AI Article Synopsis
- Omicron, a variant of SARS-CoV-2, shows significant mutations in the receptor-binding domain, which impacts antibody efficacy, especially with treatments like Casirivimab and Imdevimab.
- The variant's mutations have less effect on ACE2 binding and some antibodies, indicating a complex interaction between the virus and immune response.
- Despite booster vaccinations improving antibody levels, they still fall short compared to responses against the original Wuhan strain, highlighting Omicron's altered antigenicity and the potential effectiveness of certain antibodies in treatment.
Article Abstract
SARS-CoV-2 Omicron is the first pandemic variant of concern exhibiting an abrupt accumulation of mutations particularly in the receptor-binding domain that is a critical target of vaccination induced and therapeutic antibodies. Omicron's mutations did only marginally affect the binding of ACE2, and the two antibodies Sotrovimab and CR3022 but strongly impaired the binding of Casirivimab and Imdevimab. Moreover, as compared with Wuhan, there is reduced serum reactivity and a pronounced loss of competitive surrogate virus neutralization (sVN) against Omicron in naïve vaccinees and in COVID-19 convalescents after infection and subsequent vaccination. Finally, although the booster vaccination response conferred higher titers and better sVN, the effect was nonetheless significantly lower compared with responses against Wuhan. Overall, our data suggest that the antigenicity of Omicrons receptor binding motive has largely changed but antibodies such as Sotrovimab targeting other conserved sites maintain binding and therefore hold potential in prophylaxis and treatment of Omicron-induced COVID-19.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8920075 | PMC |
| http://dx.doi.org/10.1016/j.isci.2022.104076 | DOI Listing |
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