ArticleImmunity2026
Pharmacologic glycoengineering of Fcγ receptor IIIa enhances force-resistant IgG-FcγR interactions and anti-tumor antibody efficacy.
Article in Immunity, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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8 authors.
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Abstract
Therapeutic monoclonal antibodies (mAbs) are central to cancer treatment but often show incomplete efficacy. We show that transient pharmacologic inhibition of complex N-glycans in host cells ("glycoengineering") enhances the in vivo activity of multiple depleting mAbs, including mAbs already engineered for heightened potency. In preclinical models, glycoengineering improved α-CD20-mediated tumor clearance and survival through FcγRIIIa- and natural killer (NK) cell-dependent pathways. In B16-F10 melanoma, glycoengineering similarly enhanced anti-CD25 depletion of intratumoral regulatory T cells (Tregs). Notably, glycoengineering produced minimal changes in equilibrium binding affinity but markedly increased the mechanical durability of IgG-FcγRIIIa interactions under physiological shear stress. These results establish antibody effector function as a mechano-immunological process in which IgG-FcγR interactions can be tuned for resilience to physiological forces, thereby moving beyond the current affinity-centric paradigm in mAb engineering. Integrating mechanobiology into therapeutic development may enable mAbs optimized for the dynamic forces of human physiology, which provides a route to enhance next-generation immunotherapies.
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