedicine
卷号
74
出版商
Elsevier
简介
Background
Despite clinical success with anti-spike vaccines, the effectiveness of neutralizing antibodies and vaccines has been compromised by rapidly spreading SARS-CoV-2 variants. Viruses can hijack the glycosylation machinery of host cells to shield themselves from the host's immune response and attenuate antibody efficiency. However, it remains unclear if targeting glycosylation on viral spike protein can impair infectivity of SARS-CoV-2 and its variants.
Methods
We adopted flow cytometry, ELISA, and BioLayer interferometry approaches to assess binding of glycosylated or deglycosylated spike with ACE2. Viral entry was determined by luciferase, immunoblotting, and immunofluorescence assays. Genome-wide association study (GWAS) revealed a significant relationship between STT3A and COVID-19 severity. NF-κB/STT3A-regulated N-glycosylation was investigated by gene knockdown, chromatin …
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