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N-linked glycosylation of recombinant soluble ectodomain of HKU1 haemagglutinin esterase

ABSTRACT: Coronaviruses (CoVs) encompass many human pathogens such as HKU-1, OC43, NL63, SARS, MERS and, most recently, nCoV-2019. The spike (S) protein of CoVs has received much attention for its role in host tropism and immunity, but it is becoming increasingly clear that the haemagglutinin esterase (HE) also plays an important role in host adaptation by determining host receptor (sialic acid) specificity. We determined the structure of HKU1 HE by cryo electron microscopy and mapped site-specific N-linked glycosylation by LC-MS/MS of glycopeptides using electron transfer high-energy collision dissociation.

INSTRUMENT(S): Orbitrap Fusion ETD

ORGANISM(S): Human Coronavirus Hku1

SUBMITTER: Joost Snijder

LAB HEAD: Joost Snijder

PROVIDER: PXD017545 | Pride | 2020-07-24

REPOSITORIES: Pride

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

Hurdiss Daniel L DL Drulyte Ieva I Lang Yifei Y Shamorkina Tatiana M TM Pronker Matti F MF van Kuppeveld Frank J M FJM Snijder Joost J de Groot Raoul J RJ

Nature communications 20200916 1

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 ...[more]

PMID: 32938911

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