Humanized IgG1 monoclonal antibody targeting EGFR; blocks ligand binding and downstream signaling (RAS/RAF/MEK/ERK, PI3K/AKT), mediates ADCC, and enhances radiosensitivity in EGFR-overexpressing HNSCC.
Humanized IgG1 monoclonal antibody against EGFR that blocks ligand binding and receptor activation, suppressing downstream RAS/RAF/MEK/ERK and PI3K/AKT signaling; its Fc can engage immune effector cells to mediate ADCC, and EGFR blockade can enhance tumor radiosensitivity, particularly in EGFR-overexpressing HNSCC.
The IgG1 anti-EGFR antibody opsonizes EGFR+ cells and engages Fcγ receptors on NK cells/macrophages to induce ADCC (and possibly complement-mediated lysis). EGFR signaling blockade is mainly cytostatic/radiosensitizing.
Patient-specific chimeric monoclonal antibodies generated from each subject’s tumor, targeting mutated cell-surface neoepitopes absent from normal tissue. Mechanism: binding to mutant extracellular epitopes to mediate Fc-dependent effector functions (ADCC, macrophage phagocytosis) and complement-dependent cytotoxicity (CDC), with potential blockade of oncogenic receptor signaling.
Personalized chimeric monoclonal antibodies bind patient-specific mutated cell-surface neoepitopes on tumor cells, engaging Fcγ receptors to drive ADCC and macrophage phagocytosis and activating complement for CDC; may also block oncogenic receptor signaling when the target is a driver receptor.
Antibodies bind mutant extracellular neoepitopes on tumor cells, engage Fcγ receptors on NK cells/macrophages to drive ADCC and phagocytosis, and activate complement for CDC, causing lysis of target-expressing cells.
Chimeric anti-CD20 monoclonal antibody that depletes B cells via ADCC, complement-dependent cytotoxicity, and apoptosis; administered intralesionally in this trial.
Binds CD20 on B cells and depletes CD20+ malignant and normal B cells via Fc-mediated ADCC, complement-dependent cytotoxicity, and induction of apoptosis.
Rituximab binds CD20 on B cells and recruits immune effectors via its Fc to mediate ADCC, activates complement for CDC, and can induce apoptosis, leading to direct killing of CD20+ cells.
Genetically engineered T cells (autologous or donor-derived) modified to express a chimeric antigen receptor targeting CD33 (Siglec-3) on AML cells. Following IV infusion, the CAR provides CD3ζ signaling with co-stimulation to drive antigen-dependent T-cell activation and HLA-independent cytotoxicity (granule release and cytokines) against CD33+ AML blasts and normal myeloid progenitors/monocytes.
Autologous or donor-derived T cells engineered to express a CD33-specific chimeric antigen receptor; CAR engagement of CD33 on AML cells triggers CD3ζ-based signaling with co-stimulation, leading to antigen-dependent, HLA-independent T-cell activation and cytotoxic killing (perforin/granzyme release and cytokines) of CD33+ blasts and normal myeloid progenitors.
CD33-specific CAR T cells bind CD33 on target cells and, upon CAR activation, kill them via perforin/granzyme-mediated cytotoxicity (antigen-dependent, HLA-independent).
Subcutaneous bispecific T-cell–redirecting monoclonal antibody (anti-BCMA×CD3) that binds BCMA on malignant plasma cells and CD3 on T cells to activate and redirect T-cell cytotoxicity against myeloma cells.
Bispecific anti-BCMA×CD3 monoclonal antibody that binds BCMA on myeloma cells and CD3 on T cells, bringing them into proximity to activate and redirect T-cell cytotoxicity for targeted lysis of BCMA-expressing plasma cells.
BCMA-CD3 bispecific antibody bridges CD3+ T cells to BCMA+ cells, activating T cells to form an immune synapse and kill via perforin/granzyme-mediated cytolysis.