Autologous BCMA-directed CAR T-cell therapy administered intravenously; patient T cells are engineered to express a chimeric antigen receptor targeting BCMA on myeloma cells, activating T-cell cytotoxicity and cytokine release to kill BCMA-positive plasma cells.
Autologous T cells are genetically engineered to express a chimeric antigen receptor that binds BCMA on myeloma plasma cells. CAR engagement activates the T cells to proliferate, release cytokines, and mediate perforin/granzyme-dependent cytotoxic killing of BCMA-positive cells.
BCMA-directed CAR T cells bind BCMA on target cells and induce T cell cytotoxicity via perforin/granzyme-mediated lysis (apoptosis).
Subcutaneous bispecific T-cell–redirecting antibody (CD3×GPRC5D) that binds GPRC5D on myeloma cells and CD3 on T cells, recruiting and activating T cells to lyse GPRC5D-positive myeloma cells.
Humanized bispecific antibody that binds CD3 on T cells and GPRC5D on myeloma cells, cross-linking T cells to tumor cells to form an immune synapse and activate cytotoxic T-lymphocyte responses (perforin/granzyme release, cytokine production), leading to lysis of GPRC5D-positive myeloma cells.
Talquetamab crosslinks CD3 on T cells to GPRC5D on target cells, activating T cells to kill GPRC5D+ cells via perforin/granzyme-mediated cytolysis and apoptosis.
A humanized IgG1 bispecific T-cell–engaging monoclonal antibody (DuoBody-CD3xCD20; GEN3013) that co-binds CD20 on B cells and CD3 on T cells to form an immune synapse, activate T cells, and induce perforin/granzyme-mediated cytotoxic killing of malignant B cells; administered subcutaneously.
Humanized IgG1 bispecific antibody (DuoBody-CD3xCD20) that co-binds CD3 on T cells and CD20 on B cells to form an immune synapse, activate T cells, and drive perforin/granzyme-mediated cytotoxic killing of CD20+ malignant B cells.
Bispecific antibody co-binds CD20 on B cells and CD3 on T cells, forming an immune synapse that activates T cells to kill CD20+ cells via perforin/granzyme-mediated cytotoxicity.
Antibody-drug conjugate targeting a tumor-associated cell-surface antigen; internalizes and releases a cytotoxic payload (e.g., topoisomerase I or microtubule-targeting warhead) to kill cancer cells.
An anti-CLDN18.2 IgG1 antibody-drug conjugate with a cleavable linker to a topoisomerase I inhibitor. After binding CLDN18.2 on tumor cells, it is internalized and the linker is cleaved to release the payload, which inhibits topoisomerase I, blocks DNA replication, and triggers cell-cycle arrest and apoptosis in CLDN18.2-expressing cancer cells.
The ADC binds CLDN18.2 on target cells, is internalized, and releases a topoisomerase I inhibitor that blocks DNA replication, causing cell-cycle arrest and apoptosis.
Autologous, gene-modified T cells transduced with a lentiviral vector to express a human CD1a-specific chimeric antigen receptor (CAR) with CD3ζ signaling and costimulatory domains; upon binding CD1a on malignant T-ALL/LBL cells, the CAR T cells activate, proliferate, release cytokines, and mediate perforin/granzyme-dependent cytotoxicity in an HLA-independent manner.
Autologous T cells are lentivirally transduced to express a human CD1a-specific chimeric antigen receptor with CD3ζ signaling and costimulatory domains. Upon binding CD1a on malignant T-ALL/LBL cells, the CAR triggers HLA-independent T-cell activation, proliferation, cytokine release, and perforin/granzyme-mediated cytotoxic killing of target cells.
CAR binding to CD1a activates the engineered T cells, which kill CD1a+ cells via perforin/granzyme-mediated cytotoxicity (HLA-independent).