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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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Apart from that, all subvariants except BA.1 have additional mutations such as T19I, A27S, V213G, S371F, T376A, D405N and R408S. |
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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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S |
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Standardized Encoding Gene
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S
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Genotype/Subtype
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BA.1 |
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Viral Reference
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MN908947.3
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Functional Impact and Mechanisms
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Disease
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COVID-19
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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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South Korea |
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Literature Information
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PMID
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38003257
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Title
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Comparative Computational Analysis of Spike Protein Structural Stability in SARS-CoV-2 Omicron Subvariants
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Author
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Balupuri A,Kim JM,Choi KE,No JS,Kim IH,Rhee JE,Kim EJ,Kang NS
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Journal
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International journal of molecular sciences
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Journal Info
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2023 Nov 8;24(22):16069
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Abstract
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The continuous emergence of new severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants with multiple spike (S) protein mutations pose serious threats to current coronavirus disease 2019 (COVID-19) therapies. A comprehensive understanding of the structural stability of SARS-CoV-2 variants is vital for the development of effective therapeutic strategies as it can offer valuable insights into their potential impact on viral infectivity. S protein mediates a virus' attachment to host cells by binding to angiotensin-converting enzyme 2 (ACE2) through its receptor-binding domain (RBD), and mutations in this protein can affect its stability and binding affinity. We analyzed S protein structural stability in various Omicron subvariants computationally. Notably, the S protein sequences analyzed in this work were obtained directly from our own sample collection. We evaluated the binding free energy between S protein and ACE2 in several complex forms. Additionally, we measured distances between the RBD of each chain in S protein to analyze conformational changes. Unlike most of the prior studies, we analyzed full-length S protein-ACE2 complexes instead of only RBD-ACE2 complexes. Omicron subvariants including BA.1, BA.2, BA.2.12.1, BA.4/BA.5, BA.2.75, BA.2.75_K147E, BA.4.6 and BA.4.6_N658S showed enhanced stability compared to wild type, potentially due to distinct S protein mutations. Among them, BA.2.75 and BA.4.6_N658S exhibited the highest and lowest level of stability, respectively.
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Sequence Data
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EPI_ISL_8885887;13086512;13086514;13086515;13086516;14507613;14780352
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