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

Human coronavirus-HKU1 contains two surface projections called spike and haemagglutinin-esterase (HE), with the latter acting as a receptor-destroying enzyme. Here, the authors use cryo-EM and mass spectrometry to characterise the small, heavily glycosylated HKU1 HE, revealing a vestigial lectin dom...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Daniel L. Hurdiss, Ieva Drulyte, Yifei Lang, Tatiana M. Shamorkina, Matti F. Pronker, Frank J. M. van Kuppeveld, Joost Snijder, Raoul J. de Groot
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/e39f8123487b43869c78601f60414a16
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:e39f8123487b43869c78601f60414a16
record_format	dspace
spelling	oai:doaj.org-article:e39f8123487b43869c78601f60414a162021-12-02T18:02:24ZCryo-EM structure of coronavirus-HKU1 haemagglutinin esterase reveals architectural changes arising from prolonged circulation in humans10.1038/s41467-020-18440-62041-1723https://doaj.org/article/e39f8123487b43869c78601f60414a162020-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-18440-6https://doaj.org/toc/2041-1723Human coronavirus-HKU1 contains two surface projections called spike and haemagglutinin-esterase (HE), with the latter acting as a receptor-destroying enzyme. Here, the authors use cryo-EM and mass spectrometry to characterise the small, heavily glycosylated HKU1 HE, revealing a vestigial lectin domain covered with a putative glycan shield; and they discuss these features in the context of host adaptation.Daniel L. HurdissIeva DrulyteYifei LangTatiana M. ShamorkinaMatti F. PronkerFrank J. M. van KuppeveldJoost SnijderRaoul J. de GrootNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-10 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Daniel L. Hurdiss Ieva Drulyte Yifei Lang Tatiana M. Shamorkina Matti F. Pronker Frank J. M. van Kuppeveld Joost Snijder Raoul J. de Groot Cryo-EM structure of coronavirus-HKU1 haemagglutinin esterase reveals architectural changes arising from prolonged circulation in humans
description	Human coronavirus-HKU1 contains two surface projections called spike and haemagglutinin-esterase (HE), with the latter acting as a receptor-destroying enzyme. Here, the authors use cryo-EM and mass spectrometry to characterise the small, heavily glycosylated HKU1 HE, revealing a vestigial lectin domain covered with a putative glycan shield; and they discuss these features in the context of host adaptation.
format	article
author	Daniel L. Hurdiss Ieva Drulyte Yifei Lang Tatiana M. Shamorkina Matti F. Pronker Frank J. M. van Kuppeveld Joost Snijder Raoul J. de Groot
author_facet	Daniel L. Hurdiss Ieva Drulyte Yifei Lang Tatiana M. Shamorkina Matti F. Pronker Frank J. M. van Kuppeveld Joost Snijder Raoul J. de Groot
author_sort	Daniel L. Hurdiss
title	Cryo-EM structure of coronavirus-HKU1 haemagglutinin esterase reveals architectural changes arising from prolonged circulation in humans
title_short	Cryo-EM structure of coronavirus-HKU1 haemagglutinin esterase reveals architectural changes arising from prolonged circulation in humans
title_full	Cryo-EM structure of coronavirus-HKU1 haemagglutinin esterase reveals architectural changes arising from prolonged circulation in humans
title_fullStr	Cryo-EM structure of coronavirus-HKU1 haemagglutinin esterase reveals architectural changes arising from prolonged circulation in humans
title_full_unstemmed	Cryo-EM structure of coronavirus-HKU1 haemagglutinin esterase reveals architectural changes arising from prolonged circulation in humans
title_sort	cryo-em structure of coronavirus-hku1 haemagglutinin esterase reveals architectural changes arising from prolonged circulation in humans
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/e39f8123487b43869c78601f60414a16
work_keys_str_mv	AT daniellhurdiss cryoemstructureofcoronavirushku1haemagglutininesteraserevealsarchitecturalchangesarisingfromprolongedcirculationinhumans AT ievadrulyte cryoemstructureofcoronavirushku1haemagglutininesteraserevealsarchitecturalchangesarisingfromprolongedcirculationinhumans AT yifeilang cryoemstructureofcoronavirushku1haemagglutininesteraserevealsarchitecturalchangesarisingfromprolongedcirculationinhumans AT tatianamshamorkina cryoemstructureofcoronavirushku1haemagglutininesteraserevealsarchitecturalchangesarisingfromprolongedcirculationinhumans AT mattifpronker cryoemstructureofcoronavirushku1haemagglutininesteraserevealsarchitecturalchangesarisingfromprolongedcirculationinhumans AT frankjmvankuppeveld cryoemstructureofcoronavirushku1haemagglutininesteraserevealsarchitecturalchangesarisingfromprolongedcirculationinhumans AT joostsnijder cryoemstructureofcoronavirushku1haemagglutininesteraserevealsarchitecturalchangesarisingfromprolongedcirculationinhumans AT raouljdegroot cryoemstructureofcoronavirushku1haemagglutininesteraserevealsarchitecturalchangesarisingfromprolongedcirculationinhumans
_version_	1718378900684275712

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

Ejemplares similares