AI Article Synopsis
- Therapeutic antibodies utilize their Fc region to connect with immune mechanisms, particularly through binding to complement proteins and Fc receptors, which is vital for their effectiveness.
- Researchers have engineered various Fc region variants of anti-CD20 antibodies and conducted cell-based assays to evaluate their abilities in processes like complement-dependent and antibody-dependent cytotoxicity.
- The study provided insights into how these antibody variants perform differently, suggesting that certain variants may be better suited for specific therapeutic applications due to their unique activities and thermal stability.
Article Abstract
A critical attribute of therapeutic antibodies is their ability to engage with humoral or cellular effector mechanisms, and this depends on the ability of the Fc region to bind to complement (C1q) or Fc receptors. Investigators have sought to optimize these effects by engineering the Fc region to bind to a greater or lesser extent to individual receptors. Different approaches have been used in the clinic, but they have not been systematically compared. We have now produced a matched set of anti-CD20 antibodies representing a range of variants and compared their activity in cell-based assays for complement-dependent cytotoxicity, antibody-dependent cell-mediated cytotoxicity, and antibody-dependent phagocytosis using a range of individual Fc receptors. We have also compared the thermal stability of the variants by differential scanning fluorimetry (DSF). The results reveal a spectrum of activities which may be appropriate for different applications.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11418285 | PMC |
| http://dx.doi.org/10.1080/19420862.2024.2406539 | DOI Listing |
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