National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
United States
Citation
Journal: Cell Rep / Year: 2022 Title: Cryo-EM structures of SARS-CoV-2 Omicron BA.2 spike. Authors: Victoria Stalls / Jared Lindenberger / Sophie M-C Gobeil / Rory Henderson / Rob Parks / Maggie Barr / Margaret Deyton / Mitchell Martin / Katarzyna Janowska / Xiao Huang / Aaron May / Micah ...Authors: Victoria Stalls / Jared Lindenberger / Sophie M-C Gobeil / Rory Henderson / Rob Parks / Maggie Barr / Margaret Deyton / Mitchell Martin / Katarzyna Janowska / Xiao Huang / Aaron May / Micah Speakman / Esther Beaudoin / Bryan Kraft / Xiaozhi Lu / Robert J Edwards / Amanda Eaton / David C Montefiori / Wilton B Williams / Kevin O Saunders / Kevin Wiehe / Barton F Haynes / Priyamvada Acharya / Abstract: The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron BA.2 sub-lineage has gained in proportion relative to BA.1. Because spike (S) protein variations may underlie differences in ...The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron BA.2 sub-lineage has gained in proportion relative to BA.1. Because spike (S) protein variations may underlie differences in their pathobiology, here we determine cryoelectron microscopy (cryo-EM) structures of the BA.2 S ectodomain and compare these with previously determined BA.1 S structures. BA.2 receptor-binding domain (RBD) mutations induce remodeling of the RBD structure, resulting in tighter packing and improved thermostability. Interprotomer RBD interactions are enhanced in the closed (or 3-RBD-down) BA.2 S, while the fusion peptide is less accessible to antibodies than in BA.1. Binding and pseudovirus neutralization assays reveal extensive immune evasion while defining epitopes of two outer RBD face-binding antibodies, DH1044 and DH1193, that neutralize both BA.1 and BA.2. Taken together, our results indicate that stabilization of the closed state through interprotomer RBD-RBD packing is a hallmark of the Omicron variant and show differences in key functional regions in the BA.1 and BA.2 S proteins.
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