{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T02:40:20Z","timestamp":1791427220220,"version":"4.3.3"},"reference-count":45,"publisher":"Springer Science and Business Media LLC","issue":"7614","license":[{"start":{"date-parts":[[2016,6,23]],"date-time":"2016-06-23T00:00:00Z","timestamp":1466640000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2016,6,23]],"date-time":"2016-06-23T00:00:00Z","timestamp":1466640000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nature"],"published-print":{"date-parts":[[2016,8,4]]},"DOI":"10.1038\/nature18938","type":"journal-article","created":{"date-parts":[[2016,6,23]],"date-time":"2016-06-23T10:37:17Z","timestamp":1466678237000},"page":"48-53","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":500,"title":["Structural basis of potent Zika\u2013dengue virus antibody cross-neutralization"],"prefix":"10.1038","volume":"536","author":[{"given":"Giovanna","family":"Barba-Spaeth","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wanwisa","family":"Dejnirattisai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexander","family":"Rouvinski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marie-Christine","family":"Vaney","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Iris","family":"Medits","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arvind","family":"Sharma","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Etienne","family":"Simon-Lori\u00e8re","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anavaj","family":"Sakuntabhai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Van-Mai","family":"Cao-Lormeau","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ahmed","family":"Haouz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patrick","family":"England","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karin","family":"Stiasny","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Juthathip","family":"Mongkolsapaya","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Franz X.","family":"Heinz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gavin R.","family":"Screaton","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"F\u00e9lix A.","family":"Rey","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2016,6,23]]},"reference":[{"key":"BFnature18938_CR1","first-page":"1101","volume":"Vol. 1","author":"B Lindenbach","year":"2013","unstructured":"Lindenbach, B., Murray, C., Thiel, H. & Rice, C. Flaviviridae: The Viruses and Their Replication 6th edn, Vol. 1 1101\u20131152 (Lippincott Williams & Wilkins, 2013)","journal-title":"Flaviviridae: The Viruses and Their Replication"},{"key":"BFnature18938_CR2","doi-asserted-by":"publisher","first-page":"717","DOI":"10.1016\/S0092-8674(02)00660-8","volume":"108","author":"RJ Kuhn","year":"2002","unstructured":"Kuhn, R. J. et al. Structure of dengue virus: implications for flavivirus organization, maturation, and fusion. Cell 108, 717\u2013725 (2002)","journal-title":"Cell"},{"key":"BFnature18938_CR3","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1038\/nsmb.2463","volume":"20","author":"X Zhang","year":"2013","unstructured":"Zhang, X. et al. Cryo-EM structure of the mature dengue virus at 3.5-\u00c5 resolution. Nat. Struct. Mol. Biol. 20, 105\u2013110 (2013)","journal-title":"Nat. Struct. Mol. Biol."},{"key":"BFnature18938_CR4","doi-asserted-by":"publisher","first-page":"425","DOI":"10.1038\/nature17994","volume":"533","author":"VA Kostyuchenko","year":"2016","unstructured":"Kostyuchenko, V. A. et al. Structure of the thermally stable Zika virus. Nature 533, 425\u2013428 (2016)","journal-title":"Nature"},{"key":"BFnature18938_CR5","doi-asserted-by":"publisher","first-page":"467","DOI":"10.1126\/science.aaf5316","volume":"352","author":"D Sirohi","year":"2016","unstructured":"Sirohi, D. et al. The 3.8 \u00c5 resolution cryo-EM structure of Zika virus. Science 352, 467\u2013470 (2016)","journal-title":"Science"},{"key":"BFnature18938_CR6","doi-asserted-by":"publisher","first-page":"248","DOI":"10.1126\/science.1089316","volume":"302","author":"S Mukhopadhyay","year":"2003","unstructured":"Mukhopadhyay, S., Kim, B. S., Chipman, P. R., Rossmann, M. G. & Kuhn, R. J. Structure of West Nile virus. Science 302, 248 (2003)","journal-title":"Science"},{"key":"BFnature18938_CR7","doi-asserted-by":"publisher","first-page":"86","DOI":"10.1016\/j.jsb.2013.04.005","volume":"183","author":"W Zhang","year":"2013","unstructured":"Zhang, W., Kaufmann, B., Chipman, P. R., Kuhn, R. J. & Rossmann, M. G. Membrane curvature in flaviviruses. J. Struct. Biol. 183, 86\u201394 (2013)","journal-title":"J. Struct. Biol."},{"key":"BFnature18938_CR8","doi-asserted-by":"publisher","first-page":"37","DOI":"10.1099\/0022-1317-70-1-37","volume":"70","author":"CH Calisher","year":"1989","unstructured":"Calisher, C. H. et al. Antigenic relationships between flaviviruses as determined by cross-neutralization tests with polyclonal antisera. J. Gen. Virol. 70, 37\u201343 (1989)","journal-title":"J. Gen. Virol."},{"key":"BFnature18938_CR9","doi-asserted-by":"publisher","first-page":"9557","DOI":"10.1128\/JVI.00080-06","volume":"80","author":"K Stiasny","year":"2006","unstructured":"Stiasny, K., Kiermayr, S., Holzmann, H. & Heinz, F. X. Cryptic properties of a cluster of dominant flavivirus cross-reactive antigenic sites. J. Virol. 80, 9557\u20139568 (2006)","journal-title":"J. Virol."},{"key":"BFnature18938_CR10","doi-asserted-by":"publisher","first-page":"11567","DOI":"10.1128\/JVI.05859-11","volume":"85","author":"MR Vogt","year":"2011","unstructured":"Vogt, M. R. et al. Poorly neutralizing cross-reactive antibodies against the fusion loop of West Nile virus envelope protein protect in vivo via Fc\u03b3 receptor and complement-dependent effector mechanisms. J. Virol. 85, 11567\u201311580 (2011)","journal-title":"J. Virol."},{"key":"BFnature18938_CR11","doi-asserted-by":"publisher","first-page":"e1000790","DOI":"10.1371\/journal.ppat.1000790","volume":"6","author":"SJ Balsitis","year":"2010","unstructured":"Balsitis, S. J. et al. Lethal antibody enhancement of dengue disease in mice is prevented by Fc modification. PLoS Pathog. 6, e1000790 (2010)","journal-title":"PLoS Pathog."},{"key":"BFnature18938_CR12","doi-asserted-by":"publisher","unstructured":"Dejnirattisai, W. et al. Dengue virus sero-cross-reactivity drives antibody-dependent enhancement of infection with zika virus. Nat. Immunol. http:\/\/dx.doi.org\/10.1038\/ni.3515 (2016)","DOI":"10.1038\/ni.3515"},{"key":"BFnature18938_CR13","doi-asserted-by":"publisher","first-page":"170","DOI":"10.1038\/ni.3058","volume":"16","author":"W Dejnirattisai","year":"2015","unstructured":"Dejnirattisai, W. et al. A new class of highly potent, broadly neutralizing antibodies isolated from viremic patients infected with dengue virus. Nat. Immunol. 16, 170\u2013177 (2015)","journal-title":"Nat. Immunol."},{"key":"BFnature18938_CR14","doi-asserted-by":"publisher","first-page":"9422","DOI":"10.1073\/pnas.0703498104","volume":"104","author":"AP Goncalvez","year":"2007","unstructured":"Goncalvez, A. P., Engle, R. E., St Claire, M., Purcell, R. H. & Lai, C. J. Monoclonal antibody-mediated enhancement of dengue virus infection in vitro and in vivo and strategies for prevention. Proc. Natl Acad. Sci. USA 104, 9422\u20139427 (2007)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature18938_CR15","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1093\/infdis\/140.4.527","volume":"140","author":"SB Halstead","year":"1979","unstructured":"Halstead, S. B. In vivo enhancement of dengue virus infection in rhesus monkeys by passively transferred antibody. J. Infect. Dis. 140, 527\u2013533 (1979)","journal-title":"J. Infect. Dis."},{"key":"BFnature18938_CR16","doi-asserted-by":"publisher","first-page":"109","DOI":"10.1038\/nature14130","volume":"520","author":"A Rouvinski","year":"2015","unstructured":"Rouvinski, A. et al. Recognition determinants of broadly neutralizing human antibodies against dengue viruses. Nature 520, 109\u2013113 (2015)","journal-title":"Nature"},{"key":"BFnature18938_CR17","doi-asserted-by":"publisher","first-page":"696","DOI":"10.1016\/j.chom.2016.04.013","volume":"19","author":"L Dai","year":"2016","unstructured":"Dai, L. et al. Structures of the Zika virus envelope protein and its complex with a flavivirus broadly protective antibody. Cell Host Microbe 19, 696\u2013704 (2016)","journal-title":"Cell Host Microbe"},{"key":"BFnature18938_CR18","doi-asserted-by":"publisher","first-page":"508","DOI":"10.1016\/j.virol.2015.03.025","volume":"479-480","author":"RJ Kuhn","year":"2015","unstructured":"Kuhn, R. J., Dowd, K. A., Beth Post, C. & Pierson, T. C. Shake, rattle, and roll: Impact of the dynamics of flavivirus particles on their interactions with the host. Virology 479-480, 508\u2013517 (2015)","journal-title":"Virology"},{"key":"BFnature18938_CR19","doi-asserted-by":"publisher","first-page":"1559","DOI":"10.1016\/S0140-6736(12)61428-7","volume":"380","author":"A Sabchareon","year":"2013","unstructured":"Sabchareon, A. et al. Protective efficacy of the recombinant, live-attenuated, CYD tetravalent dengue vaccine in Thai schoolchildren: a randomised, controlled phase 2b trial. Lancet 380, 1559\u20131567 (2013)","journal-title":"Lancet"},{"key":"BFnature18938_CR20","doi-asserted-by":"publisher","first-page":"2934","DOI":"10.1016\/j.vaccine.2015.12.073","volume":"34","author":"KS Vannice","year":"2016","unstructured":"Vannice, K. S., Durbin, A. & Hombach, J. Status of vaccine research and development of vaccines for dengue. Vaccine 34, 2934\u20132938 (2016)","journal-title":"Vaccine"},{"key":"BFnature18938_CR21","doi-asserted-by":"publisher","first-page":"602","DOI":"10.1038\/embor.2011.75","volume":"12","author":"P Plevka","year":"2011","unstructured":"Plevka, P. et al. Maturation of flaviviruses starts from one or more icosahedrally independent nucleation centres. EMBO Rep. 12, 602\u2013606 (2011)","journal-title":"EMBO Rep."},{"key":"BFnature18938_CR22","doi-asserted-by":"publisher","first-page":"3269","DOI":"10.1038\/emboj.2009.245","volume":"28","author":"MV Cherrier","year":"2009","unstructured":"Cherrier, M. V. et al. Structural basis for the preferential recognition of immature flaviviruses by a fusion-loop antibody. EMBO J. 28, 3269\u20133276 (2009)","journal-title":"EMBO J."},{"key":"BFnature18938_CR23","doi-asserted-by":"publisher","first-page":"271","DOI":"10.1016\/j.chom.2010.08.007","volume":"8","author":"M Beltramello","year":"2010","unstructured":"Beltramello, M. et al. The human immune response to Dengue virus is dominated by highly cross-reactive antibodies endowed with neutralizing and enhancing activity. Cell Host Microbe 8, 271\u2013283 (2010)","journal-title":"Cell Host Microbe"},{"key":"BFnature18938_CR24","doi-asserted-by":"publisher","first-page":"11726","DOI":"10.1128\/JVI.01140-14","volume":"88","author":"KA Dowd","year":"2014","unstructured":"Dowd, K. A., Mukherjee, S., Kuhn, R. J. & Pierson, T. C. Combined effects of the structural heterogeneity and dynamics of flaviviruses on antibody recognition. J. Virol. 88, 11726\u201311737 (2014)","journal-title":"J. Virol."},{"key":"BFnature18938_CR25","doi-asserted-by":"publisher","first-page":"13729","DOI":"10.1128\/JVI.02340-13","volume":"87","author":"PD Lee","year":"2013","unstructured":"Lee, P. D. et al. The Fc region of an antibody impacts the neutralization of West Nile viruses in different maturation states. J. Virol. 87, 13729\u201313740 (2013)","journal-title":"J. Virol."},{"key":"BFnature18938_CR26","doi-asserted-by":"publisher","first-page":"7210","DOI":"10.1128\/JVI.03690-13","volume":"88","author":"S Mukherjee","year":"2014","unstructured":"Mukherjee, S. et al. Mechanism and significance of cell type-dependent neutralization of flaviviruses. J. Virol. 88, 7210\u20137220 (2014)","journal-title":"J. Virol."},{"key":"BFnature18938_CR27","doi-asserted-by":"publisher","first-page":"1358","DOI":"10.1016\/S0140-6736(14)61060-6","volume":"384","author":"MR Capeding","year":"2014","unstructured":"Capeding, M. R. et al. Clinical efficacy and safety of a novel tetravalent dengue vaccine in healthy children in Asia: a phase 3, randomised, observer-masked, placebo-controlled trial. Lancet 384, 1358\u20131365 (2014)","journal-title":"Lancet"},{"key":"BFnature18938_CR28","doi-asserted-by":"publisher","first-page":"101","DOI":"10.1038\/nature06106","volume":"449","author":"AJ Hessell","year":"2007","unstructured":"Hessell, A. J. et al. Fc receptor but not complement binding is important in antibody protection against HIV. Nature 449, 101\u2013104 (2007)","journal-title":"Nature"},{"key":"BFnature18938_CR29","doi-asserted-by":"publisher","first-page":"e1003458","DOI":"10.1371\/journal.ppat.1003458","volume":"9","author":"O Vratskikh","year":"2013","unstructured":"Vratskikh, O. et al. Dissection of antibody specificities induced by yellow fever vaccination. PLoS Pathog. 9, e1003458 (2013)","journal-title":"PLoS Pathog."},{"key":"BFnature18938_CR30","doi-asserted-by":"publisher","first-page":"13845","DOI":"10.1128\/JVI.02086-14","volume":"88","author":"J Jarmer","year":"2014","unstructured":"Jarmer, J. et al. Variation of the specificity of the human antibody responses after tick-borne encephalitis virus infection and vaccination. J. Virol. 88, 13845\u201313857 (2014)","journal-title":"J. Virol."},{"key":"BFnature18938_CR31","doi-asserted-by":"publisher","first-page":"552","DOI":"10.1038\/nature11741","volume":"493","author":"RM DuBois","year":"2013","unstructured":"DuBois, R. M. et al. Functional and evolutionary insight from the crystal structure of rubella virus protein E1. Nature 493, 552\u2013556 (2013)","journal-title":"Nature"},{"key":"BFnature18938_CR32","doi-asserted-by":"publisher","first-page":"169","DOI":"10.1093\/protein\/gzp088","volume":"23","author":"M Backovic","year":"2010","unstructured":"Backovic, M. et al. Efficient method for production of high yields of Fab fragments in Drosophila S2 cells. Protein Eng. Des. Sel. 23, 169\u2013174 (2010)","journal-title":"Protein Eng. Des. Sel."},{"key":"BFnature18938_CR33","doi-asserted-by":"publisher","first-page":"59","DOI":"10.1093\/protein\/gzr058","volume":"25","author":"AA Gilmartin","year":"2012","unstructured":"Gilmartin, A. A. et al. High-level secretion of recombinant monomeric murine and human single-chain Fv antibodies from Drosophila S2 cells. Protein Eng. Des. Sel. 25, 59\u201366 (2012)","journal-title":"Protein Eng. Des. Sel."},{"key":"BFnature18938_CR34","doi-asserted-by":"publisher","first-page":"125","DOI":"10.1107\/S0907444909047337","volume":"66","author":"W Kabsch","year":"2010","unstructured":"Kabsch, W. Xds. Acta Crystallogr. D 66, 125\u2013132 (2010)","journal-title":"Acta Crystallogr. D"},{"key":"BFnature18938_CR35","doi-asserted-by":"publisher","first-page":"1204","DOI":"10.1107\/S0907444913000061","volume":"69","author":"PR Evans","year":"2013","unstructured":"Evans, P. R. & Murshudov, G. N. How good are my data and what is the resolution? Acta Crystallogr. D 69, 1204\u20131214 (2013)","journal-title":"Acta Crystallogr. D"},{"key":"BFnature18938_CR36","doi-asserted-by":"publisher","first-page":"W252","DOI":"10.1093\/nar\/gku340","volume":"42","author":"M Biasini","year":"2014","unstructured":"Biasini, M. et al. SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information. Nucleic Acids Res. 42, W252\u2013W258 (2014)","journal-title":"Nucleic Acids Res."},{"key":"BFnature18938_CR37","doi-asserted-by":"publisher","first-page":"658","DOI":"10.1107\/S0021889807021206","volume":"40","author":"AJ McCoy","year":"2007","unstructured":"McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658\u2013674 (2007)","journal-title":"J. Appl. Crystallogr."},{"key":"BFnature18938_CR38","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1107\/S0907444910045749","volume":"67","author":"MD Winn","year":"2011","unstructured":"Winn, M. D. et al. Overview of the CCP4 suite and current developments. Acta Crystallogr. D 67, 235\u2013242 (2011)","journal-title":"Acta Crystallogr. D"},{"key":"BFnature18938_CR39","unstructured":"Bricogne, G. et al. BUSTER version 2.10.2 (Global Phasing Ltd, 2016)"},{"key":"BFnature18938_CR40","doi-asserted-by":"publisher","first-page":"486","DOI":"10.1107\/S0907444910007493","volume":"66","author":"P Emsley","year":"2010","unstructured":"Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D 66, 486\u2013501 (2010)","journal-title":"Acta Crystallogr. D"},{"key":"BFnature18938_CR41","doi-asserted-by":"publisher","first-page":"774","DOI":"10.1016\/j.jmb.2007.05.022","volume":"372","author":"E Krissinel","year":"2007","unstructured":"Krissinel, E. & Henrick, K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774\u2013797 (2007)","journal-title":"J. Mol. Biol."},{"key":"BFnature18938_CR42","doi-asserted-by":"publisher","first-page":"2947","DOI":"10.1093\/bioinformatics\/btm404","volume":"23","author":"MA Larkin","year":"2007","unstructured":"Larkin, M. A. et al. Clustal W and Clustal X version 2.0. Bioinformatics 23, 2947\u20132948 (2007)","journal-title":"Bioinformatics"},{"key":"BFnature18938_CR43","doi-asserted-by":"publisher","first-page":"W695","DOI":"10.1093\/nar\/gkq313","volume":"38","author":"M Goujon","year":"2010","unstructured":"Goujon, M. et al. A new bioinformatics analysis tools framework at EMBL-EBI. Nucleic Acids Res. 38, W695\u2013W699 (2010)","journal-title":"Nucleic Acids Res."},{"key":"BFnature18938_CR44","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1093\/bioinformatics\/15.4.305","volume":"15","author":"P Gouet","year":"1999","unstructured":"Gouet, P., Courcelle, E., Stuart, D. I. & M\u00e9toz, F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15, 305\u2013308 (1999)","journal-title":"Bioinformatics"},{"key":"BFnature18938_CR45","doi-asserted-by":"publisher","first-page":"307","DOI":"10.1093\/sysbio\/syq010","volume":"59","author":"S Guindon","year":"2010","unstructured":"Guindon, S. et al. New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0. Syst. Biol. 59, 307\u2013321 (2010)","journal-title":"Syst. Biol."}],"updated-by":[{"DOI":"10.1038\/nature19780","type":"erratum","label":"Erratum","source":"publisher","updated":{"date-parts":[[2016,9,14]],"date-time":"2016-09-14T00:00:00Z","timestamp":1473811200000}}],"container-title":["Nature"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/nature18938.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/nature18938","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/nature18938.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,9,3]],"date-time":"2021-09-03T17:11:47Z","timestamp":1630689107000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/nature18938"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,6,23]]},"references-count":45,"journal-issue":{"issue":"7614","published-print":{"date-parts":[[2016,8,4]]}},"alternative-id":["BFnature18938"],"URL":"https:\/\/doi.org\/10.1038\/nature18938","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.726446717.793522061","asserted-by":"object"}]},"ISSN":["0028-0836","1476-4687"],"issn-type":[{"value":"0028-0836","type":"print"},{"value":"1476-4687","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016,6,23]]},"assertion":[{"value":"19 May 2016","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"17 June 2016","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"23 June 2016","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The EDE antibodies and epitope are the subject of a patent application by Imperial College and Institut Pasteur on which G.S., J.M., F.R., A.R., M.C.V. and G.B.S. are named as inventors.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}]}}