An autologous, gene-edited CAR T-cell therapy targeting BCMA on myeloma cells. The CAR construct is integrated non-virally at the PD-1 locus to modulate/abrogate PD-1 signaling, aiming to reduce T-cell exhaustion and enhance antitumor activity. Ex vivo–expanded CAR T cells bind BCMA, activate cytotoxic responses, and kill BCMA+ malignant plasma cells while countering PD-1/PD-L1–mediated immunosuppression.
Autologous gene-edited CAR T cells engineered with a BCMA-specific chimeric antigen receptor recognize and bind BCMA on myeloma cells, triggering cytotoxic killing of BCMA-positive malignant plasma cells. The CAR construct is integrated at the PD-1 locus to disrupt/modulate PD-1 signaling, reducing T-cell exhaustion and countering PD-1/PD-L1-mediated immunosuppression, thereby enhancing persistence and antitumor activity.
NO
INDIRECT
PD-1 is edited on the CAR T cells to reduce inhibition; the CAR targets BCMA, so cytotoxic killing is directed at BCMA+ tumor cells via T-cell cytolysis (perforin/granzyme), not at PD-1–expressing cells.
Autologous, second-generation HER2-targeted CAR T-cell therapy. Patient T cells are engineered with an anti-HER2 scFv linked to CD3ζ plus a co-stimulatory domain (CD28 or 4-1BB) to induce activation, proliferation, cytokine release, and cytotoxicity against HER2-positive tumor cells. Administered by intravenous infusion in a dose-escalation schema; study references possible lymphodepleting preconditioning.
Autologous T cells are engineered to express a second‑generation HER2‑specific CAR (anti‑HER2 scFv fused to CD3ζ with a co‑stimulatory domain such as CD28 or 4‑1BB). Upon binding HER2 on tumor cells, the CAR provides activation and co‑stimulation, driving T‑cell proliferation, cytokine release, and perforin/granzyme‑mediated cytotoxic lysis of HER2‑positive cancer cells.
YES
DIRECT
HER2-specific CAR T cells bind HER2 on target cells, become activated, and kill via perforin/granzyme-mediated cytolysis (and death receptor pathways).
TROP2-directed antibody-drug conjugate that delivers a cleavable topoisomerase I inhibitor payload to TROP2-expressing tumor cells, causing DNA damage and bystander cytotoxicity.
TROP2-directed antibody-drug conjugate that binds TROP2 on tumor cells, is internalized, and releases a cleavable topoisomerase I inhibitor payload to induce DNA damage and cell death, with potential bystander cytotoxicity in neighboring cells.
YES
DIRECT
The ADC binds TROP2, is internalized, and releases a cleavable topoisomerase I inhibitor payload that causes DNA damage and apoptosis; the membrane-permeable payload can also produce bystander killing.
TROP2-directed antibody-drug conjugate that delivers a cleavable topoisomerase I inhibitor payload to TROP2-expressing tumor cells, causing DNA damage and bystander cytotoxicity.
TROP2-directed antibody-drug conjugate that binds TROP2 on tumor cells, is internalized, and releases a cleavable topoisomerase I inhibitor payload to induce DNA damage and cell death, with potential bystander cytotoxicity in neighboring cells.
NO
INDIRECT
The ADC binds TROP2 on tumor cells, is internalized, and releases a topoisomerase I–inhibitor payload that causes DNA damage and cell death; topoisomerase I is the intracellular enzyme target of the payload, not the surface antigen engaged by the drug.
An antibody-drug conjugate (fully human IgG1) targeting CD205/Ly75 that delivers a cytotoxic payload to CD205-high tumor cells, enabling direct tumor cell killing and potential immune activation.
Fully human IgG1 antibody targeting CD205/Ly75 linked via a cleavable SPDB linker to the maytansinoid DM4. Upon CD205 binding and internalization, intracellular proteases cleave the linker to release DM4, which binds tubulin and disrupts microtubule dynamics, inhibiting mitosis and causing tumor cell death; may also promote immune activation through antigen uptake.
YES
DIRECT
ADC binds CD205 on target cells, is internalized, and releases the maytansinoid DM4 after linker cleavage; DM4 binds tubulin, disrupts microtubules, induces mitotic arrest, and kills the CD205-expressing cells.