9OVN
Cryo-EM structure of HCoV-OC43-C2 Spike glycoprotein
Summary for 9OVN
| Entry DOI | 10.2210/pdb9ovn/pdb |
| Related | 9OVM |
| EMDB information | 70903 |
| Descriptor | Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | spike glycoprotein ectodomain, proline stablized, viral protein |
| Biological source | Human coronavirus OC43 |
| Total number of polymer chains | 3 |
| Total formula weight | 460711.30 |
| Authors | |
| Primary citation | Hassan, Z.,Jin, M.,Liu, Y.,Li, Z.,Wong, A.H.M.,Desforges, M.,Forman, A.,Nitz, M.,Gunawardena, T.,Moraes, T.J.,Narimatsu, M.,Wrana, J.L.,Yu, H.,Chen, X.,Rini, J.M. OC43 clinical isolate spike proteins have distinct carbohydrate-binding properties. Nat Commun, 2026 Cited by PubMed Abstract: 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. PubMed: 42143065DOI: 10.1038/s41467-026-73186-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (1.93 Å) |
Structure validation
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