By analyzing the cryoEM structures of antibodies against the SARS-CoV-2 virus, researchers report that the neutralizing capabilities of two antibodies are not affected by new strains as these antibodies target regions of the virus away from the ACE2 binding regions.
As the COVID-19 pandemic continues to spread worldwide, several new mutations of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have emerged. Of note are the B.1.1.7 lineage discovered in the United Kingdom (UK) and the B.1.351 that emerged in South Africa late in 2020. The B.1.1.7 variant has now spread to more than 50 countries, and both mutations are believed to increase the transmissibility of the virus.
Some studies have reported that neutralizing antibodies, particularly the neutralizing antibodies directed to the N-terminal domain, have a lower effect on these variants. However, many antibodies to the virus receptor-binding domain (RBD) seem to retain most of their potency.
In a previous study, researchers reported two extremely potent RBD antibodies, 1-57 and 2-7, whose effect was not inhibited by the new variants. To understand how these antibodies are effective against the new strains, they investigated their structures using cryo-electron microscopy (EM). They report their results in a research paper published on the bioRxiv* preprint server…