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10.1038/s41467-020-16876-4 http://scihub22266oqcxt.onion/10.1038/s41467-020-16876-4 32555182!7300015!32555182     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=32555182&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       Nat+Commun 2020 ; 11 (1): 3070 Nephropedia Template TP {{tp|p=32555182|t=2020. Cryo-EM structures of HKU2 and SADS-CoV spike glycoproteins provide insights into coronavirus evolution |pdf=|usr=}}{{32555182}} gab.com Text Cryo-EM structures of HKU2 and SADS-CoV spike glycoproteins provide insights into coronavirus evolution JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=32555182 #FOAvip Porcine coronavirus SADS-CoV has been identified from suckling piglets with severe diarrhea in southern China in 2017. The SADS-CoV genome shares ~95% identity to that of bat alpha-coronavirus HKU2, suggesting that SADS-CoV may have emerged from a natural reservoir in bats. Here we report the cryo-EM structures of HKU2 and SADS-CoV spike (S) glycoprotein trimers at 2.38 A and 2.83 A resolution, respectively. We systematically compare the domains of HKU2 spike with those of alpha-, beta-, gamma-, and delta-coronavirus spikes, showing that the S1 subunit N- and C-terminal domains of HKU2/SADS-CoV are ancestral domains in the evolution of coronavirus spike proteins. The connecting region after the fusion peptide in the S2 subunit of HKU2/SADS-CoV adopts a unique conformation. These results structurally demonstrate a close evolutionary relationship between HKU2/SADS-CoV and beta-coronavirus spikes and provide insights into the evolution and cross-species transmission of coronaviruses. Twit Text FOAVip Cryo-EM structures of HKU2 and SADS-CoV spike glycoproteins provide insights into coronavirus evolution ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=32555182 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32555182 #FOAvip English Wikipedia <ref>{{Cite pmid|32555182}}</ref> Cryo-EM structures of HKU2 and SADS-CoV spike glycoproteins provide insights into coronavirus evolution #MMPMID32555182 Yu J; Qiao S; Guo R; Wang X Nat Commun 2020[Jun]; 11 (1): 3070 PMID32555182show ga Porcine coronavirus SADS-CoV has been identified from suckling piglets with severe diarrhea in southern China in 2017. The SADS-CoV genome shares ~95% identity to that of bat alpha-coronavirus HKU2, suggesting that SADS-CoV may have emerged from a natural reservoir in bats. Here we report the cryo-EM structures of HKU2 and SADS-CoV spike (S) glycoprotein trimers at 2.38 A and 2.83 A resolution, respectively. We systematically compare the domains of HKU2 spike with those of alpha-, beta-, gamma-, and delta-coronavirus spikes, showing that the S1 subunit N- and C-terminal domains of HKU2/SADS-CoV are ancestral domains in the evolution of coronavirus spike proteins. The connecting region after the fusion peptide in the S2 subunit of HKU2/SADS-CoV adopts a unique conformation. These results structurally demonstrate a close evolutionary relationship between HKU2/SADS-CoV and beta-coronavirus spikes and provide insights into the evolution and cross-species transmission of coronaviruses. |Alphacoronavirus/*chemistry[MESH] |Animals[MESH] |Cell Line[MESH] |Chiroptera[MESH] |Coronavirus Infections[MESH] |Cryoelectron Microscopy[MESH] |Evolution, Molecular[MESH] |Glycoproteins/ultrastructure[MESH] |Humans[MESH] |Models, Molecular[MESH] |Protein Domains[MESH] |Spike Glycoprotein, Coronavirus/*ultrastructure[MESH]Cryo-EM structures of HKU2 and SADS-CoV spike glycoproteins provide in(epmc).pdf DeepDyve Pubget Overpricing