Gene-engineered natural killer (NK) cells expressing a chimeric antigen receptor based on NKG2D to recognize stress-inducible ligands (e.g., MICA, MICB, ULBPs) on AML cells and trigger NK cytotoxicity via DAP10/CD3ζ signaling.
Gene-engineered NK cells expressing an NKG2D-based chimeric antigen receptor recognize stress-inducible ligands (MICA/MICB/ULBPs) on AML cells and signal via DAP10/CD3ζ to activate NK cytotoxicity, leading to perforin/granzyme-mediated killing and cytokine release against leukemic cells.
NKG2D CAR on NK cells binds ULBP4 on target cells, signaling via DAP10/CD3ζ to activate NK degranulation and kill via perforin/granzyme-mediated apoptosis (with possible FasL/TRAIL contributions).
Gene-engineered natural killer (NK) cells expressing a chimeric antigen receptor based on NKG2D to recognize stress-inducible ligands (e.g., MICA, MICB, ULBPs) on AML cells and trigger NK cytotoxicity via DAP10/CD3ζ signaling.
Gene-engineered NK cells expressing an NKG2D-based chimeric antigen receptor recognize stress-inducible ligands (MICA/MICB/ULBPs) on AML cells and signal via DAP10/CD3ζ to activate NK cytotoxicity, leading to perforin/granzyme-mediated killing and cytokine release against leukemic cells.
NKG2D CAR on NK cells binds ULBP5 on target cells, activating DAP10/CD3ζ signaling and NK effector function, resulting in perforin/granzyme-mediated killing (and death receptor pathways).
Gene-engineered natural killer (NK) cells expressing a chimeric antigen receptor based on NKG2D to recognize stress-inducible ligands (e.g., MICA, MICB, ULBPs) on AML cells and trigger NK cytotoxicity via DAP10/CD3ζ signaling.
Gene-engineered NK cells expressing an NKG2D-based chimeric antigen receptor recognize stress-inducible ligands (MICA/MICB/ULBPs) on AML cells and signal via DAP10/CD3ζ to activate NK cytotoxicity, leading to perforin/granzyme-mediated killing and cytokine release against leukemic cells.
NKG2D CAR on NK cells binds ULBP6 on target cells, activates DAP10/CD3ζ signaling, triggering NK degranulation with perforin/granzyme-mediated killing (and death receptor pathways), leading to apoptosis of ULBP6+ cells.
Fully humanized IgG1 antibody-drug conjugate targeting B7-H3 (CD276); binds B7-H3 on tumor cells and delivers a cytotoxic payload to induce cell death.
Fully humanized IgG1 ADC targeting B7-H3 (CD276). After binding B7-H3 on tumor cells and internalization, it releases a topoisomerase inhibitor payload that blocks DNA topoisomerase activity, inhibiting DNA replication, causing cell-cycle arrest and apoptosis in B7-H3–expressing tumor cells.
The anti–B7-H3 ADC binds B7-H3 on tumor cells, is internalized, and releases a topoisomerase inhibitor payload that blocks DNA topoisomerase, halting DNA replication and triggering cell-cycle arrest and apoptosis of B7-H3–expressing cells.
Recombinant cytokine–toxin fusion (IL-3 linked to truncated diphtheria toxin) that binds CD123 (IL-3Rα) on AML cells, is internalized, and inhibits protein synthesis via EF-2 ADP-ribosylation to kill CD123+ blasts/progenitors.
Recombinant IL-3–diphtheria toxin fusion that binds CD123 (IL-3R alpha) on target cells, is internalized, and the diphtheria toxin catalytic domain ADP-ribosylates EF-2 to halt protein synthesis, leading to death of CD123-positive blasts/progenitors.
The IL-3–diphtheria toxin fusion binds CD123, is internalized, and the toxin ADP-ribosylates EF-2 to block protein synthesis, causing death of CD123+ cells.