A HER2-targeted antibody–drug conjugate that binds HER2 on tumor cells, is internalized, and releases a cytotoxic payload to induce tumor cell death, with potential bystander and immunogenic effects.
Trastuzumab-based HER2-targeted antibody-drug conjugate (trastuzumab rezetecan). After binding HER2 on tumor cells and internalization, a cleavable linker releases a camptothecin-derived topoisomerase I inhibitor (rezetecan), which stabilizes topo I–DNA complexes, causing DNA strand breaks, replication arrest, and apoptosis; may produce bystander killing and immunogenic effects.
NO
INDIRECT
SHR-A1811 targets HER2 on the cell surface; after HER2-mediated uptake, it releases a camptothecin payload that inhibits topoisomerase I, causing DNA damage and apoptosis in HER2-positive cells (with possible bystander killing). Topoisomerase I itself is not the targeted antigen.
A recombinant human broadly neutralizing monoclonal antibody that targets the HIV-1 gp120 V3-glycan (N332) supersite to inhibit viral entry; neutralizes diverse HIV-1 strains and can mediate Fc-dependent effector functions (ADCC/ADCP). The LS Fc mutations enhance FcRn binding and extend serum half-life.
10-1074-LS is a broadly neutralizing human monoclonal antibody that binds the HIV-1 Env gp120 V3-glycan (N332) supersite, blocking Env–CD4 interactions and viral attachment/entry to neutralize diverse HIV-1 strains. Its Fc region can engage Fcγ receptors to mediate effector functions such as ADCC and ADCP, aiding clearance of virions/infected cells. LS Fc mutations (M428L/N434S) enhance FcRn binding, extending serum half-life.
NO
INDIRECT
10-1074-LS binds HIV-1 Env gp120 to neutralize virus and can trigger FcγR-mediated ADCC/ADCP against Env-expressing infected cells. Its FcRn (via LS mutations) interaction only recycles IgG to extend half-life and does not kill FcRn-expressing cells.
An investigational antibody–drug conjugate (ADC) administered intravenously every 2 weeks; a tumor-targeting monoclonal antibody binds a tumor-associated surface antigen, is internalized, and releases a cytotoxic payload inside cancer cells to induce targeted cell death.
A tumor-targeting monoclonal antibody binds a tumor-associated surface antigen, is internalized by cancer cells, and releases a linked cytotoxic payload intracellularly to induce targeted cell death.
YES
DIRECT
ADC binds the tumor-associated surface antigen, is internalized, and releases an intracellular cytotoxic payload that kills the antigen-positive cell (e.g., via DNA damage or microtubule disruption leading to apoptosis).
Anti‑HER2 antibody–drug conjugate (RC48) that delivers the microtubule inhibitor MMAE via a cleavable linker; binds HER2 on urothelial tumor cells, is internalized, releases MMAE to disrupt microtubules (G2/M arrest → apoptosis), with potential bystander effect and Fc‑mediated ADCC.
Anti-HER2 antibody–drug conjugate (RC48). The anti-HER2 IgG binds HER2 on tumor cells, is internalized, and a cleavable linker releases MMAE, which inhibits tubulin polymerization to induce G2/M arrest and apoptosis; may also mediate bystander killing and Fc-dependent ADCC.
YES
DIRECT
The anti-HER2 ADC binds HER2, is internalized, and releases MMAE that inhibits tubulin polymerization, causing G2/M arrest and apoptosis; Fc-mediated ADCC and bystander effects may also contribute.
Anti‑HER2 antibody–drug conjugate (RC48) that delivers the microtubule inhibitor MMAE via a cleavable linker; binds HER2 on urothelial tumor cells, is internalized, releases MMAE to disrupt microtubules (G2/M arrest → apoptosis), with potential bystander effect and Fc‑mediated ADCC.
Anti-HER2 antibody–drug conjugate (RC48). The anti-HER2 IgG binds HER2 on tumor cells, is internalized, and a cleavable linker releases MMAE, which inhibits tubulin polymerization to induce G2/M arrest and apoptosis; may also mediate bystander killing and Fc-dependent ADCC.
NO
INDIRECT
Disitamab vedotin targets HER2, is internalized, and releases MMAE, which binds the beta-tubulin (vinca domain) to block microtubule polymerization, causing G2/M arrest and apoptosis. Killing depends on HER2-mediated delivery, not on beta-tubulin expression itself.