Authors: Han-Yi Huang, Hsin-Yu Liao, Xiaorui Chen, Szu-Wen Wang, Cheng-Wei Cheng, Md. Shahed-Al-Mahmud, Yo-Min Liu, Arpita Mohapatra, Ting-Hua Chen, Jennifer M. Lo, Yi-Min Wu, Hsiu-Hua Ma, Yi-Hsuan Chang, Ho-Yang Tsai, Yu-Chi Chou, Yi-Ping Hsueh, Ching-Yen Tsai, Pau-Yi Huang, Sui-Yuan Chang, Tai-Ling Chao, Han-Chieh Kao, Ya-Min Tsai, Yen-Hui Chen, Chung-Yi Wu, Jia-Tsrong Jan, Ting-Jen Rachel Cheng, Kuo-I Lin, Che Ma, Chi-Huey Wong
Published: 2022-03-01
DOI: 10.1126/scitranslmed.abm0899
Source: Full article
A major challenge to end the pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is to develop a broadly protective vaccine that elicits long-term immunity. As the key immunogen, the viral surface spike (S) protein is frequently mutated, and conserved epitopes are shielded by glycans. Here, we revealed that S protein glycosylation has site-differential effects on viral infectivity. We found that S protein generated by lung epithelial cells has glycoforms associated with increased infectivity. Compared to the fully glycosylated S protein, immunization of S protein with N-glycans trimmed to the mono-GlcNAc–decorated state (S