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Structure paper

TitleSialoglycan binding triggers spike opening in a human coronavirus.
Journal, issue, pagesNature, Vol. 624, Issue 7990, Page 201-206, Year 2023
Publish dateOct 4, 2023
AuthorsMatti F Pronker / Robert Creutznacher / Ieva Drulyte / Ruben J G Hulswit / Zeshi Li / Frank J M van Kuppeveld / Joost Snijder / Yifei Lang / Berend-Jan Bosch / Geert-Jan Boons / Martin Frank / Raoul J de Groot / Daniel L Hurdiss /
PubMed AbstractCoronavirus spike proteins mediate receptor binding and membrane fusion, making them prime targets for neutralizing antibodies. In the cases of severe acute respiratory syndrome coronavirus, severe ...Coronavirus spike proteins mediate receptor binding and membrane fusion, making them prime targets for neutralizing antibodies. In the cases of severe acute respiratory syndrome coronavirus, severe acute respiratory syndrome coronavirus 2 and Middle East respiratory syndrome coronavirus, spike proteins transition freely between open and closed conformations to balance host cell attachment and immune evasion. Spike opening exposes domain S1, allowing it to bind to proteinaceous receptors, and is also thought to enable protein refolding during membrane fusion. However, with a single exception, the pre-fusion spike proteins of all other coronaviruses studied so far have been observed exclusively in the closed state. This raises the possibility of regulation, with spike proteins more commonly transitioning to open states in response to specific cues, rather than spontaneously. Here, using cryogenic electron microscopy and molecular dynamics simulations, we show that the spike protein of the common cold human coronavirus HKU1 undergoes local and long-range conformational changes after binding a sialoglycan-based primary receptor to domain S1. This binding triggers the transition of S1 domains to the open state through allosteric interdomain crosstalk. Our findings provide detailed insight into coronavirus attachment, with possibilities of dual receptor usage and priming of entry as a means of immune escape.
External linksNature / PubMed:37794193 / PubMed Central
MethodsEM (single particle)
Resolution3.4 - 5.4 Å
Structure data

16882

8ohn

EMDB-16882, PDB-8ohn:
Human Coronavirus HKU1 spike glycoprotein
Method: EM (single particle) / Resolution: 3.4 Å

17076

8opm

EMDB-17076, PDB-8opm:
Human Coronavirus HKU1 spike glycoprotein in complex with an alpha2,8-linked 9-O-acetylated disialoside (closed state)
Method: EM (single particle) / Resolution: 3.7 Å

17077

8opn

EMDB-17077, PDB-8opn:
Human Coronavirus HKU1 spike glycoprotein in complex with an alpha2,8-linked 9-O-acetylated disialoside (1-up state)
Method: EM (single particle) / Resolution: 4.7 Å

17078

8opo

EMDB-17078, PDB-8opo:
Human Coronavirus HKU1 spike glycoprotein in complex with an alpha2,8-linked 9-O-acetylated disialoside (3-up state)
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-17079: Human Coronavirus HKU1 W89A spike glycoprotein incubated with an alpha2,8-linked 9-O-acetylated disialoside (closed state)
Method: EM (single particle) / Resolution: 5.1 Å

EMDB-17080: Local refinement of the Human Coronavirus HKU1 spike glycoprotein
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-17081: Local refinement of the Human Coronavirus HKU1 spike glycoprotein in complex with an alpha2,8-linked 9-O-acetylated disialoside (closed state)
Method: EM (single particle) / Resolution: 4.1 Å

EMDB-17082: Local refinement of the Human Coronavirus HKU1 spike glycoprotein in complex with an alpha2,8-linked 9-O-acetylated disialoside (3-up state)
Method: EM (single particle) / Resolution: 4.2 Å

EMDB-17083: Local refinement of the Human Coronavirus HKU1 W89A spike glycoprotein incubated with an alpha2,8-linked 9-O-acetylated disialoside (closed state)
Method: EM (single particle) / Resolution: 5.4 Å

Chemicals

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

Source
  • human coronavirus hku1
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsVIRAL PROTEIN / Virus / Coronavirus / HKU1 / Spike / Glycoprotein / Membrane fusion

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