A T-cell-engaging bispecific IgG antibody (CD20xCD3) that binds CD20 on B cells and CD3 on T cells to form an immune synapse, activating T cells to kill malignant B cells via cytotoxic granule release and cytokines.
Bispecific IgG antibody that binds CD3 on T cells and CD20 on B cells, forming an immune synapse that activates T cells to release cytotoxic granules and cytokines, resulting in targeted lysis of CD20+ malignant B cells.
NO
INDIRECT
Binding to CD3 activates T cells; the activated T cells kill CD20+ B cells via immune-synapse–mediated perforin/granzyme release. CD3+ T cells are not the cells killed.
MicAbody adaptor protein (bispecific antibody; also known as ASP101G) that binds CD20 and carries an orthogonal NKG2D ligand to dock and activate ASP2802 convertible CAR T cells, enabling titratable on/off targeting.
MA-20 (ASP101G) is a MicAbody bispecific adaptor that binds CD20 on B cells and carries an orthogonal NKG2D ligand to engage and activate ASP2802 convertible CAR T cells. By bridging CD20+ tumor cells to the engineered CAR T receptor, it enables titratable, on/off CAR T cytotoxic activity against CD20-positive malignancies.
YES
DIRECT
MA-20 binds CD20 on target cells and engages ASP2802 convertible CAR T cells via an orthogonal NKG2D ligand, bridging them to CD20+ cells and triggering CAR T–mediated killing (perforin/granzyme-dependent lysis).
A HER2-targeted antibody–drug conjugate delivering the maytansinoid DM1 (microtubule inhibitor) via a non-cleavable linker; inhibits mitosis and mediates HER2 signaling blockade and ADCC.
HER2-targeted monoclonal antibody-drug conjugate (trastuzumab linked via a non-cleavable linker to the maytansinoid DM1). After binding HER2, it is internalized and degraded to release a DM1 catabolite that inhibits microtubules, causing mitotic arrest and apoptosis; the trastuzumab component also blocks HER2 signaling and mediates ADCC.
NO
INDIRECT
T-DM1 targets HER2, not beta-tubulin. After HER2-mediated internalization, the DM1 payload binds beta-tubulin to disrupt microtubules, causing mitotic arrest and apoptosis; trastuzumab can also mediate ADCC.
Long-acting (LS-engineered) human IgG1 broadly neutralizing monoclonal antibody targeting the HIV-1 Env gp120 CD4-binding site; neutralizes free virions, blocks Env–CD4/coreceptor-mediated entry, and can recruit Fc-mediated effector functions.
LS-engineered human IgG1 broadly neutralizing monoclonal antibody targeting the HIV-1 Env gp120 CD4-binding site; neutralizes free virions and blocks Env–CD4/coreceptor-mediated entry. The Fc domain can recruit effector functions (e.g., ADCC/ADCP) against Env-expressing infected cells, and LS mutations enhance FcRn binding to extend serum half-life.
YES
DIRECT
The IgG1 bNAb binds gp120 on Env-expressing infected cells and its Fc recruits effector functions—primarily NK cell–mediated ADCC and macrophage/monocyte ADCP; it may also trigger complement (CDC)—resulting in killing of the target cells.
Long-acting (LS-engineered) human IgG1 broadly neutralizing monoclonal antibody targeting the HIV-1 Env gp120 CD4-binding site; neutralizes free virions, blocks Env–CD4/coreceptor-mediated entry, and can recruit Fc-mediated effector functions.
LS-engineered human IgG1 broadly neutralizing monoclonal antibody targeting the HIV-1 Env gp120 CD4-binding site; neutralizes free virions and blocks Env–CD4/coreceptor-mediated entry. The Fc domain can recruit effector functions (e.g., ADCC/ADCP) against Env-expressing infected cells, and LS mutations enhance FcRn binding to extend serum half-life.
NO
INDIRECT
FcRn engagement by the LS-engineered Fc only recycles IgG and extends half-life; it does not trigger cytotoxicity. Killing occurs only when the antibody binds HIV-1 Env on infected cells, enabling Fc-mediated ADCC/ADCP against Env+ cells, not FcRn+ cells.