Cryo-EM structure of coronavirus-HKU1 haemagglutinin esterase reveals architectural changes arising from prolonged circulation in humans

Daniel L. Hurdiss (), Ieva Drulyte, Yifei Lang, Tatiana M. Shamorkina, Matti F. Pronker, Frank J. M. Kuppeveld, Joost Snijder and Raoul J. Groot ()
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Daniel L. Hurdiss: Utrecht University
Ieva Drulyte: Thermo Fisher Scientific
Yifei Lang: Utrecht University
Tatiana M. Shamorkina: Utrecht University
Matti F. Pronker: Utrecht University
Frank J. M. Kuppeveld: Utrecht University
Joost Snijder: Utrecht University
Raoul J. Groot: Utrecht University

Nature Communications, 2020, vol. 11, issue 1, 1-10

Abstract: Abstract 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.

Date: 2020
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DOI: 10.1038/s41467-020-18440-6

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