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- W4316505896 abstract "Abstract Complement dependent cytotoxicity (CDC), which removes aberrant target cells through the assembly and complex formation of serum complement molecules, is the main effector function of anticancer therapeutic antibodies. In this study, we found that the CDC activity of anti-CD20 antibody increased remarkably when the symmetry of natural Immunoglobulin G (IgG) antibodies was broken. In addition, the expression of CD55 (a checkpoint inhibitor in the CDC cascade) was significantly increased in an in-house constructed rituximab-resistant cell line, suggesting that CD55 overexpression might be a mechanism by which cancer cells acquire rituximab resistance. Based on these findings, we developed an asymmetric bispecific antibody (SBU-CD55×CD20) that targets both CD55 and CD20 simultaneously to effectively remove rituximab-resistant cancer cells. In various cancer cell lines, including rituximab-resistant lymphoma cells, the SBU-CD55×CD20 antibody exhibited significantly higher CDC activity than either anti-CD20 IgG antibody alone or a combination of anti-CD20 IgG antibody and anti-CD55 IgG antibody. Furthermore, compared with other bispecific antibodies with symmetric features, the asymmetric bispecific antibody (SBU-CD55×CD20) exhibited significantly higher CDC activity against rituximab-resistant cancer cells. These results demonstrate that improving CDC using an asymmetric CD55-binding bispecific antibody could be a new strategy for designing therapeutics to treat patients with relapsed or refractory cancers." @default.
- W4316505896 created "2023-01-16" @default.
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- W4316505896 date "2023-01-16" @default.
- W4316505896 modified "2023-10-18" @default.
- W4316505896 title "Effective clearance of rituximab-resistant tumor cells by breaking the mirror-symmetry of Immunoglobulin G and simultaneous binding to CD55 and CD20" @default.
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- W4316505896 doi "https://doi.org/10.21203/rs.3.rs-2474854/v1" @default.
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