Structure, receptor recognition, and antigenicity of the human coronavirus CCoV-HuPn-2018 spike glycoprotein

• Published in: Cell Vol. 185; no. 13; pp. 2279 - 2291.e17
• Main Authors: Tortorici, M. Alejandra, Walls, Alexandra C., Joshi, Anshu, Park, Young-Jun, Eguia, Rachel T., Miranda, Marcos C., Kepl, Elizabeth, Dosey, Annie, Stevens-Ayers, Terry, Boeckh, Michael J., Telenti, Amalio, Lanzavecchia, Antonio, King, Neil P., Corti, Davide, Bloom, Jesse D., Veesler, David
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 23.06.2022
• Subjects: aminopeptidase; Animals; Cats; CCoV-HuPn-2018; CD13 Antigens - chemistry; CD13 Antigens - metabolism; Cell Line; children; Coronavirus - metabolism; Coronavirus 229E, Human - metabolism; Coronavirus Infections; cryo-EM; Dogs; glycoproteins; HCoV-229E; Humans; membrane alanyl aminopeptidase; monoclonal antibodies; oligosaccharides; Orthocoronavirinae; pathogens; Receptors, Virus - metabolism; sialosides; Spike Glycoprotein, Coronavirus - metabolism; Swine; therapeutics; vaccines; zoonotic viruses; ɑ-coronaviruses; ɑ-coronaviruses; HCoV-229E; zoonotic viruses; aminopeptidase; sialosides; CCoV-HuPn-2018; cryo-EM

The isolation of CCoV-HuPn-2018 from a child respiratory swab indicates that more coronaviruses are spilling over to humans than previously appreciated. We determined the structures of the CCoV-HuPn-2018 spike glycoprotein trimer in two distinct conformational states and showed that its domain 0 rec...