Structural basis of potent Zika–dengue virus antibody cross-neutralization

Giovanna Barba-Spaeth, Wanwisa Dejnirattisai, Alexander Rouvinski, Marie-Christine Vaney, Iris Medits, Arvind Sharma, Etienne Simon-Lorière, Anavaj Sakuntabhai, Cao-Lormeau Van-Mai, Ahmed Haouz, Patrick England, Karin Stiasny, Juthathip Mongkolsapaya, Franz X. Heinz (), Gavin R. Screaton () and Félix A. Rey ()
Additional contact information
Giovanna Barba-Spaeth: Institut Pasteur, Unité de Virologie Structurale
Wanwisa Dejnirattisai: Hammersmith campus, Imperial College London
Alexander Rouvinski: Institut Pasteur, Unité de Virologie Structurale
Marie-Christine Vaney: Institut Pasteur, Unité de Virologie Structurale
Iris Medits: Medical University of Vienna
Arvind Sharma: Institut Pasteur, Unité de Virologie Structurale
Etienne Simon-Lorière: Institut Pasteur, Unité de Génétique fonctionnelle des maladies infectieuses
Anavaj Sakuntabhai: Institut Pasteur, Unité de Génétique fonctionnelle des maladies infectieuses
Cao-Lormeau Van-Mai: Unit of Emerging Infectious Diseases, Institut Louis Malardé
Ahmed Haouz: Institut Pasteur, Plateforme de Cristallographie, CiTech
Patrick England: CNRS UMR 3528
Karin Stiasny: Medical University of Vienna
Juthathip Mongkolsapaya: Hammersmith campus, Imperial College London
Franz X. Heinz: Medical University of Vienna
Gavin R. Screaton: Hammersmith campus, Imperial College London
Félix A. Rey: Institut Pasteur, Unité de Virologie Structurale

Nature, 2016, vol. 536, issue 7614, 48-53

Abstract: Abstract Zika virus is a member of the Flavivirus genus that had not been associated with severe disease in humans until the recent outbreaks, when it was linked to microcephaly in newborns in Brazil and to Guillain–Barré syndrome in adults in French Polynesia. Zika virus is related to dengue virus, and here we report that a subset of antibodies targeting a conformational epitope isolated from patients with dengue virus also potently neutralize Zika virus. The crystal structure of two of these antibodies in complex with the envelope protein of Zika virus reveals the details of a conserved epitope, which is also the site of interaction of the envelope protein dimer with the precursor membrane (prM) protein during virus maturation. Comparison of the Zika and dengue virus immunocomplexes provides a lead for rational, epitope-focused design of a universal vaccine capable of eliciting potent cross-neutralizing antibodies to protect simultaneously against both Zika and dengue virus infections.

Date: 2016
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DOI: 10.1038/nature18938

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