Anti-CD22 antibody–drug conjugate delivering calicheamicin to induce DNA double-strand breaks in B-cell blasts.
Humanized anti-CD22 monoclonal antibody linked to calicheamicin; upon CD22 binding and internalization in B-cell blasts, the payload is released to bind the DNA minor groove and cause double-strand breaks, leading to apoptosis.
The anti-CD22 ADC binds CD22, is internalized, and releases calicheamicin inside the cell, which binds the DNA minor groove to cause double-strand breaks and apoptosis.
Anti-CD20 monoclonal antibody that mediates B-cell depletion via ADCC and complement-dependent cytotoxicity.
Chimeric anti-CD20 monoclonal antibody that binds CD20 on pre-B and mature B cells and induces B-cell depletion via antibody-dependent cellular cytotoxicity and complement-dependent cytotoxicity, with potential direct apoptotic signaling.
Anti-CD20 antibody coats CD20+ B cells, engaging FcγR-bearing effectors to mediate ADCC and activating complement for CDC; may also trigger apoptosis via CD20 signaling.
Anti-EGFR monoclonal antibody that blocks EGFR signaling (effective in RAS/RAF wild-type tumors).
Cetuximab is a chimeric anti-EGFR monoclonal antibody that binds the extracellular domain of EGFR, blocks ligand binding and receptor dimerization, thereby inhibiting downstream MAPK/PI3K signaling to suppress tumor cell proliferation and survival; efficacy is seen in RAS/RAF wild-type tumors and it may also mediate ADCC via its Fc region.
Binds EGFR on target cells and engages Fcγ receptors on immune effector cells to trigger ADCC (and can activate complement), killing EGFR+ cells; EGFR blockade may also promote apoptosis.
Autologous, gene-modified T cells engineered ex vivo to express a chimeric antigen receptor targeting a plasma cell surface antigen; upon infusion, they enable MHC-independent recognition and killing of malignant plasma cells via T-cell activation, expansion, cytokine release, and perforin/granzyme-mediated cytotoxicity in relapsed/refractory multiple myeloma and plasma cell leukemia.
Autologous T cells are gene‑modified ex vivo to express a chimeric antigen receptor that binds a plasma cell surface antigen, enabling MHC‑independent recognition of malignant plasma cells. After infusion, CAR signaling activates and expands the T cells, induces cytokine release, and drives perforin/granzyme‑mediated cytotoxic killing of multiple myeloma/plasma cell leukemia cells.
CAR-expressing T cells recognize the target antigen and directly kill antigen-positive cells via perforin/granzyme-mediated cytotoxicity after CAR engagement.
Fully human IgG1 monoclonal antibody targeting CD38, administered by IV infusion. Binds CD38 on antibody-secreting plasma cells and other CD38+ immune cells, inducing depletion via Fc-mediated cytotoxicity (ADCC, CDC, ADCP) and apoptosis to reduce donor-specific antibodies and humoral alloimmunity driving AMR.
Fully human IgG1 anti-CD38 monoclonal antibody that binds CD38 on plasma cells and other CD38+ immune cells and depletes them via Fc-mediated effector functions (ADCC, CDC, ADCP) and apoptosis, thereby reducing donor-specific antibodies and humoral alloimmunity.
Anti-CD38 IgG1 binds CD38 on target cells and recruits Fc-mediated effectors—NK-cell ADCC, complement-dependent cytotoxicity (CDC), and macrophage ADCP—and can trigger apoptosis, leading to depletion of CD38+ cells.