SARS-CoV-2 B.1.1.7 and B.1.351 Spike variants bind human ACE2 with increased affinity
| Autor: | Ian D Ferguson, Paul A. Khavari, Weili Miao, Muthukumar Ramanathan |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Genetics 2019-20 coronavirus outbreak Coronavirus disease 2019 (COVID-19) SARS-CoV-2 Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) fungi COVID-19 Spike Protein Biology Article body regions 03 medical and health sciences 030104 developmental biology 0302 clinical medicine Infectious Diseases Spike Glycoprotein Coronavirus Correspondence Humans Spike (database) Angiotensin-Converting Enzyme 2 030212 general & internal medicine skin and connective tissue diseases hormones hormone substitutes and hormone antagonists |
| Zdroj: | bioRxiv The Lancet. Infectious Diseases |
| Popis: | SARS-CoV2 being highly infectious has been particularly effective in causing widespread infection globally and more variants of SARS-CoV2 are constantly being reported with increased genomic surveillance. In particular, the focus is on mutations of Spike protein, which binds human ACE2 protein enabling SARS-CoV2 entry and infection. Here we present a rapid experimental method leveraging the speed and flexibility of Mircoscale Thermopheresis (MST) to characterize the interaction between Spike Receptor Binding Domain (RBD) and human ACE2 protein. The B.1.351 variant harboring three mutations, (E484K, N501Y, and K417N) binds the ACE2 at nearly five-fold greater affinity than the original SARS-COV-2 RBD. We also find that the B.1.1.7 variant, binds two-fold more tightly to ACE2 than the SARS-COV-2 RBD. |
| Databáze: | OpenAIRE |
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