AI Article Synopsis
- Many studies have looked at how different variants of SARS-CoV-2 affect the body's neutralizing antibodies, especially after these variants become the dominant strains.
- This research highlights that the virus can undergo multiple mutations at once in the receptor binding domain (RBD), making it harder for antibodies, from vaccines or treatments, to neutralize the virus.
- Additionally, a specific antibody was found to neutralize various variants, but the virus can still develop ways to evade this by adding sugar molecules to its structure, suggesting that escape variants will keep emerging as SARS-CoV-2 evolves.
Article Abstract
Many studies have examined the impact of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants on neutralizing antibody activity after they have become dominant strains. Here, we evaluate the consequences of further viral evolution. We demonstrate mechanisms through which the SARS-CoV-2 receptor binding domain (RBD) can tolerate large numbers of simultaneous antibody escape mutations and show that pseudotypes containing up to seven mutations, as opposed to the one to three found in previously studied variants of concern, are more resistant to neutralization by therapeutic antibodies and serum from vaccine recipients. We identify an antibody that binds the RBD core to neutralize pseudotypes for all tested variants but show that the RBD can acquire an N-linked glycan to escape neutralization. Our findings portend continued emergence of escape variants as SARS-CoV-2 adapts to humans.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9127715 | PMC |
| http://dx.doi.org/10.1126/science.abl6251 | DOI Listing |
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