PMC:7352545 / 53920-55058 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":"6.3.2. Dipeptidyl peptidase-4 (DPP4) as MERS-CoV Receptor\nThe Ser exopeptidase DPP-4/human CD26 (PDB: 4L72), a type II TM ectopeptidase, functions as a host cell receptor for MERS-CoV. The RBD structure was characterized by crystallography approaches of the MERS-CoV S glycoprotein–DPP4 complex. DPP4 is a single type II TM glycoprotein with a small cytoplasmic tail in the N-terminal region and is present as a homodimeric form. DPP4 cleaves X-proline dipeptides from the N-terminal region. S glycoprotein recognizes SA species and DPP44 as the attachment and entry receptors, respectively. The MERS-CoV S1 N-terminal domain attaches to DPP4 as the host receptor [81]. The S2 C-terminal domain of MERS-CoV anchors to cellular PM to enter. MERS-CoV S glycoprotein is cleaved at a sequence between the S1 and S2 domains [96]. Another cleavage site S2′ is present in the S2 domain. MERS CoV S glycoprotein sialyl receptors are expressed in the camel nasal respiratory epithelial cells and the human lung alveolar epithelial cells, which express DPP4. Binding capacities are hindered by the SA 9-O-acetyl group or SA 5-N-glycolyl group 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