{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,24]],"date-time":"2026-10-24T13:27:34Z","timestamp":1792848454045,"version":"4.5.0"},"reference-count":162,"publisher":"MDPI AG","issue":"7","license":[{"start":{"date-parts":[[2018,6,28]],"date-time":"2018-06-28T00:00:00Z","timestamp":1530144000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100010665","name":"H2020 Marie Sk\u0142odowska-Curie Actions","doi-asserted-by":"publisher","award":["799929"],"award-info":[{"award-number":["799929"]}],"id":[{"id":"10.13039\/100010665","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100010665","name":"H2020 Marie Sk\u0142odowska-Curie Actions","doi-asserted-by":"publisher","award":["765042"],"award-info":[{"award-number":["765042"]}],"id":[{"id":"10.13039\/100010665","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002341","name":"Academy of Finland","doi-asserted-by":"publisher","award":["275199"],"award-info":[{"award-number":["275199"]}],"id":[{"id":"10.13039\/501100002341","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100007798","name":"Helsingin Yliopiston Tiedes\u00e4\u00e4ti\u00f6","doi-asserted-by":"publisher","award":["Grant to L.I.A.P."],"award-info":[{"award-number":["Grant to L.I.A.P."]}],"id":[{"id":"10.13039\/100007798","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Viruses"],"abstract":"<jats:p>Tick-borne encephalitis virus (TBEV) is a growing health concern. It causes a severe disease that can lead to permanent neurological complications or death and the incidence of TBEV infections is constantly rising. Our understanding of TBEV\u2019s structure lags behind that of other flaviviruses, but has advanced recently with the publication of a high-resolution structure of the TBEV virion. The gaps in our knowledge include: aspects of receptor binding, replication and virus assembly. Furthermore, TBEV has mostly been studied in mammalian systems, even though the virus\u2019 interaction with its tick hosts is a central part of its life cycle. Elucidating these aspects of TBEV biology are crucial for the development of TBEV antivirals, as well as the improvement of diagnostics. In this review, we summarise the current structural knowledge on TBEV, bringing attention to the current gaps in our understanding, and propose further research that is needed to truly understand the structural-functional relationship of the virus and its hosts.<\/jats:p>","DOI":"10.3390\/v10070350","type":"journal-article","created":{"date-parts":[[2018,6,28]],"date-time":"2018-06-28T10:53:33Z","timestamp":1530183213000},"page":"350","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":98,"title":["Tick-Borne Encephalitis Virus: A Structural View"],"prefix":"10.3390","volume":"10","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3919-2498","authenticated-orcid":false,"given":"Lauri I. A.","family":"Pulkkinen","sequence":"first","affiliation":[{"name":"HiLIFE\u2014Institute of Biotechnology, University of Helsinki, 00790 Helsinki, Finland"},{"name":"Faculty of Biological and Environmental Sciences, University of Helsinki, 00790 Helsinki, Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7060-5871","authenticated-orcid":false,"given":"Sarah J.","family":"Butcher","sequence":"additional","affiliation":[{"name":"HiLIFE\u2014Institute of Biotechnology, University of Helsinki, 00790 Helsinki, Finland"},{"name":"Faculty of Biological and Environmental Sciences, University of Helsinki, 00790 Helsinki, Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4555-6446","authenticated-orcid":false,"given":"Maria","family":"Anastasina","sequence":"additional","affiliation":[{"name":"HiLIFE\u2014Institute of Biotechnology, University of Helsinki, 00790 Helsinki, Finland"},{"name":"Faculty of Biological and Environmental Sciences, University of Helsinki, 00790 Helsinki, Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2018,6,28]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"430","DOI":"10.12998\/wjcc.v3.i5.430","article-title":"Tick-borne encephalitis: A review of epidemiology, clinical characteristics, and management","volume":"3","author":"Bogovic","year":"2015","journal-title":"World J. Clin. Cases"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1214-e61","DOI":"10.1111\/ene.13356","article-title":"EAN consensus review on prevention, diagnosis and management of tick-borne encephalitis","volume":"24","author":"Taba","year":"2017","journal-title":"Eur. J. Neurol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/j.virol.2006.09.015","article-title":"Genetic characterization of tick-borne flaviviruses: New insights into evolution, pathogenetic determinants and taxonomy","volume":"361","author":"Grard","year":"2007","journal-title":"Virology"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"8663","DOI":"10.1128\/JVI.01013-12","article-title":"Revisiting the clinal concept of evolution and dispersal for the tick-borne flaviviruses by using phylogenetic and biogeographic analyses","volume":"86","author":"Heinze","year":"2012","journal-title":"J. Virol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1099\/0022-1317-80-1-179","article-title":"Sequence analysis and genetic classification of tick-borne encephalitis viruses from Europe and Asia","volume":"80","author":"Ecker","year":"1999","journal-title":"J. Gen. Virol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1006\/viro.1995.1557","article-title":"The flavivirus 3\u2019-noncoding region: Extensive size heterogeneity independent of evolutionary relationships among strains of tick-borne encephalitis virus","volume":"213","author":"Wallner","year":"1995","journal-title":"Virology"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1035","DOI":"10.1099\/0022-1317-77-5-1035","article-title":"Characterization and complete genome sequences of high- and low-virulence variants of tick-borne encephalitis virus","volume":"77","author":"Wallner","year":"1996","journal-title":"J. Gen. Virol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"18916","DOI":"10.2807\/ese.13.26.18916-en","article-title":"Tick-borne encephalitis in Europe and beyond\u2014The epidemiological situation as of 2007","volume":"13","author":"Suss","year":"2008","journal-title":"Euro Surveill."},{"key":"ref_9","first-page":"19976","article-title":"Tick-borne encephalitis in Europe, 2007 to 2009","volume":"16","author":"Mantke","year":"2011","journal-title":"Euro Surveill."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1671","DOI":"10.3201\/eid1510.090743","article-title":"Tick-borne encephalitis from eating goat cheese in a mountain region of Austria","volume":"15","author":"Holzmann","year":"2009","journal-title":"Emerg. Infect. Dis."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"806","DOI":"10.3201\/eid1905.121442","article-title":"Tick-borne encephalitis associated with consumption of raw goat milk, Slovenia, 2012","volume":"19","author":"Hudopisk","year":"2013","journal-title":"Emerg. Infect. Dis."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"4556","DOI":"10.1016\/j.vaccine.2011.04.061","article-title":"The current perspective on tick-borne encephalitis awareness and prevention in six Central and Eastern European countries: Report from a meeting of experts convened to discuss TBE in their region","volume":"29","author":"Kollaritsch","year":"2011","journal-title":"Vaccine"},{"key":"ref_13","first-page":"2157","article-title":"Tick-borne encephalitis vaccines","volume":"2011","author":"Lehrer","year":"2011","journal-title":"J. Bioterror. Biodef."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"8448","DOI":"10.3402\/gha.v4i0.8448","article-title":"The impact of climate change on the expansion of Ixodes persulcatus habitat and the incidence of tick-borne encephalitis in the north of European Russia","volume":"4","author":"Tokarevich","year":"2011","journal-title":"Glob. Health Action"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"20140051","DOI":"10.1098\/rstb.2014.0051","article-title":"Climate change and Ixodes tick-borne diseases of humans","volume":"370","author":"Ostfeld","year":"2015","journal-title":"Philos. Trans. R. Soc. B Biol. Sci."},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Moureau, G., Cook, S., Lemey, P., Nougairede, A., Forrester, N.L., Khasnatinov, M., Charrel, R.N., Firth, A.E., Gould, E.A., and De Lamballerie, X. (2015). New insights into flavivirus evolution, taxonomy and biogeographic history, extended by analysis of canonical and alternative coding sequences. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0117849"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1867","DOI":"10.1099\/0022-1317-82-8-1867","article-title":"Phylogenetic relationships of flaviviruses correlate with their epidemiology, disease association and biogeography","volume":"82","author":"Gaunt","year":"2001","journal-title":"J. Gen. Virol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"436","DOI":"10.1038\/s41467-018-02882-0","article-title":"Structure of tick-borne encephalitis virus and its neutralization by a monoclonal antibody","volume":"9","author":"Yoshii","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_19","unstructured":"Knipe, D., and Howley, P. (2013). Flaviviridae. Fields Virology, Lippincott Williams & Wilkins."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1128\/jvi.5.4.524-532.1970","article-title":"Physical and biological properties of dengue-2 virus and associated antigens","volume":"5","author":"Smith","year":"1970","journal-title":"J. Virol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1016\/S0092-8674(02)00660-8","article-title":"Structure of dengue virus: Implications for flavivirus organization, maturation, and fusion","volume":"108","author":"Kuhn","year":"2002","journal-title":"Cell"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1126\/science.1089316","article-title":"Structure of West Nile virus","volume":"302","author":"Mukhopadhyay","year":"2003","journal-title":"Science"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1038\/nsmb.2463","article-title":"Cryo-EM structure of the mature dengue virus at 3.5-\u00c5 resolution","volume":"20","author":"Zhang","year":"2012","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1126\/science.aaf5316","article-title":"The 3.8 \u00c5 resolution cryo-EM structure of Zika virus","volume":"352","author":"Sirohi","year":"2016","journal-title":"Science"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1038\/s41467-017-00024-6","article-title":"Near-atomic structure of Japanese encephalitis virus reveals critical determinants of virulence and stability","volume":"8","author":"Wang","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/j.jsb.2013.04.005","article-title":"Membrane curvature in flaviviruses","volume":"183","author":"Zhang","year":"2013","journal-title":"J. Struct. Biol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1016\/j.jsb.2006.09.002","article-title":"Structural analysis of viral nucleocapsids by subtraction of partial projections","volume":"157","author":"Zhang","year":"2007","journal-title":"J. Struct. Biol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1038\/375291a0","article-title":"The envelope glycoprotein from tick-borne encephalitis virus at 2 \u00c5 resolution","volume":"375","author":"Rey","year":"1995","journal-title":"Nature"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"3043","DOI":"10.1016\/j.vaccine.2004.11.068","article-title":"Role of the N-linked glycans of the prM and E envelope proteins in tick-borne encephalitis virus particle secretion","volume":"23","author":"Goto","year":"2005","journal-title":"Vaccine"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"2249","DOI":"10.1099\/vir.0.055269-0","article-title":"N-linked glycan in tick-borne encephalitis virus envelope protein affects viral secretion in mammalian cells, but not in tick cells","volume":"94","author":"Yoshii","year":"2013","journal-title":"J. Gen. Virol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"4268","DOI":"10.1128\/JVI.75.9.4268-4275.2001","article-title":"Mutational evidence for an internal fusion peptide in flavivirus envelope protein E","volume":"75","author":"Allison","year":"2001","journal-title":"J. Virol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"11000","DOI":"10.1128\/JVI.01735-06","article-title":"Crystal structure of West Nile virus envelope glycoprotein reveals viral surface epitopes","volume":"80","author":"Kanai","year":"2006","journal-title":"J. Virol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1342","DOI":"10.1110\/ps.051844006","article-title":"NMR solution structure and backbone dynamics of domain III of the E protein of tick-borne Langat flavivirus suggests a potential site for molecular recognition","volume":"15","author":"Mukherjee","year":"2006","journal-title":"Protein Sci."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1016\/j.virol.2006.03.030","article-title":"Structure of the envelope protein domain III of Omsk hemorrhagic fever virus","volume":"351","author":"Volk","year":"2006","journal-title":"Virology"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/j.virol.2009.09.001","article-title":"Structure of yellow fever virus envelope protein domain III","volume":"394","author":"Volk","year":"2009","journal-title":"Virology"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"9601","DOI":"10.1128\/JVI.74.20.9601-9609.2000","article-title":"Attenuation of tick-borne encephalitis virus by structure-based site-specific mutagenesis of a putative flavivirus receptor binding site","volume":"74","author":"Mandl","year":"2000","journal-title":"J. Virol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"7828","DOI":"10.1128\/JVI.00196-14","article-title":"Specificities of human CD4+ T cell responses to an inactivated flavivirus vaccine and infection: correlation with structure and epitope prediction","volume":"88","author":"Scheinost","year":"2014","journal-title":"J. Virol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"3414","DOI":"10.1073\/pnas.0305892101","article-title":"Solution structure of dengue virus capsid protein reveals another fold","volume":"101","author":"Ma","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1157","DOI":"10.1016\/j.str.2004.04.024","article-title":"West Nile Virus Core Protein: Tetramer Structure and Ribbon Formation","volume":"12","author":"Dokland","year":"2004","journal-title":"Structure"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"948","DOI":"10.1016\/j.jmb.2018.02.006","article-title":"Crystal structure of the capsid protein from Zika virus","volume":"430","author":"Shang","year":"2018","journal-title":"J. Mol. Biol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"6471","DOI":"10.1128\/JVI.02120-06","article-title":"Functional requirements of the yellow fever virus capsid protein","volume":"81","author":"Patkar","year":"2007","journal-title":"J. Virol."},{"key":"ref_42","doi-asserted-by":"crossref","unstructured":"Zhang, Y. (2008). I-TASSER server for protein 3D structure prediction. BMC Bioinform., 9.","DOI":"10.1186\/1471-2105-9-40"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1038\/nprot.2010.5","article-title":"I-TASSER: A unified platform for automated protein structure and function prediction","volume":"5","author":"Roy","year":"2010","journal-title":"Nat. Protoc."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1038\/nmeth.3213","article-title":"The I-TASSER suite: Protein structure and function prediction","volume":"12","author":"Yang","year":"2014","journal-title":"Nat. Methods"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1093\/nar\/gku316","article-title":"Deciphering key features in protein structures with the new ENDscript server","volume":"42","author":"Robert","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1254","DOI":"10.1099\/vir.0.83264-0","article-title":"Multiple regions in dengue virus capsid protein contribute to nuclear localization during virus infection","volume":"89","author":"Sangiambut","year":"2008","journal-title":"J. Gen. Virol."},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Colpitts, T.M., Barthel, S., Wang, P., and Fikrig, E. (2011). Dengue virus capsid protein binds core histones and inhibits nucleosome formation in human liver cells. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0024365"},{"key":"ref_48","first-page":"1688","article-title":"West Nile virus and dengue virus capsid protein negates the antiviral activity of human Sec3 protein through the proteasome pathway","volume":"15","author":"Bhuvanakantham","year":"2013","journal-title":"Cell. Microbiol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"13863","DOI":"10.1073\/pnas.1600544113","article-title":"Yellow fever virus capsid protein is a potent suppressor of RNA silencing that binds double-stranded RNA","volume":"113","author":"Samuel","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"2604","DOI":"10.1093\/emboj\/cdg270","article-title":"Structures of immature flavivirus particles","volume":"22","author":"Zhang","year":"2003","journal-title":"EMBO J."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1607","DOI":"10.1016\/j.str.2004.06.019","article-title":"Conformational changes of the flavivirus E glycoprotein","volume":"12","author":"Zhang","year":"2004","journal-title":"Structure"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"6141","DOI":"10.1128\/JVI.00037-07","article-title":"Structure of immature West Nile virus","volume":"81","author":"Zhang","year":"2007","journal-title":"J. Virol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1830","DOI":"10.1126\/science.1153263","article-title":"The flavivirus precursor membrane-envelope protein complex: Structure and maturation","volume":"319","author":"Li","year":"2008","journal-title":"Science"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"1834","DOI":"10.1126\/science.1153264","article-title":"Structure of the immature dengue virus at low pH primes proteolytic maturation","volume":"319","author":"Yu","year":"2008","journal-title":"Science"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"602","DOI":"10.1038\/embor.2011.75","article-title":"Maturation of flaviviruses starts from one or more icosahedrally independent nucleation centres","volume":"12","author":"Plevka","year":"2011","journal-title":"EMBO Rep."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"7700","DOI":"10.1128\/JVI.00197-13","article-title":"Immature and mature dengue serotype 1 virus structures provide insight into the maturation process","volume":"87","author":"Kostyuchenko","year":"2013","journal-title":"J. Virol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1038\/nsmb.3352","article-title":"Structure of the immature Zika virus at 9 \u00c5 resolution","volume":"24","author":"Prasad","year":"2017","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Van Der Schaar, H.M., Rust, M.J., Chen, C., Van Der Ende-Metselaar, H., Wilschut, J., Zhuang, X., and Smit, J.M. (2008). Dissecting the cell entry pathway of dengue virus by single-particle tracking in living cells. PLoS Pathog., 4.","DOI":"10.1371\/journal.ppat.1000244"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"1533","DOI":"10.1111\/j.1462-5822.2009.01345.x","article-title":"Alternative infectious entry pathways for dengue virus serotypes into mammalian cells","volume":"11","author":"Acosta","year":"2009","journal-title":"Cell. Microbiol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1186\/1423-0127-16-17","article-title":"Characterization of dengue virus entry into HepG2 cells","volume":"16","author":"Suksanpaisan","year":"2009","journal-title":"J. Biomed. Sci."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"632","DOI":"10.1016\/S0934-8840(99)80021-8","article-title":"Human laminin binding protein as a cell receptor for the tick-borne encephalitis virus","volume":"289","author":"Protopopova","year":"1999","journal-title":"Zent. Bakteriol."},{"key":"ref_62","first-page":"1328","article-title":"C-terminal fragment of human laminin-binding protein contains a receptor domain for Venezuelan equine encephalitis and tick-borne encephalitis viruses","volume":"74","author":"Malygin","year":"2009","journal-title":"Biochemistry"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1002\/jmr.2399","article-title":"Force-induced globule-coil transition in laminin binding protein and its role for viral-cell membrane fusion","volume":"27","author":"Zaitsev","year":"2014","journal-title":"J. Mol. Recognit."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1007\/BF01309594","article-title":"Tick-borne encephalitis virus interaction with the target cells","volume":"127","author":"Maldov","year":"1992","journal-title":"Arch. Virol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1159\/000024954","article-title":"A putative host cell receptor for tick-borne encephalitis virus identified by anti-idiotypic antibodies and virus affinoblotting","volume":"42","author":"Grubhoffer","year":"1999","journal-title":"Intervirology"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1006\/viro.1999.0172","article-title":"Membrane fusion activity of tick-borne encephalitis virus and recombinant subviral particles in a liposomal model system","volume":"269","author":"Corver","year":"2000","journal-title":"Virology"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"8536","DOI":"10.1128\/JVI.78.16.8536-8542.2004","article-title":"Effect of membrane curvature-modifying lipids on membrane fusion by tick-borne encephalitis virus","volume":"78","author":"Stiasny","year":"2004","journal-title":"J. Virol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"69","DOI":"10.3390\/v6010069","article-title":"Flavivirus entry receptors: An update","volume":"6","author":"Meertens","year":"2013","journal-title":"Viruses"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"5047","DOI":"10.1074\/jbc.273.9.5047","article-title":"Interaction between Pseudorabies Virus and Heparin\/Heparan Sulfate. Pseudorabies virus mutants differ in their interaction with heparin\/heparan sulfate when altered for specific glycoprotein C heparin-binding domain","volume":"273","author":"Trybala","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"10128","DOI":"10.1128\/JVI.76.20.10128-10137.2002","article-title":"Adaptation of alphaviruses to heparan sulfate: Interaction of sindbis and Semliki Forest viruses with liposomes containing lipid-conjugated heparin","volume":"76","author":"Smit","year":"2002","journal-title":"J. Virol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1016\/S0042-6822(02)00097-1","article-title":"Role of heparan sulfate for attachment and entry of tick-borne encephalitis virus","volume":"308","author":"Kroschewski","year":"2003","journal-title":"Virology"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"12714","DOI":"10.1128\/JVI.00717-09","article-title":"Heparan sulfate proteoglycans are required for cellular binding of the hepatitis E Virus ORF2 capsid protein and for viral infection","volume":"83","author":"Kalia","year":"2009","journal-title":"J. Virol."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1016\/j.virol.2009.12.012","article-title":"GAG-binding variants of tick-borne encephalitis virus","volume":"398","author":"Kozlovskaya","year":"2010","journal-title":"Virology"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"13767","DOI":"10.1128\/JVI.01364-12","article-title":"Heparan sulfate facilitates Rift Valley fever virus entry into the cell","volume":"86","author":"Kortekaas","year":"2012","journal-title":"J. Virol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"5627","DOI":"10.1128\/JVI.75.12.5627-5637.2001","article-title":"Adaptation of tick-borne encephalitis virus to BHK-21 cells results in the formation of multiple heparan sulfate binding sites in the envelope protein and attenuation in vivo","volume":"75","author":"Mandl","year":"2001","journal-title":"J. Virol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/0042-6822(87)90460-0","article-title":"Studies on the glycosylation of flavivirus E proteins and the role of carbohydrate in antigenic structure","volume":"159","author":"Winkler","year":"1987","journal-title":"Virology"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1099\/0022-1317-74-5-931","article-title":"Single amino acid codon changes detected in louping ill virus antibody-resistant mutants with reduced neurovirulence","volume":"74","author":"Jiang","year":"1993","journal-title":"J. Gen. Virol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1016\/j.cell.2005.11.042","article-title":"Cryo-EM reconstruction of dengue virus in complex with the carbohydrate recognition domain of DC-SIGN","volume":"124","author":"Pokidysheva","year":"2006","journal-title":"Cell"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"1831","DOI":"10.1099\/0022-1317-66-8-1831","article-title":"Antibody-dependent enhancement of tick-borne encephalitis virus infectivity","volume":"66","author":"Phillpotts","year":"1985","journal-title":"J. Gen. Virol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1016\/j.virol.2010.12.020","article-title":"Antibody-mediated neutralization of flaviviruses: A reductionist view","volume":"411","author":"Dowd","year":"2011","journal-title":"Virology"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1126\/science.aan6836","article-title":"Antibody-dependent enhancement of severe dengue disease in humans","volume":"6836","author":"Katzelnick","year":"2017","journal-title":"Science"},{"key":"ref_82","doi-asserted-by":"crossref","unstructured":"Haslwanter, D., Blaas, D., Heinz, F.X., and Stiasny, K. (2017). A novel mechanism of antibody-mediated enhancement of flavivirus infection. PLoS Pathog., 13.","DOI":"10.1371\/journal.ppat.1006643"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1083\/jcb.200806081","article-title":"Identification of specific histidines as pH sensors in flavivirus membrane fusion","volume":"183","author":"Fritz","year":"2008","journal-title":"J. Cell Biol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"3784","DOI":"10.1128\/JVI.76.8.3784-3790.2002","article-title":"Membrane interactions of the tick-borne encephalitis virus fusion protein E at low pH membrane interactions of the tick-borne encephalitis virus fusion protein E at low pH","volume":"76","author":"Stiasny","year":"2002","journal-title":"J. Virol."},{"key":"ref_85","doi-asserted-by":"crossref","unstructured":"Stiasny, K., K\u00f6ssl, C., Lepault, J., Rey, F., and Heinz, F. (2007). Characterization of a structural intermediate of flavivirus membrane fusion. PLoS Pathog., 3.","DOI":"10.1371\/journal.ppat.0030020"},{"key":"ref_86","doi-asserted-by":"crossref","unstructured":"Kaufmann, B., Chipman, P.R., Holdaway, H.A., Johnson, S., Fremont, D.H., Kuhn, R.J., Diamond, M.S., and Rossmann, M.G. (2009). Capturing a flavivirus pre-fusion intermediate. PLoS Pathog., 5.","DOI":"10.1371\/journal.ppat.1000672"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1021\/bi9017895","article-title":"Synthetic fusion peptides of tick-borne encephalitis virus as models for membrane fusion","volume":"49","author":"Pan","year":"2010","journal-title":"Biochemistry"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"2287","DOI":"10.1128\/JVI.02957-12","article-title":"Structure of a dengue virus envelope protein late-stage fusion intermediate","volume":"87","author":"Klein","year":"2013","journal-title":"J. Virol."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"743","DOI":"10.1128\/JVI.02411-14","article-title":"Structure of acidic pH dengue virus showing the fusogenic glycoprotein trimers","volume":"89","author":"Zhang","year":"2015","journal-title":"J. Virol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"5605","DOI":"10.1128\/JVI.73.7.5605-5612.1999","article-title":"Mapping of functional elements in the stem-anchor region of tick-borne encephalitis virus envelope protein E","volume":"73","author":"Allison","year":"1999","journal-title":"J. Virol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"728","DOI":"10.1038\/sj.emboj.7600064","article-title":"Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation","volume":"23","author":"Bressanelli","year":"2004","journal-title":"EMBO J."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"4377","DOI":"10.1128\/JVI.02458-10","article-title":"The Unique Transmembrane hairpin of flavivirus fusion protein E is essential for membrane fusion","volume":"85","author":"Fritz","year":"2011","journal-title":"J. Virol."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"9933","DOI":"10.1128\/JVI.01283-13","article-title":"The membrane-proximal \u201cstem\u201d region increases the stability of the flavivirus E protein postfusion trimer and modulates its structure","volume":"87","author":"Stiasny","year":"2013","journal-title":"J. Virol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"e04389","DOI":"10.7554\/eLife.04389","article-title":"Sequential conformational rearrangements in flavivirus membrane fusion","volume":"3","author":"Chao","year":"2014","journal-title":"eLife"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"e00804-16","DOI":"10.1128\/mBio.00804-16","article-title":"Dengue virus genome uncoating requires ubiquitination","volume":"7","author":"Byk","year":"2016","journal-title":"mBio"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1128\/JVI.78.1.178-186.2004","article-title":"Inefficient signalase cleavage promotes efficient nucleocapsid incorporation into budding flavivirus membranes","volume":"78","author":"Lobigs","year":"2004","journal-title":"J. Virol."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"11201","DOI":"10.1128\/JVI.01025-09","article-title":"Extension of flavivirus protein C differentially affects early RNA synthesis and growth in mammalian and arthropod host cells","volume":"83","author":"Schrauf","year":"2009","journal-title":"J. Virol."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/j.virol.2010.02.008","article-title":"A flavivirus signal peptide balances the catalytic activity of two proteases and thereby facilitates virus morphogenesis","volume":"401","author":"Lobigs","year":"2010","journal-title":"Virology"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"8632","DOI":"10.1128\/JVI.01253-15","article-title":"Context-dependent cleavage of the capsid protein by the West Nile virus protease modulates the efficiency of virus assembly","volume":"89","author":"VanBlargan","year":"2015","journal-title":"J. Virol."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1186\/s12985-016-0590-7","article-title":"Flavivirus NS1: A multifaceted enigmatic viral protein","volume":"13","author":"Rastogi","year":"2016","journal-title":"Virol. J."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1084\/jem.20092545","article-title":"Antagonism of the complement component C4 by flavivirus nonstructural protein NS1","volume":"207","author":"Avirutnan","year":"2010","journal-title":"J. Exp. Med."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"12225","DOI":"10.1128\/JVI.78.22.12225-12235.2004","article-title":"Analysis of adaptive mutations in Kunjin virus replicon RNA reveals a novel role for the flavivirus nonstructural protein NS2A in inhibition of beta interferon promoter-driven transcription","volume":"78","author":"Liu","year":"2004","journal-title":"J. Virol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"1934","DOI":"10.1128\/JVI.79.3.1934-1942.2005","article-title":"Inhibition of interferon signaling by the New York 99 strain and Kunjin subtype of West Nile virus involves blockage of STAT1 and STAT2 activation by nonstructural proteins","volume":"79","author":"Wang","year":"2005","journal-title":"J. Virol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"4731","DOI":"10.1128\/JVI.00002-08","article-title":"Role of nonstructural protein NS2A in flavivirus assembly","volume":"82","author":"Leung","year":"2008","journal-title":"J. Virol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"4609","DOI":"10.1128\/JVI.02424-12","article-title":"Membrane topology and function of dengue virus NS2A protein","volume":"87","author":"Xie","year":"2013","journal-title":"J. Virol."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"5735","DOI":"10.1128\/JVI.00340-16","article-title":"Transmembrane domains of NS2B contribute to both viral RNA replication and particle formation in Japanese encephalitis virus","volume":"90","author":"Li","year":"2016","journal-title":"J. Virol."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/j.antiviral.2015.03.014","article-title":"The flavivirus NS2B-NS3 protease-helicase as a target for antiviral drug development","volume":"118","author":"Luo","year":"2015","journal-title":"Antivir. Res."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"2081","DOI":"10.1099\/vir.0.012864-0","article-title":"NS4A regulates the ATPase activity of the NS3 helicase: A novel cofactor role of the non-structural protein NS4A from West Nile virus","volume":"90","author":"Shiryaev","year":"2009","journal-title":"J. Gen. Virol."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1002\/rmv.1835","article-title":"Flaviviral NS4b, chameleon and jack-in-the-box roles in viral replication and pathogenesis, and a molecular target for antiviral intervention","volume":"25","author":"Zmurko","year":"2015","journal-title":"Rev. Med. Virol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/S0065-3527(09)74002-3","article-title":"New insights into flavivirus nonstructural protein 5","volume":"Volume 74","author":"Davidson","year":"2009","journal-title":"Advances in Virus Research"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"e01970-16","DOI":"10.1128\/JVI.01970-16","article-title":"The many faces of the flavivirus NS5 protein in antagonism of type I interferon signaling","volume":"91","author":"Best","year":"2017","journal-title":"J. Virol."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1038\/nsmb1073","article-title":"Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus","volume":"13","author":"Erbel","year":"2006","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1126\/science.1247749","article-title":"Flavivirus NS1 structures reveal surfaces for associations with membranes and the immune system","volume":"343","author":"Akey","year":"2014","journal-title":"Science"},{"key":"ref_114","doi-asserted-by":"crossref","unstructured":"Zhao, Y., Soh, T.S., Zheng, J., Chan, K.W.K., Phoo, W.W., Lee, C.C., Tay, M.Y.F., Swaminathan, K., Cornvik, T.C., and Lim, S.P. (2015). A crystal structure of the dengue virus NS5 protein reveals a novel inter-domain interface essential for protein flexibility and virus replicatio. PLoS Pathog., 11.","DOI":"10.1371\/journal.ppat.1004682"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"10745","DOI":"10.1038\/srep10745","article-title":"Electron tomography analysis of tick-borne encephalitis virus infection in human neurons","volume":"5","author":"Palus","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"4611","DOI":"10.1128\/JVI.73.6.4611-4621.1999","article-title":"Genetic interaction of flavivirus nonstructural proteins NS1 and NS4A as a determinant of replicase function","volume":"73","author":"Lindenbach","year":"1999","journal-title":"J. Virol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1159\/000091471","article-title":"Differences in maturation of tick-borne encephalitis virus in mammalian and tick cell line","volume":"49","author":"Grubhoffer","year":"2006","journal-title":"Intervirology"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"8873","DOI":"10.1074\/jbc.M609919200","article-title":"The non-structural protein 4A of dengue virus is an integral membrane protein inducing membrane alterations in a 2K-regulated manner","volume":"282","author":"Miller","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"7360","DOI":"10.1128\/JVI.00157-12","article-title":"Evidence for a genetic and physical interaction between nonstructural proteins NS1 and NS4B that modulates replication of West Nile virus","volume":"86","author":"Youn","year":"2012","journal-title":"J. Virol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"6469","DOI":"10.1128\/JVI.03456-12","article-title":"Three-dimensional architecture of tick-borne encephalitis virus replication sites and trafficking of the replicated RNA","volume":"87","author":"Miorin","year":"2013","journal-title":"J. Virol."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"849","DOI":"10.1099\/vir.0.061432-0","article-title":"Tick-borne flaviviruses alter membrane structure and replicate in dendrites of primary mouse neuronal cultures","volume":"95","author":"Hirano","year":"2014","journal-title":"J. Gen. Virol."},{"key":"ref_122","doi-asserted-by":"crossref","unstructured":"Kaufusi, P.H., Kelley, J.F., Yanagihara, R., and Nerurkar, V.R. (2014). Induction of endoplasmic reticulum-derived replication-competent membrane structures by West Nile virus non-structural protein 4B. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0084040"},{"key":"ref_123","doi-asserted-by":"crossref","unstructured":"Yu, C., Achazi, K., M\u00f6ller, L., Schulzke, J.D., Niedrig, M., and B\u00fccker, R. (2014). Tick-borne encephalitis virus replication, intracellular trafficking, and pathogenicity in human intestinal Caco-2 cell monolayers. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0096957"},{"key":"ref_124","doi-asserted-by":"crossref","unstructured":"Offerdahl, D.K., Dorward, D.W., Hansen, B.T., and Bloom, M.E. (2012). A Three-dimensional comparison of tick-borne flavivirus infection in mammalian and tick cell lines. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0047912"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1007\/s00705-009-0350-8","article-title":"In vitro assembly of nucleocapsid-like particles from purified recombinant capsid protein of dengue-2 virus","volume":"154","author":"Gil","year":"2009","journal-title":"Arch. Virol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"3534","DOI":"10.1128\/JVI.76.7.3534-3543.2002","article-title":"Capsid protein C of tick-borne encephalitis virus tolerates large internal deletions and is a favorable target for attenuation of virulence","volume":"76","author":"Kofler","year":"2002","journal-title":"J. Virol."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"5581","DOI":"10.1128\/JVI.02653-08","article-title":"Helices 2 and 3 of West Nile virus capsid protein are dispensable for assembly of infectious virions","volume":"83","author":"Schlick","year":"2009","journal-title":"J. Virol."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1007\/BF01718326","article-title":"RNA binding properties of core protein of the flavivirus Kunjin","volume":"141","author":"Khromykh","year":"1996","journal-title":"Arch. Virol."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"8078","DOI":"10.1128\/JVI.78.15.8078-8084.2004","article-title":"Isolation of capsid protein dimers from the tick-borne encephalitis flavivirus and in vitro assembly of capsid-like particles","volume":"78","author":"Kiermayr","year":"2004","journal-title":"J. Virol."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.coviro.2014.09.020","article-title":"Coupling of replication and assembly in flaviviruses","volume":"9","author":"Sirohi","year":"2014","journal-title":"Curr. Opin. Virol."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"4633","DOI":"10.1128\/JVI.75.10.4633-4640.2001","article-title":"Coupling between replication and packaging of flavivirus RNA: evidence derived from the use of DNA-based full-length cDNA clones of Kunjin virus","volume":"75","author":"Khromykh","year":"2001","journal-title":"J. Virol."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1016\/j.chom.2009.03.007","article-title":"Composition and three-dimensional architecture of the dengue virus replication and assembly sites","volume":"5","author":"Welsch","year":"2009","journal-title":"Cell Host Microbe"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"4687","DOI":"10.1128\/JVI.00118-14","article-title":"Ultrastructural characterization and three-dimensional architecture of replication sites in dengue virus-infected mosquito Cells","volume":"88","author":"Junjhon","year":"2014","journal-title":"J. Virol."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"4773","DOI":"10.1128\/JVI.76.10.4773-4784.2002","article-title":"Mutations in the yellow fever virus nonstructural protein NS2A selectively block production of infectious particles mutations in the yellow fever virus nonstructural protein NS2A selectively block production of infectious particles","volume":"76","author":"Rice","year":"2002","journal-title":"J. Virol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"7804","DOI":"10.1128\/JVI.77.14.7804-7813.2003","article-title":"Molecular and functional analyses of Kunjin virus infectious cDNA clones demonstrate the essential roles for NS2A in virus assembly and for a nonconservative residue in NS3 in RNA replication","volume":"77","author":"Liu","year":"2003","journal-title":"J. Virol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"11255","DOI":"10.1128\/JVI.01559-06","article-title":"Translation of the flavivirus Kunjin NS3 gene in cis but not Its RNA sequence or secondary structure is essential for efficient RNA packaging","volume":"80","author":"Pijlman","year":"2006","journal-title":"J. Virol."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"3342","DOI":"10.1128\/JVI.02447-07","article-title":"Yellow fever virus NS3 plays an essential role in virus assembly independent of its known enzymatic functions","volume":"82","author":"Patkar","year":"2008","journal-title":"J. Virol."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"4951","DOI":"10.1128\/JVI.03351-14","article-title":"A basic cluster in the N terminus of yellow fever virus NS2A contributes to infectious particle production","volume":"89","author":"Wieseler","year":"2015","journal-title":"J. Virol."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"1298","DOI":"10.1128\/JVI.02882-14","article-title":"Two distinct sets of NS2A molecules are responsible for dengue virus RNA synthesis and virion assembly","volume":"89","author":"Xie","year":"2015","journal-title":"J. Virol."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1016\/j.virol.2012.06.028","article-title":"A novel coding-region RNA element modulates infectious dengue virus particle production in both mammalian and mosquito cells and regulates viral replication in Aedes aegypti mosquitoes","volume":"432","author":"Orozco","year":"2012","journal-title":"Virology"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"13094","DOI":"10.1128\/JVI.00704-13","article-title":"Nucleolin interacts with the dengue virus capsid protein and plays a role in formation of infectious virus particles","volume":"87","author":"Balinsky","year":"2013","journal-title":"J. Virol."},{"key":"ref_142","doi-asserted-by":"crossref","unstructured":"Ma, L., Li, F., Zhang, J.-W., Li, W., Zhao, D.-M., Wang, H., Hua, R.-H., and Bu, Z.-G. (2018). Host factor SPCS1 regulates the replication of Japanese encephalitis virus through interactions with transmembrane domains of NS2B. J. Virol.","DOI":"10.1128\/JVI.00197-18"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"5571","DOI":"10.1128\/JVI.01933-10","article-title":"The capsid-binding nucleolar helicase DDX56 is important for infectivity of West Nile virus","volume":"85","author":"Xu","year":"2011","journal-title":"J. Virol."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/j.virol.2016.10.025","article-title":"The nucleolar helicase DDX56 redistributes to West Nile virus assembly sites","volume":"500","author":"Reid","year":"2017","journal-title":"Virology"},{"key":"ref_145","doi-asserted-by":"crossref","unstructured":"Vonderstein, K., Nilsson, E., Hubel, P., Nyg\u00e5rd Skalman, L., Upadhyay, A., Pasto, J., Pichlmair, A., Lundmark, R., and \u00d6verby, A.K. (2017). Viperin targets flavivirus virulence by inducing assembly of non-infectious capsid particles. J. Virol.","DOI":"10.1128\/JVI.01751-17"},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1016\/j.bbrc.2017.02.006","article-title":"The host cell response to tick-borne encephalitis virus","volume":"492","author":"Carletti","year":"2017","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1016\/S1097-2765(01)00206-4","article-title":"Molecular organization of a recombinant subviral particle from tick-borne encephalitis virus","volume":"7","author":"Ferlenghi","year":"2001","journal-title":"Mol. Cell"},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"4370","DOI":"10.1128\/JVI.77.7.4370-4382.2003","article-title":"Intracellular assembly and secretion of recombinant subviral particles from tick-borne encephalitis virus","volume":"77","author":"Lorenz","year":"2003","journal-title":"J. Virol."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"6365","DOI":"10.1128\/JVI.00447-16","article-title":"Membrane anchors of the structural flavivirus proteins and their role in virus assembly","volume":"90","author":"Blazevic","year":"2016","journal-title":"J. Virol."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1006\/viro.1994.1013","article-title":"Structural changes and functional control of the tick-borne encephalitis virus glycoprotein E by the heterodimeric association with protein prM","volume":"198","author":"Heinz","year":"1994","journal-title":"Virology"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1016\/0042-6822(90)90099-D","article-title":"Acidotropic amines inhibit proteolytic processing of flavivirus prM protein","volume":"174","author":"Randolph","year":"1990","journal-title":"Virology"},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"1323","DOI":"10.1099\/0022-1317-72-6-1323","article-title":"Fusion activity of flaviviruses: Comparison of mature and immature (prM-containing) tick-borne encephalitis virions","volume":"72","author":"Guirakhoo","year":"1991","journal-title":"J. Gen. Virol."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"8475","DOI":"10.1128\/jvi.71.11.8475-8481.1997","article-title":"Proteolytic activation of tick-borne encephalitis virus by furin","volume":"71","author":"Stadler","year":"1997","journal-title":"J. Virol."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1099\/vir.0.18723-0","article-title":"Cleavage of protein prM is necessary for infection of BHK-21 cells by tick-borne encephalitis virus","volume":"84","author":"Elshuber","year":"2003","journal-title":"J. Gen. Virol."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"11813","DOI":"10.1128\/JVI.79.18.11813-11823.2005","article-title":"Resuscitating mutations in a furin cleavage-deficient mutant of the flavivirus tick-borne encephalitis virus","volume":"79","author":"Elshuber","year":"2005","journal-title":"J. Virol."},{"key":"ref_156","doi-asserted-by":"crossref","unstructured":"Zheng, A., Umashankar, M., and Kielian, M. (2010). In Vitro and In vivo studies identify important features of dengue virus pr-E protein interactions. PLoS Pathog., 6.","DOI":"10.1371\/journal.ppat.1001157"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"3877","DOI":"10.1038\/ncomms4877","article-title":"A toggle switch controls the low pH-triggered rearrangement and maturation of the dengue virus envelope proteins","volume":"5","author":"Zheng","year":"2014","journal-title":"Nat. Commun."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"e00055-16","DOI":"10.1128\/MMBR.00055-16","article-title":"The Antigenic structure of Zika virus and its relation to other flaviviruses: implications for infection and immunoprophylaxis","volume":"81","author":"Heinz","year":"2017","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1016\/j.coviro.2017.06.009","article-title":"Flavivirus structural heterogeneity: Implications for cell entry","volume":"24","author":"Rey","year":"2017","journal-title":"Curr. Opin. Virol."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1007\/BF01317484","article-title":"An electron and immunoelectron microscopic study of dengue-2 virus infection of cultured mosquito cells: Maturation events","volume":"92","author":"Hase","year":"1987","journal-title":"Arch. Virol."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"5483","DOI":"10.1128\/AAC.00807-15","article-title":"Nucleoside inhibitors of tick-borne encephalitis virus","volume":"59","author":"Eyer","year":"2015","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"e01028-17","DOI":"10.1128\/JVI.01028-17","article-title":"Escape of tick-borne flavivirus from 2\u2032-C-methylated nucleoside antivirals is mediated by a single conservative mutation in NS5 that has a dramatic effect on viral fitness","volume":"91","author":"Eyer","year":"2017","journal-title":"J. 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