| Title: |
Experimental Evidence for Enhanced Receptor Binding by Rapidly Spreading SARS-CoV-2 Variants |
| Authors: |
C. (Charlie) Laffeber; K.D.A. (Kelly) de Koning; R. (Roland) Kanaar; J.H.G. (Joyce) Lebbink |
| Publisher Information: |
2021-07-23 |
| Document Type: |
Electronic Resource |
| Abstract: |
Rapidly spreading new variants of SARS-CoV-2 carry multiple mutations in the viral spike protein which attaches to the angiotensin converting enzyme 2 (ACE2) receptor on host cells. Among these mutations are amino acid changes N501Y (lineage B.1.1.7, first identified in the UK), and the combination N501Y, E484K, K417N (B.1.351, first identified in South Africa), all located at the interface on the receptor binding domain (RBD). We experimentally establish that RBD containing the N501Y mutation results in 7-fold stronger binding to the hACE2 receptor than wild type RBD. The E484K mutation only slightly enhances the affinity for the receptor, while K417N attenuates affinity. As a result, RBD from B.1.351 containing all three mutations binds 3-fold stronger to hACE2 than wild type RBD but 2-fold weaker than N501Y. However, the recently emerging d |
| Index Terms: |
info:eu-repo/semantics/article |
| DOI: |
10.1016.j.jmb.2021.167058 |
| URL: |
http://repub.eur.nl/pub/135836 |
| Availability: |
Open access content. Open access content; info:eu-repo/semantics/openAccess |
| Note: |
Journal of Molecular Biology vol. 433 no. 15 |
| Other Numbers: |
QGQ oai:repub.eur.nl:135836; doi:10.1016/j.jmb.2021.167058; urn:hdl:1765/135836; 1273464261 |
| Contributing Source: |
ERASMUS UNIVERSITEIT ROTTERDAM; From OAIster®, provided by the OCLC Cooperative. |
| Accession Number: |
edsoai.on1273464261 |
| Database: |
OAIster |