PMC:7352545 / 14469-15729 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7352545","sourcedb":"PMC","sourceid":"7352545","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7352545","text":"3.1. Spike (S) Transmembrane Glycoprotein\nIn RNA viruses, the S glycoprotein (PDB: 6VSB) is the biggest protein, heavily glycosylated and its N-terminal domain (NTD) sequence binds to the host receptor to enter the ER of host cells. SARS-CoV-2 S-glycoprotein bears 22 N-glycan sequons in each protomer. Therefore, the trimeric S glycoprotein surface is dominated by 66 N-glycans. The S glycoprotein mediates direct and indirect interaction of virus with host cells in the infection cycle. All CoVs exhibit a surface S glycoprotein, which bears the receptor-binding domain (RBD). The S glycoprotein has a distinct spike structure. When S glycoprotein binds to its host receptor, a host furin-like protease cleaves the S glycoprotein, which liberates the spike fusion peptides, allowing entry of the virus into the host cell [18]. The furin-like protease-generated S1 and S2 exist as a S1/S2 complex, where S1 in a homotrimeric form interacts with the host cell membrane and S2 penetrates the cytosolic area. For SARS-CoV and MERS-CoV, the S1 C-terminal domains (CTDs) have a dual role in virus entry via attachment and fusion. The S1 NTD binds to carbohydrate receptors because the S1 domains act as the RBD. 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