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10.1038/s41467-020-16876-4

http://scihub22266oqcxt.onion/10.1038/s41467-020-16876-4
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32555182!7300015!32555182
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suck abstract from ncbi


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pmid32555182      Nat+Commun 2020 ; 11 (1): 3070
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  • 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]


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