TROP2-targeting antibody–drug conjugate that delivers a cleavable topoisomerase I inhibitor payload; binding to TROP2 leads to internalization and payload release, causing DNA damage/replication stress and tumor cell death (potential bystander effect).
Humanized anti‑TROP2 IgG1 ADC linked via a cleavable linker to the topoisomerase I inhibitor tirumotecan. Binding to TROP2 on tumor cells triggers internalization and linker cleavage, releasing the payload to inhibit topoisomerase I, inducing DNA damage/replication stress and apoptosis, with a potential bystander effect on neighboring cells.
An anti-TROP2 antibody–drug conjugate binds TROP2 on tumor cells, is internalized, and releases a cleavable topoisomerase I inhibitor (tirumotecan) intracellularly, causing DNA damage/replication stress and apoptosis, with potential bystander killing of neighboring cells.
Anti–PD‑L1 IgG1 monoclonal antibody immune checkpoint inhibitor that blocks PD‑L1 to restore T‑cell function and may engage ADCC.
Avelumab is a human IgG1 monoclonal antibody that binds PD-L1 and blocks its interaction with PD-1, releasing inhibitory checkpoint signaling to restore and enhance T‑cell–mediated antitumor activity; its IgG1 Fc can also engage antibody‑dependent cellular cytotoxicity (ADCC) against PD‑L1–expressing cells.
Avelumab binds PD-L1 on target cells and, via its IgG1 Fc, engages Fc-gamma receptors on NK cells (and other effector cells) to mediate antibody-dependent cellular cytotoxicity (ADCC), killing PD-L1-expressing cells.
An IgG1 bispecific antibody that binds CD3 on T cells and BCMA (TNFRSF17) on malignant plasma cells, redirecting T cells to BCMA-expressing myeloma cells to trigger TCR/CD3 signaling, immune synapse formation, and T-cell–mediated cytotoxicity (perforin/granzyme release and cytokine secretion). Administered intravenously with dose escalation.
IgG1 bispecific antibody that binds CD3 on T cells and BCMA (TNFRSF17) on malignant plasma cells, bringing T cells into proximity with BCMA+ myeloma cells to trigger TCR/CD3 signaling, immune synapse formation, and T-cell–mediated cytotoxicity (perforin/granzyme release and cytokine secretion), resulting in lysis of BCMA-expressing tumor cells.
Bispecific engagement of CD3 on T cells and BCMA on target cells forms an immune synapse, activates TCR/CD3 signaling, and induces perforin/granzyme-mediated T-cell cytotoxicity (with cytokine release) against BCMA+ cells.
Patient-derived T cells engineered (retroviral transduction) to express an anti-CD7 chimeric antigen receptor; cellular gene therapy targeting CD7+ T/NK cells.
Autologous T cells are genetically engineered (retroviral transduction) to express an anti‑CD7 chimeric antigen receptor. Engagement of CD7 on target T- and NK-lineage cells activates the CAR T cells, inducing perforin/granzyme-mediated cytotoxicity and inflammatory cytokine release, resulting in selective depletion of CD7+ cells and immune reset.
Anti-CD7 CAR-T cells engage CD7 on target cells, form an immunologic synapse, and kill via perforin/granzyme-mediated cytotoxicity (apoptosis), with supportive cytokine effects.
Targeted haploidentical neoantigen T-cell therapy: ex vivo–expanded donor-derived T cells (≥50% HLA match; HLA-A*02/11/24 alleles) primed to patient-specific tumor neoantigens to recognize and kill EBV-positive malignant T cells via TCR-mediated recognition and cytotoxic effector mechanisms.
Donor-derived haploidentical T cells are ex vivo expanded and primed/selected for reactivity to patient-specific tumor neoantigens. After infusion, they use native TCRs to recognize neoantigen peptides presented by HLA-A*02/11/24 on EBV-positive malignant T cells and eliminate them via perforin/granzyme-mediated cytotoxicity.
Neoantigen-primed T cells recognize the patient-specific peptide–HLA-A*02 complex via their TCR and kill the presenting tumor cell through perforin/granzyme-mediated cytotoxicity.