PMC:7352545 / 67655-69051 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":"On the other hand, from the aspect of virus ligand, the S glycoprotein decorates viral surfaces and is, therefore, the target for vaccination design. Virus internalization requires potential glycosylation of viral glycoproteins. Among the three viral envelope components, S and M are the major glycoproteins and E is nascent and not glycosylated. The M glycoprotein consists of a short glycosylated ectodomain in the N-terminal region. The S glycoprotein expressed in hemagglutinating encephalomyelitis virus is an HA that recognizes N-acetyl-9-O-NeuAc as a binding receptor expressed on erythrocyte surfaces [134]. For example, BCoVs attach to the surface receptor of N-acetyl-9-O-NeuAc (9-O-acetylated SAs) on host cells. TGEV and PEDV are currently known as a similar class of such CoVs. PEDV infects multiple hosts including bat, pig, human and monkey, where bats are considered to be the evolutionary origin for PEDV. The S glycoprotein of SARS-CoV-2 utilizes different glycosylation patterns to recognize its receptors. The glycosylation sites in minimal RBD exhibits similar sites to other CoVs. The trimeric SARS-CoV-2 S glycoprotein is also highly glycosylated with 66 N-glycans, but a few O-glycans [135]. Glycosylation of S glycoproteins leads to immune evasion. In the MERS-CoV and the bat-specific CoV-HKU4, glycosylation is linked to zoonotic infection for fusion-based entry 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