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; Van Mai Cao-Lormeau; Ahmed Haouz; Patrick England; Karin Stiasny; Juthathip Mongkolsapaya; Franz X. Heinz; Gavin R. Screaton; Félix A. Rey

doi:https://doi.org/10.1038/nature18938

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, Van Mai Cao-Lormeau, Ahmed Haouz, Patrick England, Karin Stiasny, Juthathip Mongkolsapaya, Franz X. Heinz, Gavin R. Screaton, Félix A. Rey

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	48-53
Number of pages	6
Journal	Nature
Volume	536
Issue number	7614
DOIs	https://doi.org/10.1038/nature18938
State	Published - 3 Jun 2016
Externally published	Yes

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Barba-Spaeth, G., Dejnirattisai, W., Rouvinski, A., Vaney, M. C., Medits, I., Sharma, A., Simon-Lorière, E., Sakuntabhai, A., Cao-Lormeau, V. M., Haouz, A., England, P., Stiasny, K., Mongkolsapaya, J., Heinz, F. X., Screaton, G. R., & Rey, F. A. (2016). Structural basis of potent Zika-dengue virus antibody cross-neutralization. Nature, 536(7614), 48-53. https://doi.org/10.1038/nature18938

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title = "Structural basis of potent Zika-dengue virus antibody cross-neutralization",

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-Barr{\'e} 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.",

author = "Giovanna Barba-Spaeth and Wanwisa Dejnirattisai and Alexander Rouvinski and Vaney, {Marie Christine} and Iris Medits and Arvind Sharma and Etienne Simon-Lori{\`e}re and Anavaj Sakuntabhai and Cao-Lormeau, {Van Mai} and Ahmed Haouz and Patrick England and Karin Stiasny and Juthathip Mongkolsapaya and Heinz, {Franz X.} and Screaton, {Gavin R.} and Rey, {F{\'e}lix A.}",

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doi = "https://doi.org/10.1038/nature18938",

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Barba-Spaeth, G, Dejnirattisai, W, Rouvinski, A, Vaney, MC, Medits, I, Sharma, A, Simon-Lorière, E, Sakuntabhai, A, Cao-Lormeau, VM, Haouz, A, England, P, Stiasny, K, Mongkolsapaya, J, Heinz, FX, Screaton, GR & Rey, FA 2016, 'Structural basis of potent Zika-dengue virus antibody cross-neutralization', Nature, vol. 536, no. 7614, pp. 48-53. https://doi.org/10.1038/nature18938

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AU - Barba-Spaeth, Giovanna

AU - Dejnirattisai, Wanwisa

AU - Rouvinski, Alexander

AU - Vaney, Marie Christine

AU - Medits, Iris

AU - Sharma, Arvind

AU - Simon-Lorière, Etienne

AU - Sakuntabhai, Anavaj

AU - Cao-Lormeau, Van Mai

AU - Haouz, Ahmed

AU - England, Patrick

AU - Stiasny, Karin

AU - Mongkolsapaya, Juthathip

AU - Heinz, Franz X.

AU - Screaton, Gavin R.

AU - Rey, Félix A.

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AB - 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.

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DO - https://doi.org/10.1038/nature18938

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SP - 48

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JO - Nature

JF - Nature

IS - 7614

ER -

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

Abstract

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