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TitleCryo-EM structure of coronavirus-HKU1 haemagglutinin esterase reveals architectural changes arising from prolonged circulation in humans.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 4646, Year 2020
Publish dateSep 16, 2020
AuthorsDaniel L Hurdiss / Ieva Drulyte / Yifei Lang / Tatiana M Shamorkina / Matti F Pronker / Frank J M van Kuppeveld / Joost Snijder / Raoul J de Groot /
PubMed AbstractThe human betacoronaviruses HKU1 and OC43 (subgenus Embecovirus) arose from separate zoonotic introductions, OC43 relatively recently and HKU1 apparently much longer ago. Embecovirus particles ...The human betacoronaviruses HKU1 and OC43 (subgenus Embecovirus) arose from separate zoonotic introductions, OC43 relatively recently and HKU1 apparently much longer ago. Embecovirus particles contain two surface projections called spike (S) and haemagglutinin-esterase (HE), with S mediating receptor binding and membrane fusion, and HE acting as a receptor-destroying enzyme. Together, they promote dynamic virion attachment to glycan-based receptors, specifically 9-O-acetylated sialic acid. Here we present the cryo-EM structure of the ~80 kDa, heavily glycosylated HKU1 HE at 3.4 Å resolution. Comparison with existing HE structures reveals a drastically truncated lectin domain, incompatible with sialic acid binding, but with the structure and function of the esterase domain left intact. Cryo-EM and mass spectrometry analysis reveals a putative glycan shield on the now redundant lectin domain. The findings further our insight into the evolution and host adaptation of human embecoviruses, and demonstrate the utility of cryo-EM for studying small, heavily glycosylated proteins.
External linksNat Commun / PubMed:32938911 / PubMed Central
MethodsEM (single particle)
Resolution3.39 Å
Structure data

EMDB-10676, PDB-6y3y:
Human Coronavirus HKU1 Haemagglutinin-Esterase
Method: EM (single particle) / Resolution: 3.39 Å

Chemicals

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

Source
  • human coronavirus hku1
KeywordsVIRAL PROTEIN / Coronavirus / Glycoprotein / Nidovirus / Esterase

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