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Antibodies from dengue patients with prior exposure to Japanese encephalitis virus are broadly neutralizing against Zika virus
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Abstract
Exposure to multiple mosquito-borne flaviviruses within a lifetime is not uncommon; however, how sequential exposures to different flaviviruses shape the cross-reactive humoral response against an antigen from a different serocomplex has yet to be explored. Here, we report that dengue-infected individuals initially primed with the Japanese encephalitis virus (JEV) showed broad, highly neutralizing potencies against Zika virus (ZIKV). We also identified a rare class of ZIKV-cross-reactive human monoclonal antibodies with increased somatic hypermutation and broad neutralization against multiple flaviviruses. One huMAb, K8b, binds quaternary epitopes with heavy and light chains separately interacting with overlapping envelope protein dimer units spanning domains I, II, and III through cryo-electron microscopy and structure-based mutagenesis. JEV virus-like particle immunization in mice further confirmed that such cross-reactive antibodies, mainly IgG3 isotype, can be induced and proliferate through heterologous dengue virus (DENV) serotype 2 virus-like particle stimulation. Our findings highlight the role of prior immunity in JEV and DENV in shaping the breadth of humoral response and provide insights for future vaccination strategies in flavivirus-endemic countries.
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Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Research works printed but not linked: 111
- Pierson, T. C. & Diamond, M. S. The continued threat of emerging flaviviruses. Nat. Microbiol. 5, 796–812 (2020). · DOI
- Kuno, G., Chang, G.-J. J., Tsuchiya, R., Karabatsos, N. & Cropp, C. B. Phylogeny of the genus flavivirus. J. Virol. 72, 73–83 (1998). · DOI
- Heinz, F. X. & Stiasny, K. Flaviviruses and flavivirus vaccines. Vaccine 30, 4301–4306 (2012). · DOI
- Mackenzie, J. S., Gubler, D. J. & Petersen, L. R. Emerging flaviviruses: the spread and resurgence of Japanese encephalitis, West Nile and dengue viruses. Nat. Med. 10, S98–S109 (2004). · DOI
- deAlwis, R. et al. Identification of human neutralizing antibodies that bind to complex epitopes on dengue virions. Proc. Natl Acad. Sci. USA. 109, 7439–7444 (2012). · DOI
- Collins, M. H. et al. Lack of durable cross-neutralizing antibodies against Zika virus from dengue virus infection. Emerg. Infect. Dis. 23, 773–781 (2017). · DOI
- Priyamvada, L. et al. Human antibody responses after dengue virus infection are highly cross-reactive to Zika virus. Proc. Natl Acad. Sci. USA. 113, 7852–7857 (2016). · DOI
- Dejnirattisai, W. et al. Dengue virus sero-cross-reactivity drives antibody-dependent enhancement of infection with Zika virus. Nat. Immunol. 17, 1102–1108 (2016). · DOI
- Robbiani, D. F. et al. Recurrent potent human neutralizing antibodies to Zika virus in Brazil and Mexico. Cell 169, 597–609.e11 (2017). · DOI
- Xu, M. et al. Plasmablasts generated during repeated dengue infection are virus glycoprotein–specific and bind to multiple virus serotypes. J. Immunol. 189, 5877–5885 (2012). · DOI
- Perng, G. C. et al. Seroprevalence of Zika and dengue virus antibodies among migrant workers, Taiwan, 2017. Emerg. Infect. Dis. 25, 2017–2019 (2019). · DOI
- Chien, Y. W. et al. Low seroprevalence of Zika virus infection among adults in Southern Taiwan. BMC Infect. Dis. 19, 884 (2019). · DOI
- Huang, A. S. E., Shu, P. Y. & Yang, C. H. A new reportable disease is born: Taiwan Centers for Disease Control’s response to emerging Zika virus infection. J. Formos. Med. Assoc. 115, 223–225 (2016). · DOI
- Hsu, L. C. et al. The incidence of Japanese encephalitis in Taiwan—a population-based study. PLoS Negl. Trop. Dis. 8, e3030 (2014). · DOI
- Wu, Y. C. et al. The epidemiology of Japanese encephalitis on Taiwan during 1966-1997. Am. J. Trop. Med. Hyg. 61, 78–84 (1999). · DOI
- Chang, C. J., Chen, C. S., Tien, C. J. & Lu, M. R. Epidemiological, clinical and climatic characteristics of dengue fever in Kaohsiung City, Taiwan with implication for prevention and control. PLoS One 13, 1–15 (2018).
- King, C. et al. Major epidemics of dengue in Taiwan in 1981-2000: related to intensive virus activities in Asia. Dengue Bull. 24, 1–10 (2000).
- Andrade, P. et al. Primary and secondary dengue virus infections elicit similar memory b-cell responses, but breadth to other serotypes and cross-reactivity to zika virus is higher in secondary dengue. J. Infect. Dis. 222, 590–600 (2020). · DOI
- 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). · DOI
- Montoya, M. et al. Longitudinal analysis of antibody cross-neutralization following Zika virus and dengue virus infection in Asia and the Americas. J. Infect. Dis. 218, 536–545 (2018). · DOI
- Huang, J. et al. Isolation of human monoclonal antibodies from peripheral blood B cells. Nat. Protoc. 8, 1907–1915 (2013). · DOI
- Durham, N. D. et al. Broadly neutralizing human antibodies against dengue virus identified by single B cell transcriptomics. Elife 8, 1–29 (2019). · DOI
- Wrammert, J. et al. Rapid cloning of high-affinity human monoclonal antibodies against influenza virus. Nature 453, 667–671 (2008). · DOI
- Horns, F., Dekker, C. L. & Quake, S. R. Memory B cell activation, broad anti-influenza antibodies, and bystander activation revealed by single-cell transcriptomics. Cell Rep. 30, 905–913.e6 (2020). · DOI
- Methot, S. P. & DiNoia, J. M. Molecular mechanisms of somatic hypermutation and class switch recombination. Adv. Immunol. 133, 37–87 (2017). · DOI
- Shen, W. F. et al. Epitope resurfacing on dengue virus-like particle vaccine preparation to induce broad neutralizing antibody. Elife 7, 1–24 (2018). · DOI
- Saron, W. A. A. et al. Flavivirus serocomplex cross-reactive immunity is protective by activating heterologous memory CD4 T cells. Sci. Adv. 4, 1–15 (2018). · DOI
- Lima, N. S. et al. Pre-existing immunity to Japanese encephalitis virus alters CD4 T cell responses to Zika virus inactivated vaccine. Front. Immunol. 12, 1–14 (2021). · DOI
- Kuadkitkan, A., Wikan, N., Sornjai, W. & Smith, D. R. Zika virus and microcephaly in Southeast Asia: a cause for concern?. J. Infect. Public Health 13, 11–15 (2020). · DOI
- Duong, V., Dussart, P. & Buchy, P. Zika virus in Asia. Int. J. Infect. Dis. 54, 121–128 (2017). · DOI
- Wang, W. H. et al. An epidemiological survey of the current status of Zika and the immune interaction between dengue and Zika infection in Southern Taiwan. Int. J. Infect. Dis. 93, 151–159 (2020). · DOI
- Gordon, A. et al. Prior dengue virus infection and risk of Zika: a pediatric cohort in Nicaragua. PLoS Med. 16, 1–16 (2019). · DOI
- Katzelnick, L. C. et al. Zika virus infection enhances future risk of severe dengue disease. Science 369, 1123–1128 (2020). · DOI
- Rodriguez-Barraquer, I. et al. Impact of preexisting dengue immunity on Zika virus emergence in a dengue endemic region. Science 363, 607–610 (2019). · DOI
- Katzelnick, L. C. et al. Dengue and Zika virus infections in children elicit cross-reactive protective and enhancing antibodies that persist long term. Sci. Transl. Med. 13, eabg9478 (2021). · DOI
- Bardina, S. V. et al. Enhancement of Zika virus pathogenesis by preexisting antiflavivirus immunity. Science 356, 175–180 (2017). · DOI
- McCracken, M. K. et al. Impact of prior flavivirus immunity on Zika virus infection in rhesus macaques. PLoS Pathog. 13, 1–22 (2017). · DOI
- Hou, B., Chen, H., Gao, N. & An, J. Cross-reactive immunity among five medically important mosquito-borne flaviviruses related to human diseases. Viruses 14, 1–13 (2022). · DOI
- Castanha, P. M. S. et al. Force of infection of dengue serotypes in a population-based study in the northeast of Brazil. Epidemiol. Infect. 141, 1080–1088 (2013). · DOI
- He, X. et al. The effects of Japanese encephalitis virus antibodies on Zika virus infection. Med. Microbiol. Immunol. 209, 177–188 (2020). · DOI
- Rodriguez-Barraquer, I. et al. From re-emergence to hyperendemicity: the natural history of the dengue epidemic in Brazil. PLoS Negl. Trop. Dis. 5, 1–7 (2011). · DOI
- Smith, S. A. et al. Persistence of circulating memory B cell clones with potential for dengue virus disease enhancement for decades following infection. J. Virol. 86, 2665–2675 (2012). · DOI
- Sierra, B. et al. Secondary heterologous dengue infection risk: disequilibrium between immune regulation and inflammation? Cell. Immunol. 262, 134–140 (2010). · DOI
- Halstead, S. B. Neutralization and antibody-dependent enhancement of dengue viruses. Adv. Virus Res. 60, 421–467 (2003). · DOI
- Zhang, W. et al. The pre-existing cellular immunity to Japanese encephalitis virus heterotypically protects mice from Zika virus infection. Sci. Bull. 65, 402–409 (2020). · DOI
- Konishi, E., Yamaoka, M., Khin-Sane-Win, Kurane, I. & Mason, P. W. Induction of protective immunity against Japanese encephalitis in mice by immunization with a plasmid encoding Japanese encephalitis virus premembrane and envelope genes. J. Virol. 72, 4925–4930 (1998). · DOI
- Sevvana, M. & Kuhn, R. J. Mapping the diverse structural landscape of the flavivirus antibody repertoire. Curr. Opin. Virol. 45, 51–64 (2020). · DOI
- Lorenz, C. & Chiaravalloti-Neto, F. Why are there no human West Nile virus outbreaks in South America? Lancet Reg. Health Am. 12, 100276 (2022).
- Victora, G. D. & Nussenzweig, M. C. Germinal centers. Annu. Rev. Immunol. 30, 429–457 (2012). · DOI · Paper page
- Feroldi, E. et al. Memory immune response and safety of a booster dose of Japanese encephalitis chimeric virus vaccine (JE-CV) in JE-CV-primed children. Hum. Vaccin. Immunother. 9, 889–897 (2013). · DOI
- Sohn, Y. M., Tandan, J. B., Yoksan, S., Ji, M. & Ohrr, H. A 5-year follow-up of antibody response in children vaccinated with single dose of live attenuated SA14-14-2 Japanese encephalitis vaccine: Immunogenicity and anamnestic responses. Vaccine 26, 1638–1643 (2008). · DOI
- Bosco-Lauth, A., Mason, G. & Bowen, R. Pathogenesis of Japanese encephalitis virus infection in a golden hamster model and evaluation of flavivirus cross-protective immunity. Am. J. Trop. Med. Hyg. 84, 727–732 (2011). · DOI
- Chen, D. et al. Japanese encephalitis virus-primed CD8+ T cells prevent antibody-dependent enhancement of Zika virus pathogenesis. J. Exp. Med. 217, e20192152 (2020). · DOI
- Larena, M., Prow, N. A., Hall, R. A., Petrovsky, N. & Lobigs, M. JE-ADVAX vaccine protection against Japanese encephalitis virus mediated by memory B cells in the absence of CD8 + T cells and pre-exposure neutralizing antibody. J. Virol. 87, 4395–4402 (2013). · DOI
- Wong, R. et al. Affinity-restricted memory B cells dominate recall responses to heterologous flaviviruses. Immunity 53, 1078–1094.e7 (2020). · DOI
- Shaw, R. H. et al. Effect of priming interval on reactogenicity, peak immunological response, and waning after homologous and heterologous COVID-19 vaccine schedules: exploratory analyses of Com-COV, a randomised control trial. Lancet. Respir. Med. 10, 1049–1060 (2022).
- Elliott, T. et al. Enhanced immune responses following heterologous vaccination with self-amplifying RNA and mRNA COVID-19 vaccines. PLoS Pathog. 18, 1–20 (2022). · DOI
- Moyo-Gwete, T. et al. Enhanced neutralization potency of an identical HIV neutralizing antibody expressed as different isotypes is achieved through genetically distinct mechanisms. Sci. Rep. 12, 1–9 (2022). · DOI
- Vidarsson, G., Dekkers, G. & Rispens, T. IgG subclasses and allotypes: from structure to effector functions. Front. Immunol. 5, 1–17 (2014). · DOI · Paper page
- Richardson, S. I. et al. IgG3 enhances neutralization potency and Fc effector function of an HIV V2-specific broadly neutralizing antibody. PLoS Pathog. 15, 1–25 (2019). · DOI
- Onodera, T. et al. A SARS-CoV-2 antibody broadly neutralizes SARS-related coronaviruses and variants by coordinated recognition of a virus-vulnerable site. Immunity 54, 2385–2398.e10 (2021). · DOI
- 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). · DOI
- Rogers, T. F. et al. Zika virus activates de novo and cross-reactive memory B cell responses in dengue-experienced donors. Sci. Immunol. 2, eaan6809 (2017). · DOI
- Dussupt, V. et al. Potent Zika and dengue cross-neutralizing antibodies induced by Zika vaccination in a dengue-experienced donor. Nat. Med. 26, 228–235 (2020). · DOI
- Xu, M. et al. A potent neutralizing antibody with therapeutic potential against all four serotypes of dengue virus. npj Vaccines 2, 2 (2017). · DOI
- Lubow, J. et al. Single B cell transcriptomics identifies multiple isotypes of broadly neutralizing antibodies against flaviviruses. PLoS Pathog. 19, e1011722 (2023). · DOI
- Smith, S. A. et al. The potent and broadly neutralizing human dengue virus-specific monoclonal antibody 1C19 reveals a unique cross-reactive epitope on the bc loop of domain II of the envelope protein. MBio 4, 1–12 (2013). · DOI
- Zhao, H. et al. Mechanism of differential Zika and dengue virus neutralization by a public antibody lineage targeting the DIII lateral ridge. J. Exp. Med. 217, 1–15 (2020). · DOI
- Niu, X. et al. Convalescent patient-derived monoclonal antibodies targeting different epitopes of E protein confer protection against Zika virus in a neonatal mouse model. Emerg. Microbes Infect. 8, 749–759 (2019). · DOI
- Qu, P. et al. A new class of broadly neutralizing antibodies that target the glycan loop of Zika virus envelope protein. Cell Discov. 6, 5 (2020). · DOI
- Fibriansah, G. et al. A potent anti-dengue human antibody preferentially recognizes the conformation of E protein monomers assembled on the virus surface. EMBO Mol. Med. 6, 358–371 (2014). · DOI
- Barba-Spaeth, G. et al. Structural basis of potent Zika-dengue virus antibody cross-neutralization. Nature 536, 48–53 (2016). · DOI
- Phad, G. E. et al. Clonal structure, stability and dynamics of human memory B cells and circulating plasmablasts. Nat. Immunol. 23, 1–10 (2022). · DOI
- Appanna, R. et al. Plasmablasts during acute dengue infection represent a small subset of a broader virus-specific memory B cell pool. EBioMedicine 12, 178–188 (2016). · DOI
- D’Angelo, S. et al. Many routes to an antibody heavy-chain CDR3: necessary, yet insufficient, for specific binding. Front. Immunol. 9, 1–13 (2018). · DOI
- Wang, Q. et al. Molecular determinants of human neutralizing antibodies isolated from a patient infected with Zika virus. Sci. Transl. Med. 8, 369ra179 (2016). · DOI
- Long, F. et al. Structural basis of a potent human monoclonal antibody against Zika virus targeting a quaternary epitope. Proc. Natl Acad. Sci. USA. 116, 1591–1596 (2019). · DOI
- Edeling, M. A. et al. Potent dengue virus neutralization by a therapeutic antibody with low monovalent affinity requires bivalent engagement. PLoS Pathog. 10, e1004072 (2014). · DOI
- Sharma, A. et al. The epitope arrangement on flavivirus particles contributes to Mab C10’s extraordinary neutralization breadth across Zika and dengue viruses. Cell 184, 6052–6066.e18 (2021). · DOI
- Guzman, M. G. et al. Neutralizing antibodies after infection with dengue 1 virus. Emerg. Infect. Dis. 13, 282–286 (2007). · DOI
- Turtle, L. et al. Low population Japanese encephalitis virus (JEV) seroprevalence in Udayapur district, Nepal, three years after a JE vaccination programme: a case for further catch up campaigns? PLoS Negl. Trop. Dis. 13, 1–19 (2019). · DOI
- Galula, J. U., Shen, W.-F., Chuang, S.-T., Chang, G.-J. J. & Chao, D.-Y. Virus-like particle secretion and genotype-dependent immunogenicity of dengue virus serotype 2 DNA vaccine. J. Virol. 88, 10813–10830 (2014). · DOI
- Galula, J. U., Salem, G. M., Destura, R. V., Remenyi, R., & Chao, D. Y. Comparable accuracies of nonstructural protein 1-and envelope protein-based enzyme-linked immunosorbent assays in detecting anti-dengue immunoglobulin g antibodies. Diagnostics 11, 1–17 (2021). · DOI
- VonBoehmer, L. et al. Sequencing and cloning of antigen-specific antibodies from mouse memory B cells. Nat. Protoc. 11, 1908–1923 (2016). · DOI
- Giudicelli, V., Chaume, D. & Lefranc, M. P. IMGT/V-QUEST, an integrated software program for immunoglobulin and T cell receptor V-J and V-D-J rearrangement analysis. Nucleic Acids Res. 32, 435–440 (2004). · DOI
- Li, S. et al. IMGT/HighV QUEST paradigm for T cell receptor IMGT clonotype diversity and next generation repertoire immunoprofiling. Nat. Commun. 4, 2333 (2013). · DOI
- Lefranc, M. P. et al. IMGT R, the international ImMunoGeneTics information system R 25 years on. Nucleic Acids Res. 43, D413–D422 (2015). · DOI
- Pommié, C., Levadoux, S., Sabatier, R., Lefranc, G. & Lefranc, M. P. IMGT standardized criteria for statistical analysis of immunoglobulin V-Region amino acid properties. J. Mol. Recognit. 17, 17–32 (2004). · DOI
- Chang, G. J. J. et al. Enhancing biosynthesis and secretion of premembrane and envelope proteins by the chimeric plasmid of dengue virus type 2 and Japanese encephalitis virus. Virology 306, 170–180 (2003). · DOI
- Chang, G. J. J., Davis, B. S., Stringfield, C. & Lutz, C. Prospective immunization of the endangered California condors (Gymnogyps californianus) protects this species from lethal West Nile virus infection. Vaccine 25, 2325–2330 (2007). · DOI
- Ludtke, S. J., Baldwin, P. R. & Chiu, W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128, 82–97 (1999). · DOI
- Tang, G. et al. EMAN2: an extensible image processing suite for electron microscopy. J. Struct. Biol. 157, 38–46 (2007). · DOI
- Pettersen, E. F. et al. UCSF ChimeraX: structure visualization for researchers, educators, and developers. Protein Sci. 30, 70–82 (2021). · DOI
- Honegger, A. & Plückthun, A. Yet another numbering scheme for immunoglobulin variable domains: an automatic modeling and analysis tool. J. Mol. Biol. 309, 657–670 (2001). · DOI
- Dunbar, J. & Deane, C. M. ANARCI: antigen receptor numbering and receptor classification. Bioinformatics 32, 298–300 (2016). · DOI
- Zhang, S. et al. ProDy 2.0: increased scale and scope after 10 years of protein dynamics modelling with Python. Bioinformatics 37, 3657–3659 (2021). · DOI
- Eswar, N. et al. Comparative protein structure modeling using MODELLER. Curr. Protoc. Protein Sci. 50, Chapter 2:Unit 2.9 (2007). · DOI
- Yan, R. et al. Structural basis for bivalent binding and inhibition of SARS-CoV-2 infection by human potent neutralizing antibodies. Cell Res. 31, 517–525 (2021). · DOI
- Harris, L. J., Larson, S. B., Hasel, K. W. & McPherson, A. Refined structure of an intact IgG2a monoclonal antibody. Biochemistry 36, 1581–1597 (1997). · DOI
- Ritchie, D. W., Venkatraman, V. & Ultra-fast, F. F. T. protein docking on graphics processors. Bioinformatics 26, 2398–2405 (2010). · DOI
- Topf, M. et al. Protein structure fitting and refinement guided by cryo-EM density. Structure 16, 295–307 (2008). · DOI
- Krissinel, E. & Henrick, K. Inference of macromolecular assemblies from crystalline. State J. Mol. Biol. 372, 774–797 (2007). · DOI
- Laskowski, R. A. et al. PDBsum: a web-based database of summaries and analyses of all PDB structures. Trends Biochem. Sci. 22, 488–490 (1997). · DOI
- 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). · DOI
- Deng, Y. Q. et al. A broadly flavivirus cross-neutralizing monoclonal antibody that recognizes a novel epitope within the fusion loop of e protein. PLoS One 6, e16059 (2011). · DOI
- Chao, D. Y. et al. Comprehensive evaluation of differential serodiagnosis between Zika and dengue viral infections. J. Clin. Microbiol. 57, e01506-18 (2019). · DOI
- deAlwis, R. et al. In-depth analysis of the antibody response of individuals exposed to primary dengue virus infection. PLoS Negl. Trop. Dis. 5, e1188 (2011). · DOI
- Tsai, W. et al. High-avidity and potently neutralizing cross-reactive human monoclonal antibodies derived from secondary dengue virus infection. J. Virol. 87, 12562–12575 (2013). · DOI
- Cavallo, L., Kleinjung, J. & Fraternali, F. POPS: a fast algorithm for solvent accessible surface areas at atomic and residue level. Nucleic Acids Res. 31, 3364–3366 (2003). · DOI
- Kohler, G. & Milstein, C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 254, 84–87 (1975).
- Chen, Y. C. et al. Generation and characterization of monoclonal antibodies against dengue virus type 1 for epitope mapping and serological detection by epitope-based peptide antigens. Clin. Vaccin. Immunol. 14, 404–411 (2007). · DOI
Metadata
- Authors
- Salem, G. M., Galula, J. U., Wu, S.-R., Liu, J.-H., Chen, Y.-H., Wang, W.-H., Wang, S.-F., Song, C.-S., Chen, F.-C., Abarientos, A. B., Chen, G.-W., Wang, C.-I., & Chao, D.-Y.
- Affiliations
- National Chung Hsing University (TW)
- National Cheng Kung University (TW)
- National Sun Yat-sen University (TW)
- Kaohsiung Medical University (TW)
- Agency for Science, Technology and Research (SG)
- Corresponding author
- Chao, Day-Yu
- ORCID
- Venue
- Communications Biology
- Published
- 2024-01-24
- Volume
- 7
- Issue
- 1
- Pages
- 15-15
- ISSN
- 2399-3642 (ISSN-L)
- PMC
- PMC10808242
- OpenAlex
- W4391168722
- Cited by
- 14
- References
- 1
- Citations by year
- 2026: 7 · 2025: 5 · 2024: 2
- FWCI
- 5.77
- Type
- journal article
- Language
- en
- Update notices
- correction (2024-03-01)
- Open access
- gold
- doi.org
- Locations
- Communications Biology (publishedVersion, cc-by)
- Research Square (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Ministry of Science and Technology, Taiwan (MOST-110-2313-B-005-041)
- Topics
- Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Mosquito-borne diseases and control
- Health Sciences › Medicine › Infectious Diseases › Viral Infections and Vectors
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Keywords
- Zika virus, Japanese encephalitis virus, dengue virus, cross-reactive antibodies, monoclonal antibodies, humoral immunity, flavivirus cross-reactivity, somatic hypermutation, quaternary epitope, heterologous immunity
- MeSH terms
- Zika Virus Infection, Zika Virus, Animals, Antibodies, Monoclonal, Dengue, Encephalitis Virus, Japanese, Humans, Cryoelectron Microscopy, Mice
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