Humanized IgG1 monoclonal antibody against EGFR (HER1/ErbB1); blocks ligand binding and downstream MAPK/ERK and PI3K/AKT signaling, inhibits proliferation, and can induce ADCC.
Humanized IgG1 monoclonal antibody targeting EGFR; binds the receptor’s extracellular domain to block ligand binding and receptor activation, inhibiting MAPK/ERK and PI3K/AKT signaling, suppressing tumor cell proliferation and survival, and engaging Fc-mediated ADCC.
Nimotuzumab (IgG1) binds EGFR on target cells and its Fc engages Fcγ receptors on immune effectors (e.g., NK cells), triggering ADCC (± some CDC), leading to lysis of EGFR+ cells; EGFR blockade also suppresses survival signaling.
Anti-EGFR IgG1 monoclonal antibody that blocks EGFR signaling and induces antibody-dependent cellular cytotoxicity (ADCC) via CD16 on NK cells.
Chimeric IgG1 monoclonal antibody that binds the extracellular domain of EGFR, blocking ligand binding and receptor dimerization to inhibit downstream signaling (e.g., MAPK/PI3K pathways), suppressing tumor cell proliferation; its Fc engages CD16 (FcγRIIIa) on NK cells to trigger antibody-dependent cellular cytotoxicity (ADCC).
Cetuximab binds EGFR on target cells and its IgG1 Fc engages CD16 (FcγRIIIa) on NK cells to trigger ADCC, leading to lysis of EGFR+ cells (with possible CDC/apoptosis).
Genetically modified autologous T cells engineered to express an HLA-A2–restricted T-cell receptor specific for NY-ESO-1, enabling recognition and cytotoxic killing of NY-ESO-1–expressing tumor cells.
Autologous T lymphocytes genetically modified to express an HLA-A2-restricted T-cell receptor specific for NY-ESO-1. These TCR-T cells recognize NY-ESO-1 peptide presented by HLA-A2 on tumor cells and, upon TCR engagement, activate cytotoxic effector functions (perforin/granzyme and cytokine release) to kill NY-ESO-1-positive cancer cells.
TCR-engineered autologous T cells recognize NY-ESO-1 peptide presented by HLA-A2 on tumor cells and directly kill them via perforin/granzyme-mediated cytotoxicity (and Fas-FasL apoptosis).
A humanized, afucosylated IgG1 monoclonal antibody (brand: Fasenra) that targets IL-5 receptor alpha (IL-5Rα) on eosinophils and basophils, blocks IL-5 signaling, and engages FcγRIIIa on NK cells to drive ADCC-mediated depletion of these cells; administered subcutaneously (e.g., 30 mg/10 mg) for eosinophilic asthma.
Benralizumab is an afucosylated humanized IgG1 monoclonal antibody that binds IL-5 receptor alpha on eosinophils and basophils, blocks IL-5 signaling, and engages FcγRIIIa on NK cells to trigger ADCC-mediated depletion of these cells, reducing eosinophilic inflammation.
Benralizumab binds IL-5Rα on eosinophils/basophils and its afucosylated IgG1 Fc engages FcγRIIIa on NK cells to induce antibody-dependent cellular cytotoxicity (ADCC), leading to apoptosis and depletion of the target cells.
Autologous anti-CD7 chimeric antigen receptor T-cell (CAR-T) therapy; patient T cells are engineered to express a CAR targeting CD7, and upon engagement they activate cytotoxic pathways to eliminate CD7+ malignant T cells.
Autologous T cells are engineered to express a chimeric antigen receptor that binds CD7 on T-lineage cells. Upon CD7 engagement, CAR signaling (CD3ζ with costimulatory domains) activates T‑cell cytotoxicity and cytokine release, leading to perforin/granzyme-mediated lysis of CD7+ malignant T-ALL/LL cells, with on‑target depletion of normal CD7+ T (and some NK) cells.
Anti-CD7 CAR-T cells recognize CD7 on target cells; CAR signaling activates T-cell effector functions, releasing perforin and granzymes (and Fas–FasL signaling), leading to lysis/apoptosis of CD7+ cells.