A humanized anti-CD52 monoclonal antibody used as a lymphocyte-depleting immunosuppressant; it binds CD52 on mature lymphocytes and depletes T and B cells via antibody-dependent cellular cytotoxicity, complement-mediated cytotoxicity, and apoptosis.
Humanized anti-CD52 IgG1 monoclonal antibody that binds CD52 on mature lymphocytes and depletes T and B cells (and some NK cells/monocytes) via antibody-dependent cellular cytotoxicity, complement-mediated cytotoxicity, and apoptosis, leading to profound lymphocyte depletion and immunosuppression.
YES
DIRECT
Alemtuzumab binds CD52 on lymphocytes and triggers Fc-mediated killing via ADCC (NK cells/macrophages) and complement-dependent cytotoxicity (CDC), and can induce apoptosis of the bound cells.
Subcutaneous therapeutic long-peptide vaccine derived from IDO and PD-L1 designed to elicit Th1/CD8+ T-cell responses against IDO- and PD-L1–expressing cells, reduce immunosuppressive cells, and reprogram the tumor microenvironment (targets PD-1/PD-L1 axis and IDO1 pathway).
Subcutaneous long‑peptide cancer vaccine combining IDO1- and PD-L1–derived peptides (with Montanide ISA‑51) to prime Th1/CD8+ cytotoxic T-cell responses against IDO1/PD-L1–expressing tumor and immunosuppressive cells, reducing Tregs/MDSCs and reversing PD-1/PD-L1 and IDO1-mediated immune suppression to enhance anti-tumor immunity.
YES
INDIRECT
Peptide vaccine primes PD-L1–specific CD8+ T cells that recognize PD-L1–derived epitopes on target cells and kill them via CTL-mediated lysis (perforin/granzyme).
Subcutaneous therapeutic long-peptide vaccine derived from IDO and PD-L1 designed to elicit Th1/CD8+ T-cell responses against IDO- and PD-L1–expressing cells, reduce immunosuppressive cells, and reprogram the tumor microenvironment (targets PD-1/PD-L1 axis and IDO1 pathway).
Subcutaneous long‑peptide cancer vaccine combining IDO1- and PD-L1–derived peptides (with Montanide ISA‑51) to prime Th1/CD8+ cytotoxic T-cell responses against IDO1/PD-L1–expressing tumor and immunosuppressive cells, reducing Tregs/MDSCs and reversing PD-1/PD-L1 and IDO1-mediated immune suppression to enhance anti-tumor immunity.
YES
INDIRECT
Peptide vaccine primes IDO1-specific CD8+ T cells that recognize IDO1-derived peptides on MHC I and kill IDO1-expressing cells via perforin–granzyme–mediated apoptosis.
A biologic monoclonal antibody designed as an immune-checkpoint agonist targeting PSGL-1 on T cells. It aims to selectively attenuate chronically activated effector/memory T cells via activation-induced cell death and dampening of TCR-driven signaling, reducing proinflammatory cytokine production; administered subcutaneously in single- and multiple-ascending doses.
Monoclonal antibody agonist of the immune checkpoint PSGL-1 on T cells that triggers inhibitory signaling to selectively attenuate chronically activated effector/memory T cells, inducing activation‑induced cell death and dampening TCR-driven signaling, thereby reducing proinflammatory cytokine production while sparing resting/naive T cells.
YES
DIRECT
Agonist engagement of PSGL-1 on chronically activated effector/memory T cells triggers inhibitory signaling that induces activation-induced cell death (apoptosis) of the PSGL-1–expressing T cells.
Maternal CMV-specific cytotoxic T lymphocytes used as adoptive cellular immunotherapy; generated/selected with CMV peptide pools to recognize CMV peptide–HLA complexes on infected cells and mediate antigen-specific killing via perforin/granzyme and IFN-γ, restoring antiviral immunity.
Adoptively transferred maternal cytotoxic T lymphocytes selected/expanded for native TCR recognition of CMV peptide–HLA complexes on infected cells; upon engagement they mediate antigen-specific killing via perforin/granzyme release and secrete cytokines (e.g., IFN-γ), restoring CMV-specific cellular immunity without genetic engineering.
YES
DIRECT
Adoptively transferred CMV-specific CTLs recognize CMV pp65 peptide–HLA I via their native TCR and kill target cells by releasing cytotoxic granules (perforin/granzymes) leading to apoptosis (and possibly Fas/FasL signaling).