Autologous T lymphocytes genetically engineered via lentiviral transduction to express a B7-H3–targeted chimeric antigen receptor incorporating an IL-7Rα intracellular signaling domain to enhance persistence and proliferation; administered intraventricularly via CNS catheter.
Autologous T cells are engineered to express a chimeric antigen receptor targeting B7-H3 (CD276). CAR engagement of B7-H3 on tumor cells triggers MHC-independent T-cell activation via CD3ζ signaling, inducing cytotoxic killing and cytokine release. An incorporated IL-7 receptor alpha intracellular signaling domain augments IL-7/JAK-STAT5 survival and proliferative signals to enhance CAR T-cell persistence and expansion, supporting activity in the CNS when delivered intraventricularly.
YES
DIRECT
B7-H3–binding CAR activates T cells (via CD3z and IL-7Ralpha signaling), triggering MHC-independent cytolysis of B7-H3+ cells through perforin/granzyme release and death-receptor pathways.
Intravenous chimeric IgG1 monoclonal antibody against EGFR; blocks ligand binding and receptor activation and can elicit ADCC.
Chimeric IgG1 monoclonal antibody that binds the extracellular domain of EGFR, blocking ligand binding and receptor dimerization/activation, thereby inhibiting downstream signaling and tumor cell proliferation; can also mediate antibody-dependent cellular cytotoxicity (ADCC).
YES
DIRECT
Cetuximab’s IgG1 Fc engages Fcγ receptors on NK cells and other effectors to mediate ADCC against EGFR-expressing cells (with possible complement activation), causing target-cell lysis.
Autologous, genetically engineered CAR T-cell therapy targeting CLDN18.2; engineered T cells bind CLDN18.2 on tumor cells to activate T-cell proliferation, cytokine release, and cytotoxic killing.
Autologous T cells are genetically engineered to express a chimeric antigen receptor targeting CLDN18.2. Upon binding CLDN18.2 on tumor cells, the CAR activates T cells independently of native TCR/MHC, driving T‑cell expansion, cytokine release, and cytotoxic killing of CLDN18.2‑expressing tumor cells.
YES
DIRECT
CLDN18.2-specific CAR T cells bind CLDN18.2 on target cells, become activated, and kill them via T-cell cytotoxic mechanisms (perforin/granzyme-mediated lysis and cytokine-driven apoptosis), independent of native TCR/MHC.
Subcutaneous BCMA/CD3 bispecific T-cell engager (BiTE) antibody that binds BCMA (TNFRSF17) on malignant plasma cells and CD3 on T cells to redirect T-cell cytotoxicity and cytokine release against BCMA-positive plasma cells; uses step-up priming followed by weekly/biweekly dosing to prevent progression of high-risk smoldering multiple myeloma.
Bispecific T-cell engager antibody that binds BCMA on malignant plasma cells and CD3 on T cells to form an immunologic synapse, activating T-cell cytotoxicity and cytokine release to kill BCMA-positive plasma cells.
YES
DIRECT
BiTE antibody bridges BCMA on target cells and CD3 on T cells, forming an immunologic synapse that activates T-cell killing via perforin/granzyme-mediated cytotoxicity and cytokine release against BCMA+ cells.
Subcutaneous BCMA/CD3 bispecific T-cell engager (BiTE) antibody that binds BCMA (TNFRSF17) on malignant plasma cells and CD3 on T cells to redirect T-cell cytotoxicity and cytokine release against BCMA-positive plasma cells; uses step-up priming followed by weekly/biweekly dosing to prevent progression of high-risk smoldering multiple myeloma.
Bispecific T-cell engager antibody that binds BCMA on malignant plasma cells and CD3 on T cells to form an immunologic synapse, activating T-cell cytotoxicity and cytokine release to kill BCMA-positive plasma cells.
NO
INDIRECT
CD3 is on T cells; the BiTE uses CD3 to activate and redirect T cells to kill BCMA-positive tumor cells via perforin/granzyme-mediated cytotoxicity and cytokine release. CD3+ T cells themselves are not the cytotoxic target.