Erratum: Structural basis of potent Zika-dengue virus antibody cross-neutralization (Nature (2016) 536 (48-53) DOI: 10.1038/nature18938);Structural basis of potent Zika-dengue virus antibody cross-neutralization

Nature

Volumn 536, Issue 7614, 2016, Pages 48-53

  Barba Spaeth, Giovanna ^a,b   Dejnirattisai, Wanwisa ^c   Rouvinski, Alexander ^a,b   Vaney, Marie Christine ^a,b   Medits, Iris ^d   Sharma, Arvind ^a,b   Simon Lorière, Etienne ^a,e   Sakuntabhai, Anavaj ^a,e   Cao Lormeau, Van Mai ^f   Haouz, Ahmed ^a,e   England, Patrick ^a,e   Stiasny, Karin ^d   Mongkolsapaya, Juthathip ^c,g   Heinz, Franz X ^d   Screaton, Gavin R ^c   Rey, Félix A ^a,b  

^a INSTITUT PASTEUR   (France)

^b Institut Pasteur   (France)

^c IMPERIAL COLLEGE LONDON   (United Kingdom)

^d MEDICAL UNIVERSITY OF VIENNA   (Austria)

^e CNRS   (France)

^f INSTITUT LOUIS MALARDÉ   (French Polynesia)

^g MAHIDOL UNIVERSITY   (Thailand)

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; EPITOPE; IMMUNOGLOBULIN G ANTIBODY; NEUTRALIZING ANTIBODY; VIRUS ANTIBODY; VIRUS ENVELOPE PROTEIN; ANTIGEN ANTIBODY COMPLEX; DENGUE VACCINE; MONOCLONAL ANTIBODY; VIRUS VACCINE;

ANTIBODY; CRYSTAL STRUCTURE; DENGUE FEVER; DESIGN; DISEASE SEVERITY; INFECTIVITY; MATURATION; MEMBRANE; PROTEIN; VACCINE; VIRUS;

ANTIBODY STRUCTURE; ANTIGEN ANTIBODY COMPLEX; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DENGUE VIRUS; HUMAN; NONHUMAN; PHYLOGENETIC TREE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN INTERACTION; SEROTYPE; VIRUS NEUTRALIZATION; ZIKA VIRUS; BRAZIL; CHEMICAL STRUCTURE; CHEMISTRY; CROSS REACTION; DENGUE; IMMUNOLOGY; PHYLOGENY; PREVENTION AND CONTROL; X RAY CRYSTALLOGRAPHY; ZIKA FEVER;

BRAZIL; FRENCH POLYNESIA;

DENGUE VIRUS; FLAVIVIRUS; ZIKA VIRUS;

ANTIBODIES, MONOCLONAL; ANTIBODIES, NEUTRALIZING; ANTIGEN-ANTIBODY COMPLEX; BRAZIL; CROSS REACTIONS; CRYSTALLOGRAPHY, X-RAY; DENGUE; DENGUE VACCINES; DENGUE VIRUS; EPITOPES; HUMANS; MODELS, MOLECULAR; PHYLOGENY; VIRAL ENVELOPE PROTEINS; VIRAL VACCINES; ZIKA VIRUS; ZIKA VIRUS INFECTION;

EID: 84976351583     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature19780     Document Type: Erratum

References (45)

1. Lindenbach, B., Murray, C., Thiel, H. & Rice, C. Flaviviridae: The Viruses and Their Replication 6th edn, Vol. 1 1101-1152 (Lippincott Williams & Wilkins, 2013).
2. Kuhn, R. J. et al. Structure of dengue virus: implications for flavivirus organization, maturation, and fusion. Cell 108, 717-725 (2002).
3. Zhang, X. et al. Cryo-EM structure of the mature dengue virus at 3.5-Å resolution. Nat. Struct. Mol. Biol. 20, 105-110 (2013).
4. Kostyuchenko, V. A. et al. Structure of the thermally stable Zika virus. Nature 533, 425-428 (2016).
5. Sirohi, D. et al. The 3.8 Å resolution cryo-EM structure of Zika virus. Science 352, 467-470 (2016).
6. Mukhopadhyay, S., Kim, B. S., Chipman, P. R., Rossmann, M. G. & Kuhn, R. J. Structure of West Nile virus. Science 302, 248 (2003).
7. Zhang, W., Kaufmann, B., Chipman, P. R., Kuhn, R. J. & Rossmann, M. G. Membrane curvature in flaviviruses. J. Struct. Biol. 183, 86-94 (2013).
8. Calisher, C. H. et al. Antigenic relationships between flaviviruses as determined by cross-neutralization tests with polyclonal antisera. J. Gen. Virol. 70, 37-43 (1989).
9. Stiasny, K., Kiermayr, S., Holzmann, H. & Heinz, F. X. Cryptic properties of a cluster of dominant flavivirus cross-reactive antigenic sites. J. Virol. 80, 9557-9568 (2006).
10. Vogt, M. R. et al. Poorly neutralizing cross-reactive antibodies against the fusion loop of West Nile virus envelope protein protect in vivo via Fcγ receptor and complement-dependent effector mechanisms. J. Virol. 85, 11567-11580 (2011).
11. Balsitis, S. J. et al. Lethal antibody enhancement of dengue disease in mice is prevented by Fc modification. PLoS Pathog. 6, e1000790 (2010).
12. Dejnirattisai, W. et al. Dengue virus sero-cross-reactivity drives antibodydependent enhancement of infection with zika virus. Nat. Immunol. http://dx.doi.org/10.1038/ni.3515 (2016).
13. Dejnirattisai, W. et al. A new class of highly potent, broadly neutralizing antibodies isolated from viremic patients infected with dengue virus. Nat. Immunol. 16, 170-177 (2015).
14. 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, 9422-9427 (2007).
15. Halstead, S. B. In vivo enhancement of dengue virus infection in rhesus monkeys by passively transferred antibody. J. Infect. Dis. 140, 527-533 (1979).
16. Rouvinski, A. et al. Recognition determinants of broadly neutralizing human antibodies against dengue viruses. Nature 520, 109-113 (2015).
17. Dai, L. et al. Structures of the Zika virus envelope protein and its complex with a flavivirus broadly protective antibody. Cell Host Microbe 19, 696-704 (2016).
18. 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, 508-517 (2015).
19. 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, 1559-1567 (2013).
20. Vannice, K. S., Durbin, A. & Hombach, J. Status of vaccine research and development of vaccines for dengue. Vaccine 34, 2934-2938 (2016).
21. Plevka, P. et al. Maturation of flaviviruses starts from one or more icosahedrally independent nucleation centres. EMBO Rep. 12, 602-606 (2011).
22. Cherrier, M. V. et al. Structural basis for the preferential recognition of immature flaviviruses by a fusion-loop antibody. EMBO J. 28, 3269-3276 (2009).
23. 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, 271-283 (2010).
24. 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, 11726-11737 (2014).
25. 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, 13729-13740 (2013).
26. Mukherjee, S. et al. Mechanism and significance of cell type-dependent neutralization of flaviviruses. J. Virol. 88, 7210-7220 (2014).
27. 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, 1358-1365 (2014).
28. Hessell, A. J. et al. Fc receptor but not complement binding is important in antibody protection against HIV. Nature 449, 101-104 (2007).
29. Vratskikh, O. et al. Dissection of antibody specificities induced by yellow fever vaccination. PLoS Pathog. 9, e1003458 (2013).
30. Jarmer, J. et al. Variation of the specificity of the human antibody responses after tick-borne encephalitis virus infection and vaccination. J. Virol. 88, 13845-13857 (2014).
31. DuBois, R. M. et al. Functional and evolutionary insight from the crystal structure of rubella virus protein E1. Nature 493, 552-556 (2013).
32. Backovic, M. et al. Efficient method for production of high yields of Fab fragments in Drosophila S2 cells. Protein Eng. Des. Sel. 23, 169-174 (2010).
33. 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, 59-66 (2012).
34. Kabsch, W. Xds. Acta Crystallogr. D 66, 125-132 (2010).
35. Evans, P. R. & Murshudov, G. N. How good are my data and what is the resolution? Acta Crystallogr. D 69, 1204-1214 (2013).
36. Biasini, M. et al. SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information. Nucleic Acids Res. 42, W252-W258 (2014).
37. McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
38. Winn, M. D. et al. Overview of the CCP4 suite and current developments. Acta Crystallogr. D 67, 235-242 (2011).
39. Bricogne, G. et al. BUSTER version 2.10.2 (Global Phasing Ltd, 2016).
40. Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D 66, 486-501 (2010).
41. Krissinel, E. & Henrick, K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797 (2007).
42. Larkin, M. A. et al. Clustal W and Clustal X version 2.0. Bioinformatics 23, 2947-2948 (2007).
43. Goujon, M. et al. A new bioinformatics analysis tools framework at EMBL-EBI. Nucleic Acids Res. 38, W695-W699 (2010).
44. Gouet, P., Courcelle, E., Stuart, D. I. & Métoz, F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15, 305-308 (1999).
45. Guindon, S. et al. New algorithms and methods to estimate maximumlikelihood phylogenies: assessing the performance of PhyML 3.0. Syst. Biol. 59, 307-321 (2010).