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

Authors :
Franz X. Heinz
Juthathip Mongkolsapaya
Ahmed Haouz
Arvind Sharma
Patrick England
Van-Mai Cao-Lormeau
Wanwisa Dejnirattisai
Félix A. Rey
Anavaj Sakuntabhai
Iris Medits
Etienne Simon-Loriere
Gavin R. Screaton
Karin Stiasny
Alexander Rouvinski
Giovanna Barba-Spaeth
Marie Christine Vaney
Virologie Structurale - Structural Virology
Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)
Division of Immunology and Inflammation, Department of Medicine
Imperial College London-Hammersmith Hospital Campus
Medizinische Universität Wien = Medical University of Vienna
Génétique fonctionnelle des Maladies infectieuses - Functional Genetics of Infectious Diseases
Emerging Infectious Diseases
Institut Louis Malardé [Papeete] (ILM)
Institut de Recherche pour le Développement (IRD)-Institut de Recherche pour le Développement (IRD)
Cristallographie (Plateforme) - Crystallography (Platform)
Biophysique des Macromolécules et de leurs Interactions
Siriraj Hospital, Mahidol University
Mahidol University [Bangkok]
We acknowledge support from the European Commission FP7 Programme for the DENFREE project under Grant Agreement number 282 378FP7 (F.A.R., J.M., G.R.S. and A.Sa.)
the 'Integrative Biology of Emerging Infectious Diseases' Labex (Laboratoire d’Excellence) grant number ANR-10-LABX-62-IBEID (French Government’s 'Investissements d’Avenir' program ) (F.A.R.)
the transnational ANR/FWF grant FlaviStem/I1378 (F.A.R. and K.S.), the Medical Research Council, UK (J.M.)
the National Institute for Health Research Biomedical Research Centre, Funding Scheme, UK (G.R.S.)
and the NEUTRAVIR grant from Région ile-de-France (DIM-Maladies Infectieuses) (P.E., A.H. and F.A.R.
ANR-13-ISV8-0002,flavistem,La protéine E des flavivirus : interactions et fusion membranaire(2013)
ANR-10-LABX-0062,IBEID,Integrative Biology of Emerging Infectious Diseases(2010)
European Project: 282378,EC:FP7:HEALTH,FP7-HEALTH-2011-single-stage,DENFREE(2012)
Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS)
Medical Research Council (MRC)
Wellcome Trust
Commission of the European Communities
Source :
Nature, Nature, 2016, 536 (7614), pp.48-53. ⟨10.1038/nature18938⟩, Nature, Nature Publishing Group, 2016, 536 (7614), pp.48-53. ⟨10.1038/nature18938⟩, Europe PubMed Central
Publication Year :
2016

Abstract

International audience; 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.

Details

ISSN :
14764687, 00280836, and 14764679
Volume :
536
Issue :
7614
Database :
OpenAIRE
Journal :
Nature
Accession number :
edsair.doi.dedup.....3b70a6bbd2b4be2461c471131b7f7ffe
Full Text :
https://doi.org/10.1038/nature18938⟩