N‐glycosylation of the SARS‐CoV‐2 spike protein at Asn331 and Asn343 is involved in spike‐ACE2 binding, virus entry, and regulation of IL‐6

• Published in: Microbiology and immunology Vol. 68; no. 5; pp. 165 - 178
• Main Authors: Das, Tuhin, Luo, Shuhong, Tang, Hao, Fang, Jianmin, Mao, Yinging, Yen, Haw‐Han, Dash, Sabyasachi, Shajahan, Asif, Pepi, Lauren, Huang, Steven, Jones, Valerie S., Xie, Shehuo, Huang, Gordon F., Lu, Jinqiao, Anderson, Blake, Zhang, Benyue, Azadi, Parastoo, Huang, Ruo‐Pan
• Format: Journal Article
• Language: English
• Published: Australia 01.05.2024
• Subjects: ACE2; Angiotensin-Converting Enzyme 2 - metabolism; Asparagine - metabolism; COVID-19 - metabolism; COVID-19 - virology; COVID‐19; Glycosylation; HEK293 Cells; Humans; IL‐6; Interleukin-6 - metabolism; N‐glycosylation; Polysaccharides - metabolism; Protein Binding; receptor‐binding domain; SARS-CoV-2 - metabolism; SARS-CoV-2 - physiology; SARS‐CoV‐2; Spike Glycoprotein, Coronavirus - chemistry; Spike Glycoprotein, Coronavirus - genetics; Spike Glycoprotein, Coronavirus - metabolism; spike protein; Virus Internalization; ACE2; COVID‐19; SARS‐CoV‐2; receptor‐binding domain; spike protein; N‐glycosylation; IL‐6

The coronavirus disease 2019 (COVID‐19) pandemic is an ongoing global public health crisis. The causative agent, the SARS‐CoV‐2 virus, enters host cells via molecular interactions between the viral spike protein and the host cell ACE2 surface protein. The SARS‐CoV‐2 spike protein is extensively deco...