Anti-HER2 monoclonal antibody that blocks HER2 dimerization.
Humanized anti-HER2 IgG1 monoclonal antibody that binds the HER2 extracellular dimerization domain (subdomain II), blocking HER2 heterodimerization (especially with HER3), thereby preventing downstream signaling (PI3K/AKT, MAPK) and inhibiting tumor cell proliferation; can also mediate ADCC.
YES
DIRECT
Pertuzumab binds HER2 on target cells and its Fc engages FcγR-expressing immune cells (e.g., NK cells), triggering antibody-dependent cellular cytotoxicity (ADCC) to kill the cells; HER2 signaling blockade can also promote apoptosis.
An intravenous SIRPα–Fc fusion protein biologic that acts as a decoy to bind CD47 on tumor cells, blocking the CD47–SIRPα innate immune checkpoint to restore macrophage-mediated phagocytosis and, via its Fc region, engage Fcγ receptors to enhance myeloid effector functions and dendritic cell antigen presentation, supporting downstream T-cell priming.
HCB101 is an IV SIRPalpha-Fc fusion protein that binds CD47 on tumor cells and blocks the CD47-SIRPalpha innate immune checkpoint, removing the 'don't-eat-me' signal. This restores macrophage-mediated phagocytosis and, via its IgG4 Fc domain, engages Fc-gamma receptors to enhance myeloid effector functions and dendritic cell antigen presentation, supporting downstream T-cell priming.
NO
INDIRECT
HCB101 targets CD47 on tumor cells to relieve the SIRPα ‘don’t‑eat‑me’ signal, enabling macrophage phagocytosis; its IgG4 Fc engages FcγRs (including CD32C) on myeloid cells to enhance effector function, but it does not target or kill CD32C-expressing cells.
An intravenous SIRPα–Fc fusion protein biologic that acts as a decoy to bind CD47 on tumor cells, blocking the CD47–SIRPα innate immune checkpoint to restore macrophage-mediated phagocytosis and, via its Fc region, engage Fcγ receptors to enhance myeloid effector functions and dendritic cell antigen presentation, supporting downstream T-cell priming.
HCB101 is an IV SIRPalpha-Fc fusion protein that binds CD47 on tumor cells and blocks the CD47-SIRPalpha innate immune checkpoint, removing the 'don't-eat-me' signal. This restores macrophage-mediated phagocytosis and, via its IgG4 Fc domain, engages Fc-gamma receptors to enhance myeloid effector functions and dendritic cell antigen presentation, supporting downstream T-cell priming.
NO
INDIRECT
HCB101 targets CD47 on tumor cells to unblock phagocytosis and engages Fcγ receptors to activate effector cells. CD16A (FcγRIIIa)–positive cells act as effectors via Fc engagement; they are not targeted or directly killed by the drug.
An intravenous SIRPα–Fc fusion protein biologic that acts as a decoy to bind CD47 on tumor cells, blocking the CD47–SIRPα innate immune checkpoint to restore macrophage-mediated phagocytosis and, via its Fc region, engage Fcγ receptors to enhance myeloid effector functions and dendritic cell antigen presentation, supporting downstream T-cell priming.
HCB101 is an IV SIRPalpha-Fc fusion protein that binds CD47 on tumor cells and blocks the CD47-SIRPalpha innate immune checkpoint, removing the 'don't-eat-me' signal. This restores macrophage-mediated phagocytosis and, via its IgG4 Fc domain, engages Fc-gamma receptors to enhance myeloid effector functions and dendritic cell antigen presentation, supporting downstream T-cell priming.
NO
INDIRECT
HCB101 does not target CD16B. It binds CD47 on tumor cells to block the CD47–SIRPα checkpoint and, via its IgG4 Fc, engages Fcγ receptors (including CD16B) on myeloid cells to enhance phagocytic/effector activity against CD47+ tumor cells; CD16B+ cells act as effectors, not targets.
Autologous, gene-modified chimeric antigen receptor (CAR) T cells produced with a non-viral vector, engineered to target mesothelin and MUC1 on tumor cells and to auto-secrete multifunctional antibodies to enhance antitumor immunity within the tumor microenvironment; evaluated in a dose-escalation regimen (5×10^5, 1×10^6, 5×10^6 cells/kg).
Autologous T cells engineered with a non-viral vector to express chimeric antigen receptors recognizing mesothelin and MUC1 on tumor cells, triggering CAR-mediated T-cell activation and cytolytic killing via CD3ζ and costimulatory signaling; additionally engineered to secrete multifunctional antibodies within the tumor microenvironment to enhance antitumor immunity (e.g., overcoming immunosuppression/checkpoints) and amplify T-cell activity.
YES
DIRECT
CAR T cells recognize mesothelin via their CAR, activating CD3ζ/costimulatory signaling and killing mesothelin-expressing cells through perforin/granzyme release and death-receptor pathways.