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TitleOC43 clinical isolate spike proteins have distinct carbohydrate-binding properties.
Journal, issue, pagesNat Commun, Year 2026
Publish dateMay 16, 2026
AuthorsZaky Hassan / Min Jin / Ying Liu / Zhijie Li / Alan H M Wong / Marc Desforges / Adam Forman / Mark Nitz / Tarini Gunawardena / Theo J Moraes / Masahiro Narimatsu / Jeffrey L Wrana / Hai Yu / Xi Chen / James M Rini /
PubMed AbstractThe human coronavirus HCoV-OC43 (OC43) is the most widespread of the four common cold-causing seasonal coronaviruses, and tissue culture-adapted strains of it have been used for ~50 years. ...The human coronavirus HCoV-OC43 (OC43) is the most widespread of the four common cold-causing seasonal coronaviruses, and tissue culture-adapted strains of it have been used for ~50 years. Nevertheless, clinical isolates of OC43 differ from tissue culture-adapted OC43 in ways that call into question the value of the latter as a model. Among these are differences in their entry mechanisms and the activities of their hemagglutinin-esterases (HE). We now show that the spike proteins of OC43 clinical isolates differ from that of the tissue culture-adapted reference strain (OC43-Lab) in their carbohydrate-binding properties and ability to bind mucins, decoy receptors cleaved by the HE. We also show that, unlike HCoV-HKU1 (HKU1), they do not bind with high affinity and specificity the 9-O-acetylated α2-8-linked disialic acid moiety implicated in viral entry for OC43-Lab and HKU1. The spike proteins of the OC43 clinical isolates possess two inserts, not found in OC43-Lab, that flank the carbohydrate-binding site. Our structural analysis of a representative clinical isolate shows that insert-2 is a determinant of these specificity differences and that the carbohydrate-binding site undergoes conformational changes on carbohydrate binding. These structural features are shared by HKU1 and suggest common mechanisms for adaptation to the human sialoglycome.
External linksNat Commun / PubMed:42143065
MethodsEM (single particle)
Resolution1.68 - 2.05 Å
Structure data

70900

9ovk

EMDB-70900, PDB-9ovk:
Cryo-EM structure of HCoV-OC43-Lab Spike glycoprotein in complex with 9O-acetyl GD3 sialoglycan (D1 domain local refine)
Method: EM (single particle) / Resolution: 1.7 Å

70901

9ovl

EMDB-70901, PDB-9ovl:
Cryo-EM structure of HCoV-OC43-Lab Spike glycoprotein in complex with 9O-acetyl GD3 sialoglycan
Method: EM (single particle) / Resolution: 1.68 Å

70902

9ovm

EMDB-70902, PDB-9ovm:
Cryo-EM structure of HCoV-OC43-C2 Spike glycoprotein (local refined D1 domain)
Method: EM (single particle) / Resolution: 2.05 Å

70903

9ovn

EMDB-70903, PDB-9ovn:
Cryo-EM structure of HCoV-OC43-C2 Spike glycoprotein
Method: EM (single particle) / Resolution: 1.93 Å

70904

9ovo

EMDB-70904, PDB-9ovo:
Cryo-EM structure of HCoV-OC43-C2 Spike glycoprotein in complex with 9O-acetyl GD3 sialoglycan (Local refined D1 domain)
Method: EM (single particle) / Resolution: 1.98 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

PDB-1ar1:
Structure at 2.7 Angstrom Resolution of the Paracoccus Denitrificans two-subunit Cytochrome C Oxidase Complexed with an Antibody Fv Fragment

ChemComp-HOH:
WATER

Source
  • human coronavirus oc43
KeywordsVIRAL PROTEIN / spike glycoprotein ectodomain / proline stablized

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