PMC:7352545 / 55083-56695 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":"Entry of host cells needs binding of S glycoproteins to the CEACAM receptor, forming S-protein-mediated membrane fusion. The trimeric S glycoprotein bears three S1 receptor heads. The three S1 heads of the virus bind to three receptor molecules on the host cell. Cholesterol is indirectly involved in membrane fusion through CEACAM engagement into “lipid raft” microdomains, increasing multiple S protein interaction with the receptors and triggering membrane fusion [97]. The enveloped CoV, MHV, binds to CEACAMs on cholesterol-depleted cells in BHK cell cultures. The NTD of S1 recognizes CEACAM1. For MERS-CoV, another CEACAM5 isoform is the attachment factor for virus entry [75]. The CoV S1 NTD has a similar tertiary structure to human galactose-recognizing galectins. MHV S1 NTD binds murine CEACAM1a and BCoV S1 NTD binds sugar [98,99,100]. CEACAM1a is a cell adhesion protein (CAM) and its mRNA is alternatively spliced. The cryo-EM structure of MHV S complexed with CEACAM1a was elucidated [101]. Thus, HCoVs evolutionarily combined the galectin gene of hosts into their S1 glycoprotein gene, while BCoV S1 protein is present without such gene recombination but contains the sugar-recognizing lectin capacity. MHV S1 protein also evolutionarily acquired murine CEACAM1a-recognizing activity [102]. Therefore, CoVs are under evolution to adapt their host receptor interaction to infect cross-species hosts [80,103]. 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