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Structural diversity of the SARS-CoV-2 Omicron spike.
<div class='caption-title'>Conformational diversity of the SARS-CoV-2 Omicron (B.1.1.529) S protein</div>
<div class='caption-title'>Intra-protomer communication through the NTD-to-RBD (N2R) linker</div>
Gobeil SM, Henderson R, Stalls V, Janowska K, Huang X, May A, Speakman M, Beaudoin E, Manne K, Li D, Parks R, Barr M, Deyton M, Martin M, Mansouri K, Edwards RJ, Eaton A, Montefiori DC, Sempowski GD, Saunders KO, Wiehe K, Williams W, Korber B, Haynes BF, Acharya P
OpenAccess logo Mol Cell 82 2050-2068.e6 (2022)

Cited: 87 times
EuropePMC logo PMID: 35447081

Abstract

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.

Reviews - 7tou mentioned but not cited (1)

  1. Evolution of the SARS-CoV-2 Omicron spike. Parsons RJ, Acharya P. Cell Rep 42 113444 (2023)

Articles - 7tou mentioned but not cited (3)

  1. Structural diversity of the SARS-CoV-2 Omicron spike. Gobeil SM, Henderson R, Stalls V, Janowska K, Huang X, May A, Speakman M, Beaudoin E, Manne K, Li D, Parks R, Barr M, Deyton M, Martin M, Mansouri K, Edwards RJ, Eaton A, Montefiori DC, Sempowski GD, Saunders KO, Wiehe K, Williams W, Korber B, Haynes BF, Acharya P. Mol Cell 82 2050-2068.e6 (2022)
  2. Cryo-EM structures of SARS-CoV-2 Omicron BA.2 spike. Stalls V, Lindenberger J, Gobeil SM, Henderson R, Parks R, Barr M, Deyton M, Martin M, Janowska K, Huang X, May A, Speakman M, Beaudoin E, Kraft B, Lu X, Edwards RJ, Eaton A, Montefiori DC, Williams WB, Saunders KO, Wiehe K, Haynes BF, Acharya P. Cell Rep 39 111009 (2022)
  3. Progressive membrane-binding mechanism of SARS-CoV-2 variant spike proteins. Overduin M, Kervin TA, Tran A. iScience 25 104722 (2022)


Reviews citing this publication (10)

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  2. Omicron variant (B.1.1.529) and its sublineages: What do we know so far amid the emergence of recombinant variants of SARS-CoV-2? Dhawan M, Saied AA, Mitra S, Alhumaydhi FA, Emran TB, Wilairatana P. Biomed Pharmacother 154 113522 (2022)
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  5. Distinct Conformations of SARS-CoV-2 Omicron Spike Protein and Its Interaction with ACE2 and Antibody. Lee M, Major M, Hong H. Int J Mol Sci 24 3774 (2023)
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Articles citing this publication (73)

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