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The Omicron strain has been found to have many mutations in the S-protein33,34. These mutations result in reduced or zero effectiveness of Cas and Imd mAbs against the Omicron strain29,35. We also confirmed this in our experimental setting (Fig. 2). In addition to changes in the reactivity of mAbs to Omicron, we observed different behavior of Omicron in the ADE assay compared with the SARS-CoV-2 original strain (Supplemental Figs. 6D and 7B).
Some sera from mRNA-vaccinated volunteers (collected on day 175 after the second vaccination) maintained neutralizing activity against the SARS-CoV-2 original strain (Supplemental Fig. 6D). In contrast, none of these sera exhibited neutralization, and some of them caused enhancement of infection with Omicron (Supplemental Fig. 7B). These results demonstrate that Abs raised by double vaccination (at least on day 175 after the second vaccination, Supplemental Fig. 7B) are less effective against Omicron as reported36, and suggest that the Omicron strain has acquired the ability to escape attack by pre-existing anti-SARS-CoV-2 Abs and in part can utilize infection-enhancing mechanisms, possibly including ADE, as a means of survival.
At this time, we need to further investigate what the critical factors are that are included in sera and lead to the enhancement of Omicron infection. Although Omicron has many amino acid substitutions in the receptor-binding domain of the S-protein33,34, the receptors (ACE2) on target cells seem to still be required for infection (Supplemental Fig. 8). In fact, it has been reported that Omicron S-protein has high affinity for ACE235. The unique mechanisms of Omicron infection, such as altered TMPRSS2 usage35, still need to be elucidated, and these unique features can be utilized in the development of new drugs.

Regarding neutralizing Ab drugs for SARS-CoV-2, it is important to avoid ADE potential. To this end, one promising approach is to modify the Fc-region in Abs to abrogate their binding to FcR8,13,14,37. The three therapeutic mAbs used in this study (Cas, Imd, and Sot) have human IgG1 backbones, Cas and Imd with no modification in the Fc region, and Sot with a two amino acid modification in the Fc region that confers extended half-life. All three of these mAbs bound to FcR irrespective of modification in the Fc region (Supplemental Figs. 2 and 5). Cas and Imd had ADE-causing potential (Fig. 1), while Sot had no ability to induce ADE (Fig. 2), demonstrating that an FcR-bindable Ab is not always an ADE-causing Ab.
In addition, regarding the target epitope, Cas and Imd mAbs bind to distinct and non-overlapping regions of the receptor-binding domain (RBD) of the S-protein of SARS-CoV-221. In contrast, Sot mAb targets an epitope on the S-protein that does not compete with ACE2 binding, which is a non-RBD region26. Therefore, taken together, it is not currently clear what critical factors are responsible for the lack of ADE in the case of Sot mAb, that is, the target epitope, modification of Fc, or both. These results suggest complex and multiple mechanisms for ADE. In any case, both FcR- and ACE2-positive Mylc cells will be useful for identifying ADE potential by Abs and antisera.