hIgG1-D1

hIgG1-D1 is a human monoclonal antibody construct, specifically a VH-Fc fusion protein, developed to neutralize the SARS-CoV-2 virus. It was identified through the screening of a massive human antibody library against the receptor-binding domain (RBD) of the viral spike protein. The 'D1' refers to the specific VH domain clone, which was then fused to a human IgG1 Fc region to create the bivalent 'hIgG1-D1' molecule. Its mechanism of action involves high-affinity binding to the RBD, which sterically blocks the interaction between the virus and the human angiotensin-converting enzyme 2 (ACE2) receptor, thereby preventing viral entry into host cells. While it showed significant neutralizing potency in preclinical models, related constructs like Ab8 (AB-001) were prioritized for further clinical development by the University of Pittsburgh and its spin-off, Abound Bio.

Other names

D1 VH-FcD-1 VH-FcD 1 VH-FcD1 antibodyD-1 antibodyD 1 antibody