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10.1038/s41594-020-0468-7 http://scihub22266oqcxt.onion/10.1038/s41594-020-0468-7 32647346!7610980!32647346     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=32647346&cmd=llinks): Failed to open stream: HTTP request failed! 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SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects |pdf=|usr=}}{{32647346}} gab.com Text SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects JO: Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=32647346 #FOAvip 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. Twit Text FOAVip SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects ????Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=32647346 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32647346 #FOAvip English Wikipedia <ref>{{Cite pmid|32647346}}</ref> SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects #MMPMID32647346 Wrobel AG; Benton DJ; Xu P; Roustan C; Martin SR; Rosenthal PB; Skehel JJ; Gamblin SJ Nat Struct Mol Biol 2020[Aug]; 27 (8): 763-767 PMID32647346show ga 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. |Angiotensin-Converting Enzyme 2[MESH] |Animals[MESH] |Betacoronavirus/*genetics/metabolism/ultrastructure[MESH] |Binding Sites[MESH] |COVID-19[MESH] |Chiroptera/virology[MESH] |Coronavirus Infections/virology[MESH] |Cryoelectron Microscopy[MESH] |Evolution, Molecular[MESH] |Furin/chemistry[MESH] |Gene Expression[MESH] |HEK293 Cells[MESH] |Host-Pathogen Interactions/*genetics[MESH] |Humans[MESH] |Models, Molecular[MESH] |Pandemics[MESH] |Peptidyl-Dipeptidase A/*chemistry/genetics/metabolism[MESH] |Pneumonia, Viral/virology[MESH] |Protein Binding[MESH] |Protein Conformation, alpha-Helical[MESH] |Protein Conformation, beta-Strand[MESH] |Protein Interaction Domains and Motifs[MESH] |Protein Isoforms/chemistry/genetics/metabolism[MESH] |Protein Stability[MESH] |Proteolysis[MESH] |Receptors, Virus/*chemistry/genetics/metabolism[MESH] |Recombinant Proteins/chemistry/genetics/metabolism[MESH] |SARS-CoV-2[MESH] |Spike Glycoprotein, Coronavirus/*chemistry/genetics/metabolism[MESH]SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on viru(epmc).pdf DeepDyve Pubget Overpricing