RT Journal Article
SR Electronic
T1 Structural diversity of the SARS-CoV-2 Omicron spike
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2022.01.25.477784
DO 10.1101/2022.01.25.477784
A1 Gobeil, Sophie M-C.
A1 Henderson, Rory
A1 Stalls, Victoria
A1 Janowska, Katarzyna
A1 Huang, Xiao
A1 May, Aaron
A1 Speakman, Micah
A1 Beaudoin, Esther
A1 Manne, Kartik
A1 Li, Dapeng
A1 Parks, Rob
A1 Barr, Maggie
A1 Deyton, Margaret
A1 Martin, Mitchell
A1 Mansouri, Katayoun
A1 Edwards, Robert J.
A1 Sempowski, Gregory D.
A1 Saunders, Kevin O.
A1 Wiehe, Kevin
A1 Williams, Wilton
A1 Korber, Bette
A1 Haynes, Barton F.
A1 Acharya, Priyamvada
YR 2022
UL http://biorxiv.org/content/early/2022/01/26/2022.01.25.477784.abstract
AB Aided by extensive spike protein mutation, the SARS-CoV-2 Omicron variant overtook the previously dominant Delta variant. Spike conformation plays an essential role in SARS-CoV-2 evolution via changes in receptor binding domain (RBD) and neutralizing antibody epitope presentation affecting virus transmissibility and immune evasion. Here, we determine cryo-EM structures of the Omicron and Delta spikes to understand the conformational impacts of mutations in each. The Omicron spike structure revealed an unusually tightly packed RBD organization with long range impacts that were not observed in the Delta spike. Binding and crystallography revealed increased flexibility at the functionally critical fusion peptide site in the Omicron spike. These results reveal a highly evolved Omicron spike architecture with possible impacts on its high levels of immune evasion and transmissibility.Competing Interest StatementB.F.H., G.D.S., and K.O.S., have patents submitted on the SARS-CoV-2 monoclonal antibodies studied in this paper. Other authors declare no competing interests.