Structures and distributions of SARS-CoV-2 spike proteins on intact virions
| Autor: | Hans-Georg Kräusslich, Xiaoli Xiong, Kun Qu, Joaquín Otón, Vojtech Zila, Ralf Bartenschlager, Jasenko Zivanov, Takanori Nakane, Zunlong Ke, Christopher J. Neufeldt, John M. Lu, Lesley McKeane, Mirko Cortese, Sjors H.W. Scheres, John A. G. Briggs, Berati Cerikan, Julia Peukes |
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| Přispěvatelé: | Ke, Z., Oton, J., Qu, K., Cortese, M., Zila, V., Mckeane, L., Nakane, T., Zivanov, J., Neufeldt, C. J., Cerikan, B., Lu, J. M., Peukes, J., Xiong, X., Krausslich, H. -G., Scheres, S. H. W., Bartenschlager, R., Briggs, J. A. G. |
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
viruses Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Pneumonia Viral Article Betacoronavirus 03 medical and health sciences 0302 clinical medicine Protein structure Humans Receptor Lipid bilayer Pandemics chemistry.chemical_classification Multidisciplinary biology SARS-CoV-2 Chemistry Cryoelectron Microscopy Virion COVID-19 Spike Protein biochemical phenomena metabolism and nutrition 3. Good health 030104 developmental biology Enzyme Cell culture Spike Glycoprotein Coronavirus Biophysics biology.protein Antibody Coronavirus Infections 030217 neurology & neurosurgery |
| Zdroj: | Nature |
| ISSN: | 0028-0836 |
| DOI: | 10.1038/s41586-020-2665-2 |
| Popis: | Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude1. Heavily glycosylated S trimers bind to the angiotensin-converting enzyme 2 receptor and mediate entry of virions into target cells2–6. S exhibits extensive conformational flexibility: it modulates exposure of its receptor-binding site and subsequently undergoes complete structural rearrangement to drive fusion of viral and cellular membranes2,7,8. The structures and conformations of soluble, overexpressed, purified S proteins have been studied in detail using cryo-electron microscopy2,7,9–12, but the structure and distribution of S on the virion surface remain unknown. Here we applied cryo-electron microscopy and tomography to image intact SARS-CoV-2 virions and determine the high-resolution structure, conformational flexibility and distribution of S trimers in situ on the virion surface. These results reveal the conformations of S on the virion, and provide a basis from which to understand interactions between S and neutralizing antibodies during infection or vaccination. Cryo-electron microscopy and tomography studies reveal the structures, conformations and distributions of spike protein trimers on intact severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions and provide a basis for understanding the interactions of the spike protein with neutralizing antibodies. |
| Databáze: | OpenAIRE |
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