EMD-34217
Cryo-EM structure of SARS-CoV-2 Omicron BA.2 RBD in complex with rat ACE2 (local refinement)
EMD-34217
Single-particle3.29 Å
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Map released: 19/07/2023
Last modified: 16/10/2024
Sample Organism:
Rattus norvegicus,
Severe acute respiratory syndrome coronavirus 2
Sample: Cryo-EM structure of SARS-CoV-2 Omicron BA.2 RBD in complex with mouse ACE2 (local refinement)
Fitted models: 8gry (Avg. Q-score: 0.425)
Deposition Authors: Zhao ZN, Xie YF, Chai Y, Qi JX, Gao GF
Sample: Cryo-EM structure of SARS-CoV-2 Omicron BA.2 RBD in complex with mouse ACE2 (local refinement)
Fitted models: 8gry (Avg. Q-score: 0.425)
Deposition Authors: Zhao ZN, Xie YF, Chai Y, Qi JX, Gao GF
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Structural basis for receptor binding and broader interspecies receptor recognition of currently circulating Omicron sub-variants.
Zhao Z,
Xie Y
,
Bai B,
Luo C,
Zhou J,
Li W,
Meng Y,
Li L,
Li D,
Li X,
Li X,
Wang X,
Sun J,
Xu Z,
Sun Y
,
Zhang W,
Fan Z,
Zhao X
,
Wu L,
Ma J,
Li OY,
Shang G,
Chai Y,
Liu K
,
Wang P
,
Gao GF
,
Qi J
(2023) Nat Commun , 14 , 4405 - 4405
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(2023) Nat Commun , 14 , 4405 - 4405
Abstract:
Multiple SARS-CoV-2 Omicron sub-variants, such as BA.2, BA.2.12.1, BA.4, and BA.5, emerge one after another. BA.5 has become the dominant strain worldwide. Additionally, BA.2.75 is significantly increasing in some countries. Exploring their receptor binding and interspecies transmission risk is urgently needed. Herein, we examine the binding capacities of human and other 28 animal ACE2 orthologs covering nine orders towards S proteins of these sub-variants. The binding affinities between hACE2 and these sub-variants remain in the range as that of previous variants of concerns (VOCs) or interests (VOIs). Notably, R493Q reverse mutation enhances the bindings towards ACE2s from humans and many animals closely related to human life, suggesting an increased risk of cross-species transmission. Structures of S/hACE2 or RBD/hACE2 complexes for these sub-variants and BA.2 S binding to ACE2 of mouse, rat or golden hamster are determined to reveal the molecular basis for receptor binding and broader interspecies recognition.
Multiple SARS-CoV-2 Omicron sub-variants, such as BA.2, BA.2.12.1, BA.4, and BA.5, emerge one after another. BA.5 has become the dominant strain worldwide. Additionally, BA.2.75 is significantly increasing in some countries. Exploring their receptor binding and interspecies transmission risk is urgently needed. Herein, we examine the binding capacities of human and other 28 animal ACE2 orthologs covering nine orders towards S proteins of these sub-variants. The binding affinities between hACE2 and these sub-variants remain in the range as that of previous variants of concerns (VOCs) or interests (VOIs). Notably, R493Q reverse mutation enhances the bindings towards ACE2s from humans and many animals closely related to human life, suggesting an increased risk of cross-species transmission. Structures of S/hACE2 or RBD/hACE2 complexes for these sub-variants and BA.2 S binding to ACE2 of mouse, rat or golden hamster are determined to reveal the molecular basis for receptor binding and broader interspecies recognition.