PMC:7352545 / 65747-69051 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":"6.4. Effects of Receptor and Ligand S Glycosylation on Virus–Host Interaction\nSAs are predominant surface determinants for pathogen attachment, adherence and entry to host cells. Eleven representative vertebrate virus families utilize SAs as initial entry receptors or as attachment factors. Interaction of virus with SA-containing glycans is complex because virus SA-binding lectins are inherently of very low affinity. Viruses acquire enzymes to catalyze virion elution by regional depletion of binding receptors [56]. TM S glycoprotein recognizes oligosaccharide receptors. Using cryo-EM technology and observed structures of S glycoprotein trimers of CoV OC43 complexed with 9-O-acetylated SA, S glycoprotein was demonstrated to mediate virus adhesion and entry to host cells. All CoV S proteins show conservation in binding to 9-O-acetyl-SAs. MERS-CoV also recognizes 9-carbon sugar SA species. MERS-CoV S-1A binds to SA species. For example, SAα2,3- over SAα2,6-linkages expressed in human erythrocytes and mucins are preferentially targeted by MERS-CoV S-1A. Binding is hence blocked by SA modification to 5-N-NeuGc and 7, 9-O-NeuAc species [73]. For example, impairment of ACE2 receptor glycosylation does not influence S-glycoprotein-ACE2 interaction, however, SARS-CoV-2 virus entry into respiratory epithelial host cells was downregulated [133]. Changes in ACE2 N-glycans do not apparently influence interaction with the SARS-CoV S glycoprotein, but instead, impair viral S glycoprotein-mediated membrane fusion. The receptor glycan structures decide the entry of some human viruses. Changes in ACE2 receptor sialylation influences interaction affinity between virus ligands and host receptor. Inter-species or individual genetic variations such as drift and mutation may occur in SARS-CoVs. This explains currently emerging differences in CoV responses within the same population such as humans.\nOn 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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