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10.1038/s41467-022-28768-w http://scihub22266oqcxt.onion/10.1038/s41467-022-28768-w 35246509!8897445!35246509     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\35246509.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Nat+Commun 2022 ; 13 (1): 1178 Nephropedia Template TP {{tp|p=35246509|t=2022. Evolution of the SARS-CoV-2 spike protein in the human host |pdf=|usr=}}{{35246509}} gab.com Text Evolution of the SARS-CoV-2 spike protein in the human host JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=35246509 #FOAvip Recently emerged variants of SARS-CoV-2 contain in their surface spike glycoproteins multiple substitutions associated with increased transmission and resistance to neutralising antibodies. We have examined the structure and receptor binding properties of spike proteins from the B.1.1.7 (Alpha) and B.1.351 (Beta) variants to better understand the evolution of the virus in humans. Spikes of both variants have the same mutation, N501Y, in the receptor-binding domains. This substitution confers tighter ACE2 binding, dependent on the common earlier substitution, D614G. Each variant spike has acquired other key changes in structure that likely impact virus pathogenesis. The spike from the Alpha variant is more stable against disruption upon binding ACE2 receptor than all other spikes studied. This feature is linked to the acquisition of a more basic substitution at the S1-S2 furin site (also observed for the variants of concern Delta, Kappa, and Omicron) which allows for near-complete cleavage. In the Beta variant spike, the presence of a new substitution, K417N (also observed in the Omicron variant), in combination with the D614G, stabilises a more open spike trimer, a conformation required for receptor binding. Our observations suggest ways these viruses have evolved to achieve greater transmissibility in humans. Twit Text FOAVip Evolution of the SARS-CoV-2 spike protein in the human host ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=35246509 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=35246509 #FOAvip English Wikipedia <ref>{{Cite pmid|35246509}}</ref> Evolution of the SARS-CoV-2 spike protein in the human host #MMPMID35246509 Wrobel AG; Benton DJ; Roustan C; Borg A; Hussain S; Martin SR; Rosenthal PB; Skehel JJ; Gamblin SJ Nat Commun 2022[Mar]; 13 (1): 1178 PMID35246509show ga Recently emerged variants of SARS-CoV-2 contain in their surface spike glycoproteins multiple substitutions associated with increased transmission and resistance to neutralising antibodies. We have examined the structure and receptor binding properties of spike proteins from the B.1.1.7 (Alpha) and B.1.351 (Beta) variants to better understand the evolution of the virus in humans. Spikes of both variants have the same mutation, N501Y, in the receptor-binding domains. This substitution confers tighter ACE2 binding, dependent on the common earlier substitution, D614G. Each variant spike has acquired other key changes in structure that likely impact virus pathogenesis. The spike from the Alpha variant is more stable against disruption upon binding ACE2 receptor than all other spikes studied. This feature is linked to the acquisition of a more basic substitution at the S1-S2 furin site (also observed for the variants of concern Delta, Kappa, and Omicron) which allows for near-complete cleavage. In the Beta variant spike, the presence of a new substitution, K417N (also observed in the Omicron variant), in combination with the D614G, stabilises a more open spike trimer, a conformation required for receptor binding. Our observations suggest ways these viruses have evolved to achieve greater transmissibility in humans. |*Mutation, Missense[MESH] |Angiotensin-Converting Enzyme 2/chemistry/*metabolism/ultrastructure[MESH] |Binding Sites/genetics[MESH] |COVID-19/*metabolism/transmission/virology[MESH] |Cryoelectron Microscopy[MESH] |Cytopathogenic Effect, Viral/genetics[MESH] |Evolution, Molecular[MESH] |Host-Pathogen Interactions[MESH] |Humans[MESH] |Kinetics[MESH] |Models, Molecular[MESH] |Protein Binding[MESH] |Protein Domains[MESH] |SARS-CoV-2/*genetics/metabolism/physiology[MESH]Evolution of the SARS-CoV-2 spike protein in the human host (epmc).pdf DeepDyve Pubget Overpricing