Antibody–drug conjugate targeting TROP2; upon internalization it releases deruxtecan, a topoisomerase I inhibitor, causing tumor DNA damage.
Humanized anti‑TROP2 monoclonal antibody linked via a cleavable linker to deruxtecan (DXd), a topoisomerase I inhibitor. After binding TROP2 on tumor cells and internalization, the linker is cleaved to release DXd, which inhibits topoisomerase I, causing DNA damage and apoptosis; the membrane‑permeable payload can also exert a bystander effect.
YES
DIRECT
Anti-TROP2 ADC binds TROP2, is internalized, and releases the DXd topoisomerase I inhibitor, causing DNA damage and apoptosis in target cells; the membrane-permeable payload can also cause bystander killing.
Antibody–drug conjugate targeting TROP2; upon internalization it releases deruxtecan, a topoisomerase I inhibitor, causing tumor DNA damage.
Humanized anti‑TROP2 monoclonal antibody linked via a cleavable linker to deruxtecan (DXd), a topoisomerase I inhibitor. After binding TROP2 on tumor cells and internalization, the linker is cleaved to release DXd, which inhibits topoisomerase I, causing DNA damage and apoptosis; the membrane‑permeable payload can also exert a bystander effect.
NO
INDIRECT
Dato-DXd does not bind topoisomerase I on cells. It binds TROP2 on tumor cells, is internalized, and releases deruxtecan, which inhibits topoisomerase I to cause DNA damage and apoptosis in TROP2-positive cells (with possible bystander effect).
Autologous mRNA-engineered BCMA-directed CAR T-cell therapy in which patient T cells are transiently modified to express a chimeric antigen receptor targeting B-cell maturation antigen (BCMA), resulting in CAR-mediated T-cell activation and cytotoxicity against myeloma cells.
Autologous patient T cells are transiently mRNA-engineered to express a BCMA-targeted chimeric antigen receptor; CAR binding to BCMA on myeloma cells activates the T cells to release cytotoxic effectors and kill BCMA-positive plasma cells, with transient expression limiting persistence and avoiding genomic integration.
YES
DIRECT
BCMA-directed CAR T cells recognize BCMA on target cells, become activated, and kill BCMA+ cells via perforin/granzyme-mediated cytolysis and death-receptor–mediated apoptosis.
An allogeneic engineered cellular immunotherapy composed of γδ T cells expressing a chimeric antigen receptor targeting B7-H3 (CD276). Administered via local (meningeal/CSF) injection at 3×10^7 cells per dose with optional repeat dosing. CAR engagement enables MHC-independent recognition of B7-H3+ tumor cells, activating T-cell signaling for cytotoxic killing (perforin/granzyme) and cytokine release; γδ T cells contribute innate-like stress-antigen recognition (e.g., via γδ TCR/NKG2D) with lower alloreactivity.
Allogeneic γδ T cells engineered with a chimeric antigen receptor targeting B7‑H3 (CD276) recognize tumor cells independently of MHC and, upon CAR engagement, activate T‑cell signaling to mediate cytotoxic killing via perforin/granzyme and cytokine release; the γδ T-cell phenotype adds innate-like stress‑antigen recognition (e.g., via γδ TCR/NKG2D) with lower alloreactivity.
YES
DIRECT
B7-H3–targeted CAR-γδ T cells bind B7-H3 on target cells and, upon CAR signaling, directly kill them via T-cell cytotoxicity (perforin/granzyme release and death-receptor pathways).
Rabbit polyclonal anti-thymocyte globulin that depletes T cells to prevent rejection and GVHD.
Rabbit polyclonal anti-thymocyte IgG that binds multiple T-cell surface antigens and depletes T cells via complement-dependent cytotoxicity, antibody-dependent cellular cytotoxicity, and apoptosis, producing immunosuppression to prevent rejection and GVHD.
YES
DIRECT
ATG contains antibodies that bind CD2 on T cells, leading to complement-dependent lysis and Fc-mediated ADCC; receptor cross-linking can also induce apoptosis.