A fully human IgG1κ monoclonal antibody that binds the conserved AD-2 site I epitope on HCMV glycoprotein B (gB), neutralizing virus by blocking gB-mediated attachment/fusion and cell-to-cell spread, and engaging Fc-mediated effector functions (ADCC and complement).
Fully human IgG1κ monoclonal antibody that binds the conserved AD‑2 site I epitope on HCMV glycoprotein B (gB), neutralizing virus by blocking gB‑mediated attachment/fusion and cell‑to‑cell spread, while engaging Fc‑mediated effector functions (ADCC and complement) to enhance clearance.
NO
INDIRECT
TRL345 binds HCMV gB on virions/infected cells; its Fc engages Fcγ receptors (including CD64) on effector cells to mediate ADCC/complement against gB+ infected cells. CD64+ cells serve as effectors, not targets, and are not killed.
A fully human IgG1κ monoclonal antibody that binds the conserved AD-2 site I epitope on HCMV glycoprotein B (gB), neutralizing virus by blocking gB-mediated attachment/fusion and cell-to-cell spread, and engaging Fc-mediated effector functions (ADCC and complement).
Fully human IgG1κ monoclonal antibody that binds the conserved AD‑2 site I epitope on HCMV glycoprotein B (gB), neutralizing virus by blocking gB‑mediated attachment/fusion and cell‑to‑cell spread, while engaging Fc‑mediated effector functions (ADCC and complement) to enhance clearance.
NO
INDIRECT
TRL345 binds HCMV gB on virions/infected cells and recruits FcγR-bearing effectors (via its Fc) to mediate ADCC/complement against gB-expressing infected cells. CD32A+ cells serve as effector cells, not targets, and are not killed by the drug.
A fully human IgG1κ monoclonal antibody that binds the conserved AD-2 site I epitope on HCMV glycoprotein B (gB), neutralizing virus by blocking gB-mediated attachment/fusion and cell-to-cell spread, and engaging Fc-mediated effector functions (ADCC and complement).
Fully human IgG1κ monoclonal antibody that binds the conserved AD‑2 site I epitope on HCMV glycoprotein B (gB), neutralizing virus by blocking gB‑mediated attachment/fusion and cell‑to‑cell spread, while engaging Fc‑mediated effector functions (ADCC and complement) to enhance clearance.
NO
INDIRECT
TRL345 targets HCMV glycoprotein B, not C1q. It neutralizes virus and can mediate ADCC/CDC against gB-expressing infected cells; C1q A chain is only recruited via Fc for complement activation and is not a cytotoxic target.
Autologous tumor-infiltrating lymphocyte (TIL) cellular therapy manufactured from a patient’s tumor, expanded ex vivo, and reinfused to mediate antitumor activity through native TCR recognition, cytotoxic mechanisms, and cytokine secretion.
Autologous TILs expanded ex vivo and reinfused; they recognize patient-specific tumor antigens via native TCR–MHC interactions and mediate antitumor effects through cytotoxic killing (perforin/granzymes) and cytokine secretion within the tumor microenvironment.
YES
DIRECT
Autologous TILs recognize the peptide–HLA class II complex via native TCRs and kill the presenting cells through perforin/granzyme-mediated cytolysis and related T-cell effector pathways.
A fully human IgG1κ monoclonal antibody that binds the conserved AD-2 site I epitope on HCMV glycoprotein B (gB), neutralizing virus by blocking gB-mediated attachment/fusion and cell-to-cell spread, and engaging Fc-mediated effector functions (ADCC and complement).
Fully human IgG1κ monoclonal antibody that binds the conserved AD‑2 site I epitope on HCMV glycoprotein B (gB), neutralizing virus by blocking gB‑mediated attachment/fusion and cell‑to‑cell spread, while engaging Fc‑mediated effector functions (ADCC and complement) to enhance clearance.
NO
INDIRECT
TRL345 targets HCMV glycoprotein B and can mediate ADCC/CDC against gB-expressing infected cells; it does not bind Complement component C1q B chain, so cells expressing C1qB are not targeted or killed.