Pierson, T. C. & Diamond, M. S. The continued menace of rising flaviviruses. Nat. Microbiol. 5, 796–812 (2020).
Kaiser, J. A., Wang, T. & Barrett, A. D. Virulence determinants of West Nile virus: how can these be used for vaccine design? Future Virol. 12, 283–295 (2017).
Arroyo, J. et al. ChimeriVax-West Nile virus live-attenuated vaccine: preclinical analysis of security, immunogenicity, and efficacy. J. Virol. 78, 12497–12507 (2004).
Kaiser, J. A. et al. Genotypic and phenotypic characterization of West Nile virus NS5 methyltransferase mutants. Vaccine 37, 7155–7164 (2019).
Li, G. et al. An attenuated Zika virus NS4B protein mutant is a potent inducer of antiviral immune responses. NPJ Vaccines 4, 48 (2019).
Zust, R. et al. Rational design of a dwell attenuated dengue vaccine: 2’-o-methyltransferase mutants are extremely attenuated and immunogenic in mice and macaques. PLoS Pathog. 9, e1003521 (2013).
Wicker, J. A. et al. A single amino acid substitution within the central portion of the West Nile virus NS4B protein confers a extremely attenuated phenotype in mice. Virology 349, 245–253 (2006).
Crabtree, M. B., Kinney, R. M. & Miller, B. R. Deglycosylation of the NS1 protein of dengue 2 virus, pressure 16681: building and characterization of mutant viruses. Arch. Virol. 150, 771–786 (2005).
Whiteman, M. C. et al. Growth and characterization of non-glycosylated E and NS1 mutant viruses as a possible candidate vaccine for West Nile virus. Vaccine 28, 1075–1083 (2010).
Muylaert, I. R., Chambers, T. J., Galler, R. & Rice, C. M. Mutagenesis of the N-linked glycosylation websites of the yellow fever virus NS1 protein: results on virus replication and mouse neurovirulence. Virology 222, 159–168 (1996).
Hurrelbrink, R. J. & McMinn, P. C. Molecular determinants of virulence: the structural and useful foundation for flavivirus attenuation. Adv. Virus Res. 60, 1–42 (2003).
Kuno, G., Chang, G. J., Tsuchiya, Okay. R., Karabatsos, N. & Cropp, C. B. Phylogeny of the genus Flavivirus. J. Virol. 72, 73–83 (1998).
Zhang, S. et al. A mutation within the envelope protein fusion loop attenuates mouse neuroinvasiveness of the NY99 pressure of West Nile virus. Virology 353, 35–40 (2006).
Huang, C. Y. et al. The dengue virus kind 2 envelope protein fusion peptide is crucial for membrane fusion. Virology 396, 305–315 (2010).
Wang, X. et al. Close to-atomic construction of Japanese encephalitis virus reveals essential determinants of virulence and stability. Nat. Commun. 8, 14 (2017).
Rey, F. A., Heinz, F. X., Mandl, C., Kunz, C. & Harrison, S. C. The envelope glycoprotein from tick-borne encephalitis virus at 2 A decision. Nature 375, 291–298 (1995).
Allison, S. L., Schalich, J., Stiasny, Okay., Mandl, C. W. & Heinz, F. X. Mutational proof for an inner fusion peptide in flavivirus envelope protein E. J. Virol. 75, 4268–4275 (2001).
Kuhn, R. J. et al. Construction of dengue virus: implications for flavivirus group, maturation, and fusion. Cell 108, 717–725 (2002).
Allison, S. L. et al. Oligomeric rearrangement of tick-borne encephalitis virus envelope proteins induced by an acidic pH. J. Virol. 69, 695–700 (1995).
Modis, Y., Ogata, S., Clements, D. & Harrison, S. C. Construction of the dengue virus envelope protein after membrane fusion. Nature 427, 313–319 (2004).
Modis, Y., Ogata, S., Clements, D. & Harrison, S. C. A ligand-binding pocket within the dengue virus envelope glycoprotein. Proc. Natl. Acad. Sci. USA 100, 6986–6991 (2003).
Kanai, R. et al. Crystal construction of west nile virus envelope glycoprotein reveals viral floor epitopes. J. Virol. 80, 11000–11008 (2006).
Bressanelli, S. et al. Construction of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation. EMBO J. 23, 728–738 (2004).
Cecilia, D. & Gould, E. A. Nucleotide adjustments answerable for lack of neuroinvasiveness in Japanese encephalitis virus neutralization-resistant mutants. Virology 181, 70–77 (1991).
Beasley, D. W. & Aaskov, J. G. Epitopes on the dengue 1 virus envelope protein acknowledged by neutralizing IgM monoclonal antibodies. Virology 279, 447–458 (2001).
de Wispelaere, M. et al. Inhibition of flaviviruses by focusing on a conserved pocket on the viral envelope protein. Cell Chem. Biol. 25, 1006–1016.e1008 (2018).
Monath, T. P. et al. Single mutation within the flavivirus envelope protein hinge area will increase neurovirulence for mice and monkeys however decreases viscerotropism for monkeys: relevance to growth and security testing of dwell, attenuated vaccines. J. Virol. 76, 1932–1943 (2002).
Lee, E., Weir, R. C. & Dalgarno, L. Modifications within the dengue virus main envelope protein on passaging and their localization on the three-dimensional construction of the protein. Virology 232, 281–290 (1997).
Schlesinger, J. J. et al. Replication of yellow fever virus within the mouse central nervous system: comparability of neuroadapted and non-neuroadapted virus and partial sequence evaluation of the neuroadapted pressure. J. Gen. Virol. 77, 1277–1285 (1996).
McMinn, P. C., Weir, R. C. & Dalgarno, L. A mouse-attenuated envelope protein variant of Murray Valley encephalitis virus with altered fusion exercise. J. Gen. Virol. 77, 2085–2088 (1996).
Butrapet, S. et al. Amino acid adjustments throughout the E protein hinge area that have an effect on dengue virus kind 2 infectivity and fusion. Virology 413, 118–127 (2011).
Kinney, R. M. et al. Avian virulence and thermostable replication of the North American pressure of West Nile virus. J. Gen. Virol. 87, 3611–3622 (2006).
Whiteman, M. C. et al. A number of amino acid adjustments on the first glycosylation motif in NS1 protein of West Nile virus are obligatory for full attenuation for mouse neuroinvasiveness. Vaccine 29, 9702–9710 (2011).
Beasley, D. W. et al. Envelope protein glycosylation standing influences mouse neuroinvasion phenotype of genetic lineage 1 West Nile virus strains. J. Virol. 79, 8339–8347 (2005).
Kaiser, J. A. & Barrett, A. D. T. Twenty years of progress towards West Nile virus vaccine growth. Viruses 11, 823 (2019).
Muraki, Y. et al. The efficacy of inactivated West Nile vaccine (WN-VAX) in mice and monkeys. Virol. J. 12, 54 (2015).
Ferguson, M. et al. WHO Working Group on technical specs for manufacture and analysis of yellow fever vaccines, Geneva, Switzerland, 13-14 Could 2009. Vaccine 28, 8236–8245 (2010).
Trent, D. W. et al. WHO working group on the standard, security and efficacy of japanese encephalitis vaccines (dwell attenuated) for human use, Bangkok, Thailand, 21-23 February 2012. Biologicals 41, 450–457 (2013).
Thomas, S. J. & Yoon, I. Okay. A evaluation of Dengvaxia(R): growth to deployment. Hum. Vaccin Immunother. 15, 2295–2314 (2019).
Kaiser, J. A. et al. Japanese encephalitis vaccine-specific envelope protein E138K mutation doesn’t attenuate virulence of West Nile virus. NPJ Vaccines 4, 50 (2019).
Goo, L., VanBlargan, L. A., Dowd, Okay. A., Diamond, M. S. & Pierson, T. C. A single mutation within the envelope protein modulates flavivirus antigenicity, stability, and pathogenesis. PLoS Pathog. 13, e1006178 (2017).
Hurrelbrink, R. J. & McMinn, P. C. Attenuation of Murray Valley encephalitis virus by site-directed mutagenesis of the hinge and putative receptor-binding areas of the envelope protein. J. Virol. 75, 7692–7702 (2001).
Man, B. et al. Preclinical and medical growth of YFV 17D-based chimeric vaccines in opposition to dengue, West Nile and Japanese encephalitis viruses. Vaccine 28, 632–649 (2010).
Zhang, X. Okay. et al. Cryo-EM construction of the mature dengue virus at 3.5-angstrom decision. Nat. Struct. Mol. Biol. 20, 105–U133 (2013).
Moratorio, G., Iriarte, A., Moreno, P., Musto, H. & Cristina, J. An in depth comparative evaluation on the general codon utilization patterns in West Nile virus. Infect. Genet. Evol. 14, 396–400 (2013).
Kudlacek, S. T. et al. Designed, extremely expressing, thermostable dengue virus 2 envelope protein dimers elicit quaternary epitope antibodies. Sci. Adv. 7, eabg4084 (2021).
Onofrio, A. et al. Distance-dependent hydrophobic-hydrophobic contacts in protein folding simulations. Phys. Chem. Chem. Phys. 16, 18907–18917 (2014).
Ni, H. et al. Interplay of yellow fever virus French neurotropic vaccine pressure with monkey mind: characterization of monkey mind membrane receptor escape variants. J. Virol. 74, 2903–2906 (2000).
Christian, E. A. et al. Atomic-level useful mannequin of dengue virus Envelope protein infectivity. Proc. Natl. Acad. Sci. USA 110, 18662–18667 (2013).
Gibbons, D. L. et al. Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus. Nature 427, 320–325 (2004).
Guardado-Calvo, P. et al. Mechanistic perception into bunyavirus-induced membrane fusion from structure-function analyses of the hantavirus envelope glycoprotein Gc. PLoS Pathog. 12, e1005813 (2016).
Serris, A. et al. The hantavirus floor glycoprotein lattice and its fusion management mechanism. Cell 183, 442–456.e416 (2020).
Monera, O. D., Sereda, T. J., Zhou, N. E., Kay, C. M. & Hodges, R. S. Relationship of sidechain hydrophobicity and alpha-helical propensity on the steadiness of the single-stranded amphipathic alpha-helix. J. Pept. Sci. 1, 319–329 (1995).
Kovacs, J. M., Mant, C. T. & Hodges, R. S. Willpower of intrinsic hydrophilicity/hydrophobicity of amino acid facet chains in peptides within the absence of nearest-neighbor or conformational results. Biopolymers 84, 283–297 (2006).
Beasley, D. W. et al. Restricted evolution of West Nile virus has occurred throughout its southwesterly unfold in the USA. Virology 309, 190–195 (2003).
Chao, D. Y., Davis, B. S. & Chang, G. J. Growth of multiplex real-time reverse transcriptase PCR assays for detecting eight medically necessary flaviviruses in mosquitoes. J. Clin. Microbiol. 45, 584–589 (2007).
Clarke, D. H. & Casals, J. Methods for hemagglutination and hemagglutination-inhibition with arthropod-borne viruses. Am. J. Trop. Med. Hyg. 7, 561–573 (1958).
Lyons, A. C. et al. Shedding of Japanese encephalitis virus in oral fluid of contaminated swine. Vector Borne Zoonotic. Dis. 18, 469–474 (2018).
Roehrig, J. T., Hombach, J. & Barrett, A. D. Tips for plaque-reduction neutralization testing of human antibodies to dengue viruses. Viral Immunol. 21, 123–132 (2008).