PMC:7712180 / 80382-82273
Annnotations
{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7712180","sourcedb":"PMC","sourceid":"7712180","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7712180","text":"Observation of agglutination of human erythrocytes by intact MERS-CoV particles led to the finding that Sia-binding activity of MERS-CoV is mediated by multivalent S1A (S1-NTD) [112]. One hundred thirty-five glycan structures were used for determination of receptor binding specificity of multivalent MERS-S1A-containing nanoparticles by glycan arrays. It appeared that MERS-S1A nanoparticles bind selectively to nonmodified Neu5Ac but not to Neu5Gc or (7,)9-O-acetylated Neu5Ac. No binding to Neu5Gc-terminated glycans was explained by steric hindrance of the extra hydroxyl group of Neu5Gc in the MERS- S1A hydrophobic pocket formed by F39, F101, I131 and I132 [148]. For sialyl linkage specificity, MERS-CoV S1A prefers α2,3 over α2,6 linkages, either short, sulfated, α2,3-linked mono-Sia LewisX or long, branched, α2,3-linked tri-Sia with four type 2 LN repeats. Pretreatment of Calu-3 human airway cells with neuraminidase inhibited infection of MERS-CoV, indicating that Sia is necessary for MERS-CoV infection. Accordingly, multivalent MERS-CoV S1A-containing nanoparticles were shown to specifically bind to infection sites in individual hosts: dromedary camel nasal epithelial cells, human type II pneumocytes in the alveolar wall that contains an abundance of α2,3-sialyl type 2 LN and a small amount of α2,3-sialyl-LewisX [19], and pipistrelle bat intestinal epithelial cells. Removal of Sia from cell surface glycans by treatment with neuraminidase abolished binding of the nanoparticles, confirming that MERS-CoV S1A binds to infected cells via Sia recognition [108]. The cryo-EM structure of MERS-CoV S in complex with α2,3-SLN (pdb: 6q06) showed Sia binding in a surface-exposed groove (domain A) of each monomer (Figure 9, left). Analysis of the structure indicated the five residues Q36, A92, I132, S133 and R307 directly anchoring Neu5Ac as shown in Figure 9, right 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