Gene-modified autologous T cells engineered with a chimeric antigen receptor targeting BCMA and FcRL5 to mediate targeted cytotoxicity against multiple myeloma cells; dual targeting aims to reduce antigen escape.
Autologous T cells are gene-modified to express a chimeric antigen receptor that recognizes BCMA and FcRL5 on multiple myeloma cells. CAR engagement triggers TCR signaling (CD3ζ with costimulatory domains), leading to targeted T-cell activation, proliferation, and cytotoxic killing of BCMA+/FcRL5+ tumor cells. Dual targeting is intended to reduce antigen escape and enhance tumor clearance.
YES
DIRECT
Anti-FCRL5 CAR T cells bind FCRL5 on target cells, triggering TCR/CD3zeta signaling and cytolytic killing via perforin/granzyme (and Fas/FasL)–mediated apoptosis of FCRL5+ cells.
Intravenous HER2-targeted antibody-drug conjugate: a humanized anti-HER2 IgG1 linked via a cleavable linker to a topoisomerase I inhibitor payload (DXd); binds HER2, is internalized, releases DXd to induce DNA damage, with Fc-mediated ADCC and bystander killing.
Humanized anti-HER2 IgG1 linked via a cleavable linker to a topoisomerase I inhibitor payload (DXd). After binding HER2, the ADC is internalized and the linker is cleaved to release DXd, which induces DNA damage and cell death. The Fc domain can mediate ADCC, and the membrane-permeable payload enables bystander killing of adjacent tumor cells.
YES
DIRECT
Anti-HER2 ADC binds HER2, is internalized, and releases the DXd topoisomerase I inhibitor, causing DNA damage and cell death; Fc-mediated ADCC can contribute, with some bystander killing from membrane-permeable payload.
Intravenous HER2-targeted antibody-drug conjugate: a humanized anti-HER2 IgG1 linked via a cleavable linker to a topoisomerase I inhibitor payload (DXd); binds HER2, is internalized, releases DXd to induce DNA damage, with Fc-mediated ADCC and bystander killing.
Humanized anti-HER2 IgG1 linked via a cleavable linker to a topoisomerase I inhibitor payload (DXd). After binding HER2, the ADC is internalized and the linker is cleaved to release DXd, which induces DNA damage and cell death. The Fc domain can mediate ADCC, and the membrane-permeable payload enables bystander killing of adjacent tumor cells.
NO
INDIRECT
The ADC binds HER2, is internalized, and releases the DXd payload, which inhibits topoisomerase I to cause DNA damage; killing depends on HER2-directed delivery (with bystander effect), not on binding cells for their topoisomerase I expression.
An anti-HER2 antibody–drug conjugate (RC48) linking a humanized anti‑HER2 monoclonal antibody to the cytotoxic payload monomethyl auristatin E (MMAE). Binds HER2 on urothelial tumor cells, is internalized, and releases MMAE to disrupt microtubules, causing cell-cycle arrest and apoptosis; Fc-mediated effects and a bystander effect may contribute.
Humanized anti-HER2 monoclonal antibody linked via a cleavable linker to monomethyl auristatin E (MMAE). After binding HER2 on tumor cells and internalization, MMAE is released to inhibit tubulin polymerization and disrupt microtubules, leading to G2/M cell-cycle arrest and apoptosis; Fc-mediated effector functions and a bystander effect may also contribute.
NO
INDIRECT
The ADC binds HER2 on target cells, is internalized, and releases MMAE that binds beta-tubulin to disrupt microtubules and induce apoptosis; killing is directed by HER2 recognition, not by beta-tubulin expression.
Genetically engineered T cells transduced via lentivirus to express a synthetic antigen receptor targeting LILRB4 (ILT3) on leukemic/myeloid cells, activating T-cell cytotoxicity; administered after lymphodepletion for R/R AML/CMML.
Autologous T cells are lentivirally engineered to express a synthetic/chimeric antigen receptor that recognizes LILRB4 (ILT3) on leukemic and immunosuppressive myeloid cells. Upon LILRB4 binding, the CAR activates T-cell signaling, leading to proliferation, cytokine release, and perforin/granzyme-mediated cytotoxicity, eliminating LILRB4-positive AML/CMML cells; lymphodepletion supports in vivo expansion and persistence.
YES
DIRECT
LILRB4-targeted CAR-T cells bind LILRB4 on target cells and, upon activation, kill them via perforin/granzyme-mediated cytotoxicity (and apoptotic pathways).