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SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects

Nature structural & molecular biology, 2020-08, Vol.27 (8), p.763-767 [Peer Reviewed Journal]

COPYRIGHT 2020 Nature Publishing Group ;The Author(s), under exclusive licence to Springer Nature America, Inc. 2020. ;ISSN: 1545-9993 ;EISSN: 1545-9985 ;DOI: 10.1038/s41594-020-0468-7 ;PMID: 32647346

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Title:
SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects
Author: Wrobel, Antoni G ; Benton, Donald J ; Xu, Pengqi ; Roustan, Chloë ; Martin, Stephen R ; Rosenthal, Peter B ; Skehel, John J ; Gamblin, Steven J
Subjects: ACE2 ; Angiotensin-Converting Enzyme 2 ; Animals ; Bats ; Betacoronavirus - genetics ; Betacoronavirus - metabolism ; Betacoronavirus - ultrastructure ; Binding ; Binding Sites ; Chiroptera - virology ; Cleavage ; Comparative analysis ; Coronavirus Infections - virology ; Coronaviruses ; COVID-19 ; Cryoelectron Microscopy ; Evolution, Molecular ; Furin ; Furin - chemistry ; Gene Expression ; Glycoproteins ; HEK293 Cells ; Host-Pathogen Interactions - genetics ; Host-virus relationships ; Humans ; Models, Molecular ; Pandemics ; Peptidyl-Dipeptidase A - chemistry ; Peptidyl-Dipeptidase A - genetics ; Peptidyl-Dipeptidase A - metabolism ; Physiological aspects ; Pneumonia, Viral - virology ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Interaction Domains and Motifs ; Protein Isoforms - chemistry ; Protein Isoforms - genetics ; Protein Isoforms - metabolism ; Protein Stability ; Proteins ; Proteolysis ; Receptors ; Receptors, Virus - chemistry ; Receptors, Virus - genetics ; Receptors, Virus - metabolism ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; SARS-CoV-2 ; Severe acute respiratory syndrome ; Severe acute respiratory syndrome coronavirus 2 ; Spike glycoprotein ; Spike Glycoprotein, Coronavirus - chemistry ; Spike Glycoprotein, Coronavirus - genetics ; Spike Glycoprotein, Coronavirus - metabolism ; Stability ; Structural Homology, Protein ; Structure ; Virus research ; Viruses
Is Part Of: Nature structural & molecular biology, 2020-08, Vol.27 (8), p.763-767
Description: SARS-CoV-2 is thought to have emerged from bats, possibly via a secondary host. Here, we investigate the relationship of spike (S) glycoprotein from SARS-CoV-2 with the S protein of a closely related bat virus, RaTG13. We determined cryo-EM structures for RaTG13 S and for both furin-cleaved and uncleaved SARS-CoV-2 S; we compared these with recently reported structures for uncleaved SARS-CoV-2 S. We also biochemically characterized their relative stabilities and affinities for the SARS-CoV-2 receptor ACE2. Although the overall structures of human and bat virus S proteins are similar, there are key differences in their properties, including a more stable precleavage form of human S and about 1,000-fold tighter binding of SARS-CoV-2 to human receptor. These observations suggest that cleavage at the furin-cleavage site decreases the overall stability of SARS-CoV-2 S and facilitates the adoption of the open conformation that is required for S to bind to the ACE2 receptor.
Publisher: United States: Nature Publishing Group
Language: English
Identifier: ISSN: 1545-9993
EISSN: 1545-9985
DOI: 10.1038/s41594-020-0468-7
PMID: 32647346
Source: MEDLINE
ProQuest Central

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SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects

COPYRIGHT 2020 Nature Publishing Group ;The Author(s), under exclusive licence to Springer Nature America, Inc. 2020. ;ISSN: 1545-9993 ;EISSN: 1545-9985 ;DOI: 10.1038/s41594-020-0468-7 ;PMID: 32647346

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