Structures, conformations and distributions of SARS-CoV-2 spike protein trimers on intact virions
Abstract Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude. Heavily glycosylated S trimers bind the ACE2 receptor and mediate entry of virions into target cells. S exhibits extensive conformational flexibility: it modulates the exposure of its receptor binding site and later undergoes complete structural rearrangement to drive fusion of viral and cellular membranes. The structures and conformations of soluble, overexpressed, purified S proteins have been studied in detail using cryo-electron microscopy. The structure and distribution of S on the virion surface, however, has not been characterised. Here we applied cryo-electron microscopy and tomography to image intact SARS-CoV-2 virions, determining the high-resolution structure, conformational flexibility and distributions of S trimers in situ on the virion surface. These results provide a basis for understanding the conformations of S present on the virion, and for studying their interactions with neutralizing antibodies..
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Preprint| Erscheinungsjahr: |
2020 |
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| Erschienen: |
2020 |
| Enthalten in: |
bioRxiv.org - (2020) vom: 08. Dez. Zur Gesamtaufnahme - year:2020 |
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| Sprache: |
Englisch |
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| Beteiligte Personen: |
Ke, Zunlong [VerfasserIn] |
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| Links: |
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| doi: |
10.1101/2020.06.27.174979 |
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| PPN (Katalog-ID): |
XBI018235034 |
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| 520 | |a Abstract Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude. Heavily glycosylated S trimers bind the ACE2 receptor and mediate entry of virions into target cells. S exhibits extensive conformational flexibility: it modulates the exposure of its receptor binding site and later undergoes complete structural rearrangement to drive fusion of viral and cellular membranes. The structures and conformations of soluble, overexpressed, purified S proteins have been studied in detail using cryo-electron microscopy. The structure and distribution of S on the virion surface, however, has not been characterised. Here we applied cryo-electron microscopy and tomography to image intact SARS-CoV-2 virions, determining the high-resolution structure, conformational flexibility and distributions of S trimers in situ on the virion surface. These results provide a basis for understanding the conformations of S present on the virion, and for studying their interactions with neutralizing antibodies. | ||
| 700 | 1 | |a Oton, Joaquin |e verfasserin |4 aut | |
| 700 | 1 | |a Qu, Kun |e verfasserin |4 aut | |
| 700 | 1 | |a Cortese, Mirko |e verfasserin |4 aut | |
| 700 | 1 | |a Zila, Vojtech |e verfasserin |4 aut | |
| 700 | 1 | |a McKeane, Lesley |e verfasserin |4 aut | |
| 700 | 1 | |a Nakane, Takanori |e verfasserin |4 aut | |
| 700 | 1 | |a Zivanov, Jasenko |e verfasserin |4 aut | |
| 700 | 1 | |a Neufeldt, Christopher J. |e verfasserin |4 aut | |
| 700 | 1 | |a Lu, John M. |e verfasserin |4 aut | |
| 700 | 1 | |a Peukes, Julia |e verfasserin |4 aut | |
| 700 | 1 | |a Xiong, Xiaoli |e verfasserin |4 aut | |
| 700 | 1 | |a Kräusslich, Hans-Georg |e verfasserin |4 aut | |
| 700 | 1 | |a Scheres, Sjors H.W. |e verfasserin |4 aut | |
| 700 | 1 | |a Bartenschlager, Ralf |e verfasserin |4 aut | |
| 700 | 1 | |a Briggs, John A.G. |e verfasserin |4 aut | |
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