Researchers have determined the structure of a human antibody bound to the Zika virus, revealing details about how the antibody interferes with the infection mechanism – findings that could aid in development of antiviral medications.

The new findings also suggest the antibody might be especially effective because a lower concentration than expected is needed to inhibit a key mechanism of infection, making it more potent than previous antibodies studied. The research was performed by a team from Purdue University, Vanderbilt University Medical Center and the Washington University School of Medicine.

The human antibody was isolated by the Vanderbilt and Washington University researchers, who reported their findings earlier this year. Those findings showed that the antibody, which was isolated from a person previously infected with Zika virus, neutralizes Zika strains that belong to African, Asian and American lineages and is able to reduce fetal infection and death in mice.

“However, until now what remained unknown was the mechanism of neutralization of Zika infection by the antibody and the structural basis for neutralization,” said Michael Rossmann, Purdue’s Hanley Distinguished Professor of Biological Sciences.

The findings were reported March 16 in the journal Nature Communications.

In the new findings, researchers determined the combined three–dimensional structure of the Zika virus while attached to a key binding site on the antibody known as the antigen binding fragment, or a Fab molecule.