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Basic Characteristics of Mutations
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Mutation Site
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D405N |
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Mutation Site Sentence
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The difference between the BA.2 RBD and the BA.1 RBD is that BA.2 contains S371F, T376A, D405N, and R408S mutations, but BA.1 RBD does not, whereas BA.1 contains the G446S and G496S mutations, but BA.2 does not. |
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Mutation Level
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Amino acid level |
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Mutation Type
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Nonsynonymous substitution |
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Gene/Protein/Region
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RBD |
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Standardized Encoding Gene
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S
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Genotype/Subtype
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BA.2 |
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Viral Reference
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EPI_ISL_402119;EPI_ISL_683466;EPI_ISL_678615;EPI_ISL_833172;EPI_ISL_2020954;EPI_ISL_6640916;EPI_ISL_ 496747;EPI_ISL_9845731;EPI_ISL_7605713;NP_001358344
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Functional Impact and Mechanisms
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Disease
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-
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Immune
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- |
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Target Gene
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-
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Clinical and Epidemiological Correlations
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Clinical Information
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- |
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Treatment
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- |
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Location
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- |
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Literature Information
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PMID
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35809570
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Title
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Structural basis of human ACE2 higher binding affinity to currently circulating Omicron SARS-CoV-2 sub-variants BA.2 and BA.1.1
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Author
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Li L,Liao H,Meng Y,Li W,Han P,Liu K,Wang Q,Li D,Zhang Y,Wang L,Fan Z,Zhang Y,Wang Q,Zhao X,Sun Y,Huang N,Qi J,Gao GF
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Journal
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Cell
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Journal Info
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2022 Aug 4;185(16):2952-2960
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Abstract
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The currently circulating Omicron sub-variants are the SARS-CoV-2 strains with the highest number of known mutations. Herein, we found that human angiotensin-converting enzyme 2 (hACE2) binding affinity to the receptor-binding domains (RBDs) of the four early Omicron sub-variants (BA.1, BA.1.1, BA.2, and BA.3) follows the order BA.1.1 > BA.2 > BA.3 approximately BA.1. The complex structures of hACE2 with RBDs of BA.1.1, BA.2, and BA.3 reveal that the higher hACE2 binding affinity of BA.2 than BA.1 is related to the absence of the G496S mutation in BA.2. The R346K mutation in BA.1.1 majorly affects the interaction network in the BA.1.1 RBD/hACE2 interface through long-range alterations and contributes to the higher hACE2 affinity of the BA.1.1 RBD than the BA.1 RBD. These results reveal the structural basis for the distinct hACE2 binding patterns among BA.1.1, BA.2, and BA.3 RBDs.
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Sequence Data
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-
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