HER2-directed antibody–drug conjugate (IgG1 trastuzumab linked via a cleavable linker to the deruxtecan [DXd] topoisomerase I inhibitor). Binds HER2, internalizes, releases DXd in lysosomes to inhibit TOP1 causing DNA damage; trastuzumab component can inhibit HER2 signaling and mediate ADCC; payload can exert a bystander effect.
HER2-directed antibody-drug conjugate: trastuzumab (IgG1) linked via a cleavable linker to deruxtecan (DXd), a topoisomerase I inhibitor. After HER2 binding and internalization, lysosomal cleavage releases DXd to inhibit TOP1, causing DNA damage and tumor cell death. The trastuzumab component also blocks HER2 signaling and mediates ADCC; the membrane-permeable payload can produce a bystander effect.
ADC binds HER2, is internalized, and releases the TOP1 inhibitor deruxtecan in lysosomes, causing DNA damage and tumor cell death; Fc can also mediate ADCC, with a membrane-permeable payload enabling bystander killing.
TROP2-directed antibody–drug conjugate (IgG1 anti-TROP2 datopotamab linked via a cleavable linker to the deruxtecan [DXd] topoisomerase I inhibitor). Binds TROP2, internalizes, releases DXd in lysosomes to inhibit TOP1 causing DNA damage; membrane-permeable payload may produce a bystander effect.
TROP2-directed IgG1 antibody–drug conjugate that binds TROP2 on tumor cells, is internalized, and releases the DXd (deruxtecan) topoisomerase I inhibitor via a cleavable linker in lysosomes; DXd inhibits TOP1, causing DNA damage and apoptosis, with a membrane-permeable payload enabling a bystander effect.
ADC binds TROP2 on target cells, is internalized, and releases the DXd topoisomerase I inhibitor after lysosomal linker cleavage, causing DNA damage and apoptosis (with a membrane-permeable payload that can also cause a bystander effect).
Autologous CD19-directed chimeric antigen receptor (CAR) T-cell therapy in which a patient’s T cells are engineered to express a CD19-targeted CAR to deplete CD19+ B-lineage cells (including plasmablasts), aiming to reduce pathogenic autoantibody production in autoimmune diseases.
Autologous T cells are engineered to express a CD19-specific chimeric antigen receptor that recognizes CD19 on B-lineage cells (including plasmablasts). Upon antigen engagement, CAR T cells activate and mediate cytotoxic killing of CD19+ cells, depleting pathogenic B-cell populations to reduce autoantibody production and reset humoral immunity in autoimmune disease.
CD19-targeted CAR T cells bind CD19 on B-lineage cells and induce cytolysis via T-cell effector mechanisms (perforin/granzyme-mediated apoptosis, Fas–FasL).
Autologous T cells genetically modified to express a chimeric antigen receptor targeting mesothelin, enabling MHC-independent recognition and cytotoxic killing of mesothelin-positive tumor cells after reinfusion (typically 1–10×10^6 cells/kg IV; local delivery optional).
Autologous T cells are genetically engineered to express a chimeric antigen receptor specific for mesothelin, enabling MHC-independent recognition of mesothelin-positive tumor cells. CAR engagement triggers CD3ζ and costimulatory signaling, leading to T-cell activation, cytokine release, proliferation, and targeted cytotoxic killing of mesothelin-expressing cancer cells.
CAR T cells bind mesothelin on target cells and induce killing via perforin/granzyme-mediated cytolysis and Fas–FasL apoptosis after CAR signaling.
Autologous CAR-T cells engineered to target HER2 (ERBB2), designed for MHC-independent recognition and killing of HER2-expressing tumors with activation via CD3ζ and costimulatory signaling domains.
Autologous T cells engineered to express a HER2-specific chimeric antigen receptor. Binding to HER2 triggers CD3zeta and costimulatory signaling, activating the T cells to proliferate, release cytokines, and kill HER2-expressing tumor cells via perforin/granzyme in an MHC-independent manner.
HER2-directed CAR-T cells bind HER2 on target cells, activating CD3zeta/costimulatory signaling and inducing T-cell cytotoxicity via perforin/granzyme-mediated lysis (and death receptor pathways), MHC-independent.