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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
PMID32555182
show 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 ?-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?Å and 2.83?Å
resolution, respectively. We systematically compare the domains of HKU2 spike
with those of ?-, ?-, ?-, and ?-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 ?-coronavirus spikes and provide insights into the evolution and
cross-species transmission of coronaviruses.