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TitleCetacean coronavirus spikes highlight S glycoprotein structural plasticity.
Journal, issue, pagesPLoS Pathog, Vol. 22, Issue 4, Page e1013855, Year 2026
Publish dateApr 8, 2026
AuthorsRuben J G Hulswit / Tatiana M Shamorkina / Joline van der Lee / Floor Rosman / Lisanne S Wetzels / Frank J M van Kuppeveld / Joost Snijder / Berend Jan Bosch / Daniel L Hurdiss /
PubMed AbstractCoronaviruses (CoVs) exhibit a remarkable ability for spill-over infections into naive host populations. While much research has focused on the spike (S) glycoproteins of zoonotic alpha- and ...Coronaviruses (CoVs) exhibit a remarkable ability for spill-over infections into naive host populations. While much research has focused on the spike (S) glycoproteins of zoonotic alpha- and betacoronaviruses, the S proteins of gamma- and deltacoronaviruses, which predominantly infect avian hosts, remain poorly understood. Here, we present high-resolution cryo-EM structures of S proteins from two distinct gammacoronaviruses (75.7% sequence identity) that atypically infect marine mammals and belong to the Gammacoronavirus delphinapteri species. The cryo-EM reconstructions reveal that the spikes exhibit a unique quaternary architecture that distinguishes them from other coronaviruses. The S protein features a previously unidentified, tripodal quaternary assembly of the S1 subunit, in which S1B domains are presented in an upright position while their putative receptor binding sites are shielded by extended loops from the S1A domain of the same protomers. Additionally, the CeCoV spike proteins have evolved an additional and unique ~200 residue N-terminal domain (S10). S10 lacks homology to known protein sequences but displays structural similarity to members of the cupin protein superfamily. This represents a remarkable case of coronaviral exaptation of a host protein integrated into the S glycoprotein. Moreover, glycoproteomic analyses reveal that CeCoV S proteins are extensively N-glycosylated (>100 N-glycans per trimer), with a notable abundance of high-mannose glycans on S10 and O-glycosylation sites within a mucin-like loop at the trimer apex, all contributing to a dense glycan shield and potentially masking immunogenic epitopes. These findings demonstrate the structural diversity and adaptability of CoV S proteins, including alternative quaternary assemblies, additional domains, and diverse glycosylation strategies, offering new insights into the evolutionary mechanisms that enable coronaviruses to expand their host range and establish infections in novel species.
External linksPLoS Pathog / PubMed:41950284 / PubMed Central
MethodsEM (single particle)
Resolution2.24 - 2.65 Å
Structure data

53512

9r1q

EMDB-53512, PDB-9r1q:
Beluga whale coronavirus spike glycoprotein
Method: EM (single particle) / Resolution: 2.24 Å

53513

9r1r

EMDB-53513, PDB-9r1r:
Bottlenose dolphin coronavirus spike glycoprotein
Method: EM (single particle) / Resolution: 2.65 Å

Chemicals

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

Source
  • beluga whale coronavirus sw1
  • bottlenose dolphin coronavirus hku22
KeywordsVIRAL PROTEIN / spike / glycoprotein / coronavirus

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