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Structure paper

TitleStructure, receptor recognition, and antigenicity of the human coronavirus CCoV-HuPn-2018 spike glycoprotein.
Journal, issue, pagesCell, Vol. 185, Issue 13, Page 2279-2291.e17, Year 2022
Publish dateJun 23, 2022
AuthorsM 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 Veesler /
PubMed AbstractThe 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- ...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 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 introduction of an oligosaccharide at position N739 of human APN renders cells susceptible to CCoV-HuPn-2018 spike-mediated entry, suggesting that single-nucleotide polymorphisms might account for viral detection in some individuals. Human polyclonal plasma antibodies elicited by HCoV-229E infection and a porcine coronavirus monoclonal antibody inhibit CCoV-HuPn-2018 spike-mediated entry, underscoring the cross-neutralizing activity among ɑ-coronaviruses. These data pave the way for vaccine and therapeutic development targeting this zoonotic pathogen representing the eighth human-infecting coronavirus.
External linksCell / PubMed:35700730 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.8 - 3.8 Å
Structure data

26727

7us6

EMDB-26727, PDB-7us6:
Structure of the human coronavirus CCoV-HuPn-2018 spike glycoprotein with domain 0 in the proximal conformation
Method: EM (single particle) / Resolution: 3.8 Å

26729

7us9

EMDB-26729, PDB-7us9:
CCoV-HuPn-2018 S in the proximal conformation (local refinement of domain 0)
Method: EM (single particle) / Resolution: 3.8 Å

26730

7usa

EMDB-26730, PDB-7usa:
Structure of the human coronavirus CCoV-HuPn-2018 spike glycoprotein with domain 0 in the swung out conformation
Method: EM (single particle) / Resolution: 2.8 Å

26731

7usb

EMDB-26731, PDB-7usb:
CCoV-HuPn-2018 S in the swung out conformation (local refinement of domain 0)
Method: EM (single particle) / Resolution: 3.1 Å

PDB-7u0l:
Crystal structure of the CCoV-HuPn-2018 RBD (domain B) in complex with canine APN
Method: X-RAY DIFFRACTION / Resolution: 3.3 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-HOH:
WATER / Water

Source
  • unidentified human coronavirus
  • canis lupus familiaris (dog)
  • coronaviridae sp. (virus)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / SARS-CoV-2 spike / COVID-19 / fusion peptide / Fab / VIRAL PROTEIN / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID / VIRAL PROTEIN-IMMUNE SYSTEM complex / Human coronavirus / Coronavirus / CCoV-HuPn-2018 / spike glycoprotein / Alpha-coronaviruses

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