A detailed analysis of the experimental Ebola treatment ZMAb, published in Scientific Reports, explores how this drug recognizes and neutralizes Ebola virus. The study confirms that ZMAb binds to specific structures on the virus to achieve efficient neutralization. Moreover, the work indicates that information regarding the structure of the target protein and the binding site of antibodies can be used to rationally design future drugs against related viruses.
Cocktails of monoclonal antibodies (mAbs) - proteins that bind to proteins on the surface of viruses - have shown promising results for the treatment and prevention of Ebola virus infection. One such cocktail is ZMAb, which consists of three antibodies extracted from mice that have been vaccinated against Ebola virus. Xiangguo Qiu and colleagues explore the molecular properties of the three mAbs in more detail and show that all three are capable of neutralizing the Mayinga Ebola virus (a variant from the 1976 Zaire outbreak). The authors demonstrate that the mAbs target specific portions of the glycoprotein present of the surface of the virus, particularly a region called the glycan cap and the interface between two protein subunits, GP1 and GP2. These results suggest that combinations antibodies targeting the GP1-GP2 and the glycan cap are needed to provide protection against Ebola virus infection.