2G12

2G12 is a broadly neutralizing human monoclonal antibody (bNAb) that targets the HIV-1 envelope glycoprotein gp120. It is distinguished by its unique recognition of a dense cluster of alpha1->2 mannose residues on the glycan shield of gp120, rather than a protein-based epitope. This binding is achieved through a rare domain-swapped structure in which the two variable heavy (VH) domains interlock to form a single multivalent binding surface. Originally discovered by researchers at Polymun Scientific, 2G12 was one of the first bNAbs to enter clinical trials. Rockefeller University evaluated C2G12 (a clinical-grade version produced in CHO cells) both as a monotherapy and as part of a triple-antibody cocktail (with 2F5 and 4E10) to assess its safety and ability to suppress viral rebound in HIV-infected individuals undergoing analytical treatment interruption. While it demonstrated the ability to neutralize certain HIV strains, its clinical utility was limited by the rapid emergence of resistant mutations, and it has largely been superseded by more potent second-generation bNAbs.

Other names

anti-HIV-1 monoclonal antibody 2G12anti-HIV1 monoclonal antibody 2G12anti-HIV 1 monoclonal antibody 2G12human monoclonal antibody 2G12