Omicron BQ and XBB subvariants most resistant viruses to monoclonal antibodies Coronavirus Disease COVID19 Omicron SARSCoV2 biorxivpreprint
By Tarun Sai LomteFeb 13 2023Reviewed by Benedette Cuffari, M.Sc. Since its emergence in November of 2021, the SARS-CoV-2 Omicron variant has mutated into several sub-variants. A recent study posted to the bioRxiv* preprint server examines the neutralization of severe acute respiratory syndrome coronavirus 2 Omicron sub-variants by sera from vaccinated and boosted individuals, as well as those diagnosed with a breakthrough infection.
Since lifting the zero-COVID policy in December 2022, China continues to record thousands of new COVID-19 cases daily, most of which are caused by SARS-CoV-2 Omicron BF.7 or BA.5 sub-variants. A similar neutralization resistance pattern was observed with serum samples obtained from individuals receiving the heterologous booster. Only a few samples retained marginal neutralization against XBB.1, XBB.1.5, BQ.1, and BQ.1.1 sub-variants.
The neutralizing potency of sera from individuals with BA.5 or BF.7 breakthrough infection was also examined. To this end, BA.5 breakthrough infection elicited high GMTs against the wild-type strain and Omicron sub-variants, including BQ.1 and BQ.1.1; however, XBB.1.5, BA.2.75.2, and BN.1 were more resistant to neutralization. Similarly high neutralization titers were observed with BF.7 breakthrough infection sera.
Finally, the susceptibility of emergent Omicron sub-variants to neutralization by 12 monoclonal antibodies against the viral spike and two mAbs against the human angiotensin-converting enzyme 2 receptor was assessed. To this end, LY-CoV1404 was inactive against XBB.1, BE.1.1.1, BQ.1, XBB.1.5, and BQ.1.1, which might be due to K444T and V445P amino acid substitutions.
Some receptor-binding domain -directed mAbs were also evaluated. For example, 2-36, DH1047, and S2X259 mAbs lost neutralization against all Omicron sub-variants, while S2K146 mAb retained activity against BN.1, BA.2.75, BA.2, and BA.2.75.6. Structural analysis indicated that the F486 substitutions could abrogate the hydrogen bonds between the spike and heavy antibody chain.
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