Structure, receptor recognition and antigenicity of the human coronavirus CCoV-HuPn-2018 spike glycoproteinThe isolation of CCoV-HuPn-2018 from a child respiratory swab indicates that more coronaviruses are spilling over to humans than previously appreciated. We determined structures of the CCoV-HuPn-2018 spike glycoprotein trimer in two distinct conformational states and show that its domain 0 recognizes sialosides. We identified that the CCoV-HuPn-2018 spike binds canine, feline and porcine aminopeptidase N (APN) orthologs, which serve as entry receptors, and determined the structure of the receptor-binding B domain in complex with canine APN.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 structures of the CCoV-HuPn-2018 spike glycoprotein trimer in two distinct conformational states and show that its domain 0 recognizes sialosides. We identified that the CCoV-HuPn-2018 spike binds canine, feline and porcine aminopeptidase N (APN) orthologs, which serve as entry receptors, and determined the structure of the receptor-binding B domain in complex with canine APN.M. Alejandra Tortorici, Alexandra C. Walls, Anshu Joshi, Young-Jun Park, Rachel T. Eguia, Marcos C. Miranda, Elizabeth Kepl, Annie Dosey, Terry Stevens-Ayers, Michael J. Boeckh, Amalio Telenti, Antonio Lanzavecchia, Neil P. King, Davide Corti, Jesse D. Bloom, David Veeslerhttps://secure.jbs.elsevierhealth.com/action/getSharedSiteSession?redirect=https%3A%2F%2Fwww.cell.com%2Fcell%2Ffulltext%2FS0092-8674%2822%2900650-X%3Frss%3Dyes&rc=0http://www.cell.com/cell/inpress.rssCellCell RSS feed.Wireless News CampaignMay 27, 2022

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