Reference - Detail
| RRC ID | 80098 |
|---|---|
| Author | Tachibana K, Nakamura Y, Do TL, Kihara T, Kawada H, Yamamoto N, Ando K. |
| Title | Mutations in the SARS-cov-2 spike proteins affected the ACE2-binding affinity during the development of omicron pandemic variants. |
| Journal | Biochem Biophys Res Commun |
| Abstract |
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. |
| Volume | 719 |
| Pages | 150120 |
| Published | 2024-5-14 |
| DOI | 10.1016/j.bbrc.2024.150120 |
| PII | S0006-291X(24)00656-9 |
| PMID | 38759524 |
| MeSH | Angiotensin-Converting Enzyme 2* / genetics Angiotensin-Converting Enzyme 2* / metabolism Animals COVID-19* / metabolism COVID-19* / virology Humans Mice Mutation* Pandemics Protein Binding* SARS-CoV-2* / genetics SARS-CoV-2* / metabolism Spike Glycoprotein, Coronavirus* / chemistry Spike Glycoprotein, Coronavirus* / genetics Spike Glycoprotein, Coronavirus* / metabolism |
| Resource | |
| Human and Animal Cells | 293T(RCB2202) |