A human anti-EphA5 monoclonal antibody–drug conjugate that binds EphA5 on tumor cells, is internalized, and releases the cytotoxic payload MMAE to inhibit tubulin polymerization, causing G2/M arrest and apoptosis in advanced solid tumors.
Human anti-EphA5 IgG1 antibody linked via a protease-cleavable linker to MMAE. After binding EphA5 on tumor cells and internalization, the linker is cleaved to release MMAE, which inhibits tubulin polymerization, causing G2/M cell-cycle arrest and apoptosis in EphA5-expressing cancer cells.
Anti-EphA5 ADC binds EphA5, is internalized, linker is cleaved to release MMAE, which inhibits tubulin polymerization, causing G2/M arrest and apoptosis of EphA5-expressing cells.
Fully human anti-CD20 monoclonal antibody that depletes CD20+ B cells via complement-dependent cytotoxicity and ADCC to reduce pathogenic autoantibodies in pemphigus vulgaris.
Fully human anti-CD20 IgG1 monoclonal antibody that binds CD20 on B cells and depletes CD20+ B cells via complement-dependent cytotoxicity and antibody-dependent cell-mediated cytotoxicity, thereby reducing pathogenic autoantibody production.
Ofatumumab binds CD20 on B cells and triggers complement-dependent cytotoxicity and Fc-mediated ADCC (e.g., by NK cells), leading to lysis of CD20+ cells.
Allogeneic anti-CD20 CAR-engineered gamma-delta (γδ) T-cell therapy that targets and depletes CD20-positive B cells to reduce autoantibody production and B cell–driven inflammation in autoimmune diseases.
Allogeneic gamma-delta T cells engineered with an anti-CD20 chimeric antigen receptor bind CD20 on B cells independent of MHC, become activated, and kill CD20+ B cells via cytotoxic effector mechanisms, depleting pathogenic B cells and reducing autoantibody-driven inflammation.
Anti-CD20 CAR γδ T cells bind CD20 on B cells, become activated, and directly kill the CD20+ cells via cytotoxic effector mechanisms (perforin/granzyme-mediated lysis and apoptosis; Fas/FasL), independent of MHC.
Autologous TCR-engineered T cell therapy targeting an HPV18-derived peptide presented by HLA-DRB1*0901; infused T cells recognize HPV18+ tumor cells and mediate cytotoxicity via TCR signaling, cytokine release, and perforin/granzyme pathways.
Autologous T cells are engineered to express a T-cell receptor that recognizes an HPV18-derived peptide presented by HLA-DRB1*0901 on tumor cells. Antigen recognition activates TCR signaling, leading to cytokine release and cytotoxic killing via perforin/granzyme pathways, selectively eliminating HPV18-positive tumor cells.
Engineered TCR T cells recognize the HPV18-derived peptide presented by HLA-DRB1*0901 on tumor cells, triggering TCR signaling and killing via perforin/granzyme-mediated cytolysis (with cytokine-driven apoptosis).
Chimeric IgG1 anti‑EGFR monoclonal antibody that inhibits EGFR signaling (RAS/RAF/MEK/ERK, PI3K/AKT), impairs DNA repair and cell‑cycle progression, and induces ADCC via NK cells; increases radiosensitivity.
Chimeric IgG1 monoclonal antibody against EGFR that binds the extracellular domain to block ligand binding, receptor activation and dimerization, thereby inhibiting downstream RAS/RAF/MEK/ERK and PI3K/AKT signaling; reduces proliferation, cell-cycle progression and DNA repair, induces NK cell–mediated ADCC via its Fc region, and increases radiosensitivity.
Cetuximab binds EGFR on target cells and its IgG1 Fc engages Fcγ receptors on NK cells to trigger antibody-dependent cellular cytotoxicity (ADCC), killing EGFR+ cells (with possible complement-mediated cytotoxicity). Signaling blockade is primarily cytostatic.