OctaV

OctaV is an engineered, dual-function recombinant fusion protein designed to concurrently mimic both intrinsic-tenase and prothrombinase complexes. Developed by researchers at the Children's Hospital of Philadelphia and the University of Pennsylvania, OctaV is constructed by fusing a single-chain variable fragment (scFv) derived from the factor IXa (FIXa)-binding arm of emicizumab to the C-terminus of "FV Short," a naturally occurring factor V (FV) variant with a truncated B-domain. This design leverages the high-affinity membrane-binding properties of the FV C1 and C2 domains to anchor FIXa to the membrane, while also facilitating the intramolecular channeling of nascent factor Xa (FXa) directly to the FVa moiety. In preclinical coagulation assays, OctaV demonstrated potent dual cofactor activity, correcting clotting defects in FV-deficient, FVIII-deficient, and combined FV/FVIII-deficient plasmas, with FVIII-mimetic activity surpassing that of emicizumab. It is being investigated as a potential therapeutic candidate for hemophilia A (FVIII deficiency) and combined FV/FVIII deficiency.

Other names

OctaV