A human IgG1κ monoclonal antibody administered intravenously with FcRn-enhanced half-life that binds the “a” determinant on hepatitis B surface antigen (HBsAg). It neutralizes HBV virions and subviral particles, forms immune complexes to accelerate antigen clearance, engages Fcγ receptor–mediated effector functions (e.g., ADCC, phagocytosis), and lowers circulating HBsAg to mitigate T-cell exhaustion and potentially restore adaptive immune responses.
Human IgG1κ monoclonal antibody with FcRn-enhanced half-life that binds the “a” determinant of hepatitis B surface antigen (HBsAg). It neutralizes HBV virions and subviral particles and forms immune complexes that accelerate antigen clearance, while engaging Fcγ receptors to drive ADCC and phagocytosis. By lowering circulating HBsAg, it may reduce T-cell exhaustion and help restore HBV-specific adaptive immune responses.
NO
INDIRECT
The antibody binds HBsAg; its Fc engages CD16a on NK cells/monocytes to drive ADCC and phagocytosis against HBsAg-bearing targets. CD16a-expressing cells act as effectors and are not killed.
A human IgG1κ monoclonal antibody administered intravenously with FcRn-enhanced half-life that binds the “a” determinant on hepatitis B surface antigen (HBsAg). It neutralizes HBV virions and subviral particles, forms immune complexes to accelerate antigen clearance, engages Fcγ receptor–mediated effector functions (e.g., ADCC, phagocytosis), and lowers circulating HBsAg to mitigate T-cell exhaustion and potentially restore adaptive immune responses.
Human IgG1κ monoclonal antibody with FcRn-enhanced half-life that binds the “a” determinant of hepatitis B surface antigen (HBsAg). It neutralizes HBV virions and subviral particles and forms immune complexes that accelerate antigen clearance, while engaging Fcγ receptors to drive ADCC and phagocytosis. By lowering circulating HBsAg, it may reduce T-cell exhaustion and help restore HBV-specific adaptive immune responses.
NO
INDIRECT
The antibody binds HBsAg on virions or infected cells and, via its Fc, engages Fcγ receptors (including CD32a) on immune effector cells to trigger ADCC and phagocytosis of HBsAg-bearing targets; CD32a+ cells act as effectors and are not killed.
TROP2-directed antibody–drug conjugate targeting TACSTD2 on epithelial tumor cells; internalization and payload release lead to cytotoxicity in TROP2-expressing cells.
TROP2 (TACSTD2)-directed IgG1 antibody–drug conjugate linked via a cleavable linker to SHR9265 (an exatecan-derived topoisomerase I inhibitor). After binding TROP2 on tumor cells and internalization, linker cleavage releases the payload, inhibiting topoisomerase I, blocking DNA replication and inducing cell cycle arrest and apoptosis in TROP2-expressing cells.
NO
INDIRECT
The ADC binds TROP2 on tumor cells, is internalized, and releases an exatecan-derived payload that inhibits DNA topoisomerase I, causing DNA damage and apoptosis in TROP2-expressing cells; TOP1 expression itself is not the delivery target.
A human IgG1κ monoclonal antibody administered intravenously with FcRn-enhanced half-life that binds the “a” determinant on hepatitis B surface antigen (HBsAg). It neutralizes HBV virions and subviral particles, forms immune complexes to accelerate antigen clearance, engages Fcγ receptor–mediated effector functions (e.g., ADCC, phagocytosis), and lowers circulating HBsAg to mitigate T-cell exhaustion and potentially restore adaptive immune responses.
Human IgG1κ monoclonal antibody with FcRn-enhanced half-life that binds the “a” determinant of hepatitis B surface antigen (HBsAg). It neutralizes HBV virions and subviral particles and forms immune complexes that accelerate antigen clearance, while engaging Fcγ receptors to drive ADCC and phagocytosis. By lowering circulating HBsAg, it may reduce T-cell exhaustion and help restore HBV-specific adaptive immune responses.
NO
INDIRECT
The antibody binds HBsAg and engages FcγRI (CD64) on effector cells via its Fc to drive ADCC/phagocytosis of HBsAg-bearing targets; CD64+ cells serve as effectors and are not killed.
A human IgG1κ monoclonal antibody administered intravenously with FcRn-enhanced half-life that binds the “a” determinant on hepatitis B surface antigen (HBsAg). It neutralizes HBV virions and subviral particles, forms immune complexes to accelerate antigen clearance, engages Fcγ receptor–mediated effector functions (e.g., ADCC, phagocytosis), and lowers circulating HBsAg to mitigate T-cell exhaustion and potentially restore adaptive immune responses.
Human IgG1κ monoclonal antibody with FcRn-enhanced half-life that binds the “a” determinant of hepatitis B surface antigen (HBsAg). It neutralizes HBV virions and subviral particles and forms immune complexes that accelerate antigen clearance, while engaging Fcγ receptors to drive ADCC and phagocytosis. By lowering circulating HBsAg, it may reduce T-cell exhaustion and help restore HBV-specific adaptive immune responses.
NO
INDIRECT
FcRn binding is used for IgG recycling and half-life extension; the antibody targets HBsAg, with any killing mediated via Fc gamma receptor–dependent ADCC/ADCP against HBsAg-bearing virions or infected cells, not FcRn-expressing cells.