ArticleFrontiers in immunology2026
A fully human IgG1 antibody targeting MICA α1 domain inhibits interaction with NKG2D and activates immune effector functions against MICA-expressing cells.
Article in Frontiers in immunology, 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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Abstract
Background: MICA is a stress-induced ligand for the activating receptor NKG2D and plays a central role in immune recognition and elimination of tumor cells. Tumor-derived soluble MICA (sMICA) and its allelic diversity impair immune responses by disrupting NKG2D function and promoting immune evasion, highlighting the need for antibody-based strategies targeting the MICA/NKG2D axis. Methods: We generated a fully human IgG1 monoclonal antibody targeting the α1 domain of MICA using phage display and rational epitope design focused on a conserved, low-polymorphic region. We characterized its binding specificity and affinity for MICA, competition with NKG2D, and its ability to trigger immune effector functions, including antibody-dependent cell cytotoxicity (ADCC), antibody-dependent cell phagocytosis (ADCP) and activation of the classical complement pathway. Results: The antibody displayed high affinity for recombinant MICA (app K Conclusion: By combining high-affinity recognition of broad MICA alleles and robust activation of immune effector functions, this fully human anti-MICA α1 antibody offers a novel strategy to modulate the MICA/NKG2D axis and activate Fc-mediated immune effector functions against MICA-expressing tumor cells. Its dual mechanism of action supports its development as a standalone or combinatorial agent with immune checkpoint inhibitors in MICA-expressing tumors.
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