Anti-CD38 IgG1 monoclonal antibody that targets CD38 on malignant plasma cells, mediating ADCC/CDC, inducing apoptosis, and modulating CD38 ectoenzyme activity.
Human IgG1 monoclonal antibody against CD38 on malignant plasma cells; binding triggers Fc-mediated ADCC and complement-dependent cytotoxicity, directly induces apoptosis, and inhibits/modulates CD38 ectoenzyme activity, leading to depletion of CD38-positive tumor cells.
YES
DIRECT
Isatuximab binds CD38 on target cells and triggers Fc-mediated ADCC and complement-dependent cytotoxicity; it can also directly induce apoptosis, killing CD38+ cells.
Disitamab vedotin (RC48) is an anti-HER2 antibody–drug conjugate composed of a humanized monoclonal antibody linked to the cytotoxic payload monomethyl auristatin E (MMAE), a microtubule inhibitor. After binding HER2 on tumor cells, the ADC is internalized and releases MMAE to disrupt microtubules, causing G2/M arrest and apoptosis; the antibody may also mediate ADCC and inhibit HER2 signaling.
Anti-HER2 antibody-drug conjugate that binds HER2 on tumor cells, is internalized, and releases the microtubule inhibitor MMAE to inhibit tubulin polymerization, causing G2/M cell-cycle arrest and apoptosis; the antibody may also mediate ADCC and inhibit HER2 signaling.
YES
DIRECT
The ADC binds HER2, is internalized, and releases MMAE, which inhibits tubulin polymerization causing G2/M arrest and apoptosis; the antibody Fc can also mediate ADCC against HER2+ cells.
Disitamab vedotin (RC48) is an anti-HER2 antibody–drug conjugate composed of a humanized monoclonal antibody linked to the cytotoxic payload monomethyl auristatin E (MMAE), a microtubule inhibitor. After binding HER2 on tumor cells, the ADC is internalized and releases MMAE to disrupt microtubules, causing G2/M arrest and apoptosis; the antibody may also mediate ADCC and inhibit HER2 signaling.
Anti-HER2 antibody-drug conjugate that binds HER2 on tumor cells, is internalized, and releases the microtubule inhibitor MMAE to inhibit tubulin polymerization, causing G2/M cell-cycle arrest and apoptosis; the antibody may also mediate ADCC and inhibit HER2 signaling.
NO
INDIRECT
The ADC binds HER2 on tumor cells, is internalized, and releases MMAE, which then binds β‑tubulin (vinca site) to disrupt microtubules, causing G2/M arrest and apoptosis. β‑tubulin expression alone does not lead to targeting or killing.
Autologous dendritic cell vaccine generated ex vivo from a patient’s peripheral blood monocytes, differentiated into dendritic cells and pulsed with multiple EBV antigens to prime EBV-specific T-cell responses against EBV-positive nasopharyngeal carcinoma; dosed 5×10^6 cells subcutaneously every 2 weeks for 3–5 doses.
Autologous monocyte-derived dendritic cells pulsed ex vivo with EBV antigens are re-administered to present these antigens via MHC I/II, priming and expanding EBV-specific CD8+ cytotoxic T cells and CD4+ helper T cells. The resulting Th1/IFN-γ–biased response targets and lyses EBV-positive tumor cells in nasopharyngeal carcinoma.
YES
INDIRECT
The DC vaccine primes EBV-specific T cells; EBNA1-expressing tumor cells presenting EBNA1 peptides on MHC are recognized by EBV-specific CD8+ CTLs and lysed via perforin/granzyme-mediated apoptosis (with Th1 CD4+ help).
Autologous dendritic cell vaccine generated ex vivo from a patient’s peripheral blood monocytes, differentiated into dendritic cells and pulsed with multiple EBV antigens to prime EBV-specific T-cell responses against EBV-positive nasopharyngeal carcinoma; dosed 5×10^6 cells subcutaneously every 2 weeks for 3–5 doses.
Autologous monocyte-derived dendritic cells pulsed ex vivo with EBV antigens are re-administered to present these antigens via MHC I/II, priming and expanding EBV-specific CD8+ cytotoxic T cells and CD4+ helper T cells. The resulting Th1/IFN-γ–biased response targets and lyses EBV-positive tumor cells in nasopharyngeal carcinoma.
YES
INDIRECT
DC vaccination primes EBV-specific CD8+ T cells that recognize LMP1-derived peptides on MHC I of EBV+ cells and kill them via perforin/granzyme (and Fas–FasL), supported by a Th1/IFN-γ response.