EMD-27205
Closed state of SARS-CoV-2 BA.2 variant spike protein
EMD-27205
Single-particle2.8 Å
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Map released: 07/06/2023
Last modified: 06/11/2024
Sample Organism:
Severe acute respiratory syndrome coronavirus 2
Sample: Closed state of pre-fusion SARS-CoV-2 BA.2 variant spike protein
Fitted models: 8d55 (Avg. Q-score: 0.434)
Deposition Authors: Zhang J
,
Tang WC,
Gao HL,
Shi W
,
Peng HQ,
Volloch SR,
Xiao TS,
Chen B
Sample: Closed state of pre-fusion SARS-CoV-2 BA.2 variant spike protein
Fitted models: 8d55 (Avg. Q-score: 0.434)
Deposition Authors: Zhang J
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Structural and functional characteristics of the SARS-CoV-2 Omicron subvariant BA.2 spike protein.
Zhang J
,
Tang W,
Gao H,
Lavine CL,
Shi W
,
Peng H
,
Zhu H
,
Anand K,
Kosikova M,
Kwon HJ,
Tong P,
Gautam A
,
Rits-Volloch S,
Wang S,
Mayer ML,
Wesemann DR,
Seaman MS,
Lu J,
Xiao T
,
Xie H
,
Chen B
(2023) Nat Struct Mol Biol , 30 , 980 - 990
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(2023) Nat Struct Mol Biol , 30 , 980 - 990
Abstract:
The Omicron subvariant BA.2 has become the dominant circulating strain of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) in many countries. Here, we have characterized structural, functional and antigenic properties of the full-length BA.2 spike (S) protein and compared replication of the authentic virus in cell culture and an animal model with previously prevalent variants. BA.2 S can fuse membranes slightly more efficiently than Omicron BA.1, but still less efficiently than other previous variants. Both BA.1 and BA.2 viruses replicated substantially faster in animal lungs than the early G614 (B.1) strain in the absence of pre-existing immunity, possibly explaining the increased transmissibility despite their functionally compromised spikes. As in BA.1, mutations in the BA.2 S remodel its antigenic surfaces, leading to strong resistance to neutralizing antibodies. These results suggest that both immune evasion and replicative advantage may contribute to the heightened transmissibility of the Omicron subvariants.
The Omicron subvariant BA.2 has become the dominant circulating strain of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) in many countries. Here, we have characterized structural, functional and antigenic properties of the full-length BA.2 spike (S) protein and compared replication of the authentic virus in cell culture and an animal model with previously prevalent variants. BA.2 S can fuse membranes slightly more efficiently than Omicron BA.1, but still less efficiently than other previous variants. Both BA.1 and BA.2 viruses replicated substantially faster in animal lungs than the early G614 (B.1) strain in the absence of pre-existing immunity, possibly explaining the increased transmissibility despite their functionally compromised spikes. As in BA.1, mutations in the BA.2 S remodel its antigenic surfaces, leading to strong resistance to neutralizing antibodies. These results suggest that both immune evasion and replicative advantage may contribute to the heightened transmissibility of the Omicron subvariants.