دورية أكاديمية
Mutations in the SARS-CoV-2 spike proteins affected the ACE2-binding affinity during the development of Omicron pandemic variants.
العنوان: | Mutations in the SARS-CoV-2 spike proteins affected the ACE2-binding affinity during the development of Omicron pandemic variants. |
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المؤلفون: | Tachibana K; Tokai University School of Medicine, Department of Internal Medicine, Division of Hematology and Oncology, 143 Shimokasuya, Isehara, Kanagawa, Japan. Electronic address: kouichi-tachibana@aist.go.jp., Nakamura Y; Tokai University School of Medicine, Center for Regenerative Medicine, 143 Shimokasuya, Isehara, Kanagawa, Japan., Do TL; The University of Kitakyusyu, Department of Life and Environment Engineering, 1-1 Hibikino, Wakamatu, Kitakyusyu, Fukuoka, Japan., Kihara T; The University of Kitakyusyu, Department of Life and Environment Engineering, 1-1 Hibikino, Wakamatu, Kitakyusyu, Fukuoka, Japan., Kawada H; Tokai University School of Medicine, Department of Internal Medicine, Division of Hematology and Oncology, 143 Shimokasuya, Isehara, Kanagawa, Japan., Yamamoto N; Tokai University School of Medicine, Department of Microbiology, 143 Shimokasuya, Isehara, Kanagawa, Japan., Ando K; Tokai University School of Medicine, Department of Internal Medicine, Division of Hematology and Oncology, 143 Shimokasuya, Isehara, Kanagawa, Japan. |
المصدر: | Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2024 Jul 30; Vol. 719, pp. 150120. Date of Electronic Publication: 2024 May 14. |
نوع المنشور: | Journal Article |
اللغة: | English |
بيانات الدورية: | Publisher: Elsevier Country of Publication: United States NLM ID: 0372516 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1090-2104 (Electronic) Linking ISSN: 0006291X NLM ISO Abbreviation: Biochem Biophys Res Commun Subsets: MEDLINE |
أسماء مطبوعة: | Publication: <2002- >: San Diego, CA : Elsevier Original Publication: New York, Academic Press. |
مواضيع طبية MeSH: | Angiotensin-Converting Enzyme 2*/metabolism , Angiotensin-Converting Enzyme 2*/genetics , Spike Glycoprotein, Coronavirus*/genetics , Spike Glycoprotein, Coronavirus*/metabolism , Spike Glycoprotein, Coronavirus*/chemistry , SARS-CoV-2*/genetics , SARS-CoV-2*/metabolism , Mutation* , Protein Binding* , COVID-19*/virology , COVID-19*/metabolism, Humans ; Animals ; Mice ; Pandemics |
مستخلص: | Mutations in SARS-CoV-2 caused multiple waves of pandemics. To identify the function of such mutations, we investigated the binding affinity of the S protein with its receptor, ACE2. Omicron BA.1 showed significantly lower binding affinity with human ACE2 than prototype SARS-CoV-2 and Alpha strain, indicating that pre-Omicron to Omicron transition was not mediated by increasing the ACE2-binding affinity. Meanwhile, the later Omicron variants, BA.5 and XBB.1.5, showed significantly higher ACE2-binding affinity, suggesting that the increased ACE2-binding could be involved in the variant transition within Omicron strains. Furthermore, Alpha and Omicron variants, but not prototype SARS-CoV-2, bound mouse ACE2, which lead to a hypothesis that early Omicron strains evolved from Alpha strain by acquiring multiple mutations in mice. Competing Interests: Declaration of Competing interest All authors declare that there is no conflict of interest in this study. (Copyright © 2024 Elsevier Inc. All rights reserved.) |
فهرسة مساهمة: | Keywords: ACE2; Binding; Mouse; Omicron; SARS-CoV-2; Spike protein |
المشرفين على المادة: | EC 3.4.17.23 (Angiotensin-Converting Enzyme 2) 0 (Spike Glycoprotein, Coronavirus) 0 (spike protein, SARS-CoV-2) EC 3.4.17.23 (ACE2 protein, human) EC 3.4.17.23 (Ace2 protein, mouse) |
SCR Organism: | SARS-CoV-2 variants |
تواريخ الأحداث: | Date Created: 20240517 Date Completed: 20240603 Latest Revision: 20240611 |
رمز التحديث: | 20240611 |
DOI: | 10.1016/j.bbrc.2024.150120 |
PMID: | 38759524 |
قاعدة البيانات: | MEDLINE |
تدمد: | 1090-2104 |
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DOI: | 10.1016/j.bbrc.2024.150120 |