Autologous T lymphocytes genetically engineered to express a chimeric antigen receptor specific for CD70; upon binding CD70 on tumor cells, they activate, proliferate, and mediate cytolysis and cytokine release.
Autologous T lymphocytes engineered to express a CD70-specific chimeric antigen receptor; binding to CD70 on tumor cells activates the T cells, leading to proliferation, perforin/granzyme-mediated cytolysis, and cytokine release to eliminate CD70-expressing cancer cells.
CD70 CAR T cells bind CD70 on target cells and induce cytolysis via T‑cell degranulation (perforin/granzyme–mediated apoptosis), with possible death‑receptor and cytokine effects.
Autologous, fully human anti-CD19 chimeric antigen receptor T-cell therapy that depletes CD19+ B-lineage cells to reduce pathogenic autoantibodies in generalized myasthenia gravis.
Autologous T cells are engineered with a lentiviral vector to express an anti-CD19 chimeric antigen receptor (scFv-CD19 with CD8α hinge/transmembrane, CD28 costimulatory, and CD3ζ signaling domains). After infusion, the CAR T cells recognize CD19 on B-lineage cells (B cells and plasmablasts), become activated, and mediate cytotoxic lysis, depleting CD19+ cells and reducing pathogenic autoantibody production in generalized myasthenia gravis.
Anti-CD19 CAR T cells bind CD19 on B-lineage cells and, upon activation, kill them via T cell cytotoxic mechanisms (perforin/granzyme release and death-receptor signaling), leading to lysis/apoptosis of CD19+ cells.
Anti-EGFR IgG1 monoclonal antibody that inhibits EGFR-driven signaling (RAS–RAF–MAPK, PI3K–AKT) and induces antibody-dependent cellular cytotoxicity (ADCC).
Cetuximab is an IgG1 monoclonal antibody that binds the extracellular domain of EGFR, blocking ligand binding and receptor dimerization to inhibit downstream RAS–RAF–MAPK and PI3K–AKT signaling, suppressing tumor cell proliferation and survival; its Fc region also engages immune effector cells to induce antibody-dependent cellular cytotoxicity (ADCC).
Cetuximab binds EGFR on target cells and its IgG1 Fc engages FcγR-expressing effector cells (e.g., NK cells) to induce antibody-dependent cellular cytotoxicity; it can also activate complement (CDC). EGFR signaling blockade may further promote apoptosis.
Chimeric anti-CD20 monoclonal antibody that depletes CD20-expressing B cells and may affect CD20+ T cells to preserve beta-cell function in recent-onset type 1 diabetes.
Chimeric anti-CD20 monoclonal antibody that binds CD20 on B lymphocytes (and a subset of CD20+ T cells) and depletes these cells via complement-dependent cytotoxicity, antibody-dependent cellular cytotoxicity, and apoptosis, thereby dampening autoimmunity and aiming to preserve beta-cell function.
Rituximab binds CD20 on target cells and eliminates them via complement-dependent cytotoxicity and Fc-mediated effector functions (ADCC/ADCP), and can also induce apoptosis.
Autologous neoantigen-targeted T cell therapy: ex vivo expanded patient PBMC-derived cytotoxic T cells (primarily CD8+) specific to personalized tumor neoantigens; mediate TCR-dependent recognition of neoantigen–HLA class I on tumor cells and kill via perforin/granzyme.
Autologous PBMC-derived cytotoxic T cells (primarily CD8+) are ex vivo expanded and selected for specificity to patient-specific tumor neoantigens. These unengineered T cells use their endogenous TCRs to recognize neoantigen peptides presented on HLA class I on tumor cells, leading to targeted killing via perforin/granzyme-mediated cytolysis.
Tumor cells presenting the patient-specific neoantigen peptide on HLA-A*02:01 are recognized by the infused neoantigen-specific CD8+ T cells via their endogenous TCRs, leading to perforin/granzyme-mediated cytolysis (with possible Fas–FasL apoptosis).