An antibody–drug conjugate consisting of a humanized anti–Trop‑2 IgG1 linked via a cleavable linker to SN‑38 (the active metabolite of irinotecan, a topoisomerase I inhibitor). It binds Trop‑2 on tumor cells, is internalized, and releases SN‑38 to inhibit topoisomerase I, causing DNA damage and cell death, with potential bystander effect.
Humanized anti–Trop-2 IgG1 antibody linked via a cleavable linker to SN-38 (topoisomerase I inhibitor). After binding Trop-2 on tumor cells and internalization, SN-38 is released intracellularly to inhibit topoisomerase I, inducing DNA damage, cell-cycle arrest, and apoptosis; the cleavable linker can enable a bystander effect.
YES
DIRECT
The ADC binds TROP-2, is internalized, and releases SN-38 (topoisomerase I inhibitor), causing DNA damage, cell-cycle arrest, and apoptosis; a cleavable linker can also enable a bystander effect.
An antibody–drug conjugate consisting of a humanized anti–Trop‑2 IgG1 linked via a cleavable linker to SN‑38 (the active metabolite of irinotecan, a topoisomerase I inhibitor). It binds Trop‑2 on tumor cells, is internalized, and releases SN‑38 to inhibit topoisomerase I, causing DNA damage and cell death, with potential bystander effect.
Humanized anti–Trop-2 IgG1 antibody linked via a cleavable linker to SN-38 (topoisomerase I inhibitor). After binding Trop-2 on tumor cells and internalization, SN-38 is released intracellularly to inhibit topoisomerase I, inducing DNA damage, cell-cycle arrest, and apoptosis; the cleavable linker can enable a bystander effect.
NO
INDIRECT
Sacituzumab govitecan binds Trop-2 on tumor cells, is internalized, and releases SN-38, which inhibits DNA topoisomerase I to cause DNA damage and apoptosis. Topoisomerase I is the intracellular payload target, not the antigen recognized by the drug.
Patient-derived T lymphocytes genetically engineered to express a chimeric antigen receptor that recognizes a tumor-associated antigen and activates T-cell effector functions via CD3ζ and a costimulatory domain (e.g., CD28 or 4-1BB), leading to cytotoxic killing, cytokine release, expansion, and persistence.
Autologous T lymphocytes are genetically engineered to express a chimeric antigen receptor that binds a tumor-associated antigen independent of MHC, initiating CD3ζ signaling with a costimulatory domain (e.g., CD28 or 4-1BB) to activate cytotoxic killing, cytokine release, proliferation, and persistence of the T cells to eliminate antigen-expressing tumor cells.
YES
DIRECT
CAR T cells recognize the target antigen via the CAR and, upon CD3ζ/costimulatory signaling, directly kill antigen-positive cells through perforin–granzyme release and Fas–FasL–mediated apoptosis (with cytokine-mediated effects).
Anti-HER2 IgG1 monoclonal antibody that inhibits HER2 signaling/dimerization and mediates antibody-dependent cellular cytotoxicity (ADCC).
Humanized IgG1 monoclonal antibody targeting HER2 (ERBB2); binds the extracellular domain to inhibit HER2 dimerization/signaling and promote receptor downregulation, while engaging Fcγ receptors to mediate antibody-dependent cellular cytotoxicity (ADCC) against HER2-overexpressing tumor cells.
YES
DIRECT
Trastuzumab binds HER2 on tumor cells and its Fc engages Fc gamma receptors on immune effectors (e.g., NK cells, macrophages) to mediate antibody-dependent cellular cytotoxicity and phagocytosis, killing HER2+ cells; it also inhibits HER2 signaling.
Autologous, genetically engineered anti-CD19/CD20 chimeric antigen receptor (CAR) T-cell therapy; single IV infusion designed to deplete CD19+/CD20+ B cells to treat refractory autoimmune diseases.
Autologous T cells are genetically engineered to express a dual-target chimeric antigen receptor recognizing CD19 and CD20 on B cells. Upon antigen engagement, the CAR T cells become activated and mediate cytotoxic killing of CD19+/CD20+ B-lineage cells, leading to B-cell depletion and suppression of autoantibody-driven immune responses.
YES
DIRECT
CD19-binding CAR T cells engage CD19 on B cells and induce cytolysis via immune-synapse–mediated perforin/granzyme release (and Fas–FasL apoptosis).