Crystal Structure Determined for Binding Site of Zika/Dengue Neutralizing Antibodies

The X-ray crystal structure of the antibody in complex with the envelope protein of Zika virus revealed details of a conserved epitope, which was also the site of interaction of the envelope protein dimer with the precursor prM protein during virus maturation. This binding site on the Zika virus is the same as the one on the dengue virus, raising the possibility of producing a vaccine that would stimulate the production of antibodies capable of binding to and neutralizing both types of virus at the same time.

"We wanted to see whether the antibodies isolated for dengue could be used to neutralize other flaviviruses, and Zika seemed like the best candidate," said senior author Dr. Félix Rey, head of the structural virology laboratory at the Institut Pasteur. "We never expected to discover that the dengue virus and the Zika virus are so close that some antibodies produced against the dengue virus could also neutralize the Zika virus so potently. The antibodies could be used, for example, to protect pregnant women at risk of contracting the Zika virus, because there is currently no vaccine or treatment for this disease."

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