How do mutations in emergent SARS-CoV-2 Omicron variants affect viral function, human immunity, and recognition by therapeutic antibodies? biorxivpreprint UW WUSTLmed mutation coronavirus covid COVID19 SARSCoV2 Omicron immunity
By Tarun Sai LomteJan 19 2023Reviewed by Danielle Ellis, B.Sc. In a recent study posted to bioRxiv*, researchers explored how mutations in emergent severe acute respiratory syndrome coronavirus 2 variants affect viral function, human immunity, and recognition by therapeutic antibodies.
BLI revealed a similar binding affinity for BA.5 and BQ.1.1 RBDs, suggesting that additional mutations of BQ.1.1 did not impact hACE2 engagement. It also showed a higher binding affinity of BA.2.75 RBD relative to BA.2. XBB.1 RBD had a similar affinity as Wuhan-Hu-1 RBD. Surface plasmon resonance revealed results comparable to BLI. The team observed reduced and slower fusogenicity for BA.1, BA.2, and BA.5 spikes relative to the Delta spike.
Antibodies eBook Compilation of the top interviews, articles, and news in the last year. Download a free copy The binding affinity of the mAb to variant RBDs decreased approximately 100-fold relative to Wu RBD. In addition, sotrovimab showed efficient cross-reactivity to cell surface-expressed spike trimers of XBB.1 and BQ.1.1 variants. Nonetheless, neutralization potency was variable, with about 6.5- and 94-fold loss against XBB.1 and BQ.1.1, respectively, relative to Wu.
Additional experiments indicated that plasma antibodies eliciting fragment-crystallizable effector functions varied among individuals but were broadly reactive against Omicron variants. The researchers compared memory B cells among four cohorts by enumerating the frequency of Wu and Omicron RBD-specific MBCs and Wu/Omicron cross-reactive MBCs.
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