Subcutaneous bispecific T‑cell–engaging antibody (BCMA×CD3) that redirects cytotoxic T cells to BCMA-expressing myeloma cells to induce lysis.
Bispecific antibody targeting BCMA on myeloma cells and CD3 on T cells; crosslinks T cells to BCMA-positive plasma cells to form an immune synapse, activate cytotoxic T lymphocytes, and induce perforin/granzyme-mediated tumor cell lysis.
NO
INDIRECT
Elranatamab binds CD3ε on T cells to activate and redirect them to BCMA+ myeloma cells; the T cells then kill BCMA-expressing targets via perforin/granzyme. CD3+ T cells are not the cytotoxic targets.
Patient-derived T cells genetically engineered to express a T-cell receptor recognizing the TP53 R248Q mutant peptide presented by HLA-A*11:01; reinfused to mediate antigen-specific cytotoxicity against TP53 R248Q–positive tumor cells.
Autologous T cells are engineered to express an HLA-A*11:01–restricted T-cell receptor that recognizes the TP53 R248Q mutant peptide on MHC class I. Upon binding the mutant peptide–MHC complex on tumor cells, the T cells activate TCR signaling and mediate antigen-specific cytotoxicity via perforin/granzyme release and cytokine-driven killing, selectively targeting TP53 R248Q–positive cancer cells.
YES
DIRECT
Engineered TCR T cells recognize the TP53 R248Q peptide presented by HLA-A*11:01 on target cells and directly kill them via TCR-triggered cytolytic synapse with perforin/granzyme release (and death receptor/cytokine-mediated apoptosis).
An antibody–drug conjugate consisting of a humanized anti–Trop-2 IgG1 monoclonal antibody linked to SN-38 (irinotecan’s active metabolite), a topoisomerase I inhibitor; binding to Trop-2 leads to internalization and SN-38 release, causing DNA damage and tumor cell death.
Humanized anti–Trop-2 IgG1 monoclonal antibody conjugated to SN-38 (irinotecan’s active metabolite). After binding Trop-2 on tumor cells, the complex is internalized and the linker is cleaved to release SN-38, which inhibits topoisomerase I by stabilizing Top1–DNA complexes, causing DNA strand breaks, replication arrest, and apoptosis; released SN-38 can also exert a bystander effect.
YES
DIRECT
ADC binds TROP-2 on tumor cells, is internalized, and releases SN-38, a topoisomerase I inhibitor, causing DNA strand breaks and apoptosis; released SN-38 can also kill nearby cells (bystander effect).
An antibody–drug conjugate consisting of a humanized anti–Trop-2 IgG1 monoclonal antibody linked to SN-38 (irinotecan’s active metabolite), a topoisomerase I inhibitor; binding to Trop-2 leads to internalization and SN-38 release, causing DNA damage and tumor cell death.
Humanized anti–Trop-2 IgG1 monoclonal antibody conjugated to SN-38 (irinotecan’s active metabolite). After binding Trop-2 on tumor cells, the complex is internalized and the linker is cleaved to release SN-38, which inhibits topoisomerase I by stabilizing Top1–DNA complexes, causing DNA strand breaks, replication arrest, and apoptosis; released SN-38 can also exert a bystander effect.
NO
INDIRECT
Sacituzumab govitecan binds Trop-2 on cells, is internalized, and releases SN-38, which inhibits topoisomerase I to cause DNA damage and apoptosis; topoisomerase I is the intracellular payload target, not the antigen determining cell targeting.
A patient-specific neoantigen peptide vaccine designed to elicit anti-tumor immunity by promoting dendritic cell/MHC presentation of tumor-derived neoantigens, priming and expanding tumor-specific CD8+ cytotoxic and CD4+ helper T cells and generating immune memory.
Patient-specific tumor neoantigen peptides are taken up by dendritic cells and presented on MHC class I and II, priming and expanding neoantigen-specific CD8+ cytotoxic and CD4+ helper T cells to mediate tumor cell killing and establish durable immune memory.
NO
INDIRECT
The vaccine primes neoantigen-specific CD8+ T cells, which kill cells presenting the specific neoantigen peptide in HLA-A via perforin/granzyme cytolysis (and Fas–FasL apoptosis); HLA-A expression alone is not targeted.