{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T06:43:30Z","timestamp":1790837010997,"version":"4.1.0"},"reference-count":67,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2022,4,11]],"date-time":"2022-04-11T00:00:00Z","timestamp":1649635200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004359","name":"Swedish Research Council","doi-asserted-by":"publisher","award":["315950"],"award-info":[{"award-number":["315950"]}],"id":[{"id":"10.13039\/501100004359","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100006306","name":"Sigrid Jus\u00e9lius Foundation","doi-asserted-by":"publisher","award":["95-7202-38"],"award-info":[{"award-number":["95-7202-38"]}],"id":[{"id":"10.13039\/501100006306","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004012","name":"Jane and Aatos Erkko Foundation","doi-asserted-by":"publisher","award":["-"],"award-info":[{"award-number":["-"]}],"id":[{"id":"10.13039\/501100004012","id-type":"DOI","asserted-by":"publisher"}]},{"name":"European Union\u2019s Horizon 2020 Research and Innovation Programme under the Marie Sk\u0142odowska-Curie grant agreements","award":["765042"],"award-info":[{"award-number":["765042"]}]},{"name":"European Union\u2019s Horizon 2020 Research and Innovation Programme under the Marie Sk\u0142odowska-Curie grant agreements","award":["799929"],"award-info":[{"award-number":["799929"]}]},{"name":"University of Helsinki Research Foundation","award":["-"],"award-info":[{"award-number":["-"]}]},{"name":"Laboratory for Molecular Infection Medicine Sweden (MIMS)","award":["-"],"award-info":[{"award-number":["-"]}]},{"DOI":"10.13039\/501100002341","name":"Academy of Finland","doi-asserted-by":"publisher","award":["315950"],"award-info":[{"award-number":["315950"]}],"id":[{"id":"10.13039\/501100002341","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 pathogenic, enveloped, positive-stranded RNA virus in the family Flaviviridae. Structural studies of flavivirus virions have primarily focused on mosquito-borne species, with only one cryo-electron microscopy (cryo-EM) structure of a tick-borne species published. Here, we present a 3.3 \u00c5 cryo-EM structure of the TBEV virion of the Kuutsalo-14 isolate, confirming the overall organisation of the virus. We observe conformational switching of the peripheral and transmembrane helices of M protein, which can explain the quasi-equivalent packing of the viral proteins and highlights their importance in stabilising membrane protein arrangement in the virion. The residues responsible for M protein interactions are highly conserved in TBEV but not in the structurally studied Hypr strain, nor in mosquito-borne flaviviruses. These interactions may compensate for the lower number of hydrogen bonds between E proteins in TBEV compared to the mosquito-borne flaviviruses. The structure reveals two lipids bound in the E protein which are important for virus assembly. The lipid pockets are comparable to those recently described in mosquito-borne Zika, Spondweni, Dengue, and Usutu viruses. Our results thus advance the understanding of tick-borne flavivirus architecture and virion-stabilising interactions.<\/jats:p>","DOI":"10.3390\/v14040792","type":"journal-article","created":{"date-parts":[[2022,4,12]],"date-time":"2022-04-12T22:48:45Z","timestamp":1649803725000},"page":"792","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":43,"title":["Molecular Organisation of Tick-Borne Encephalitis Virus"],"prefix":"10.3390","volume":"14","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3919-2498","authenticated-orcid":false,"given":"Lauri I. A.","family":"Pulkkinen","sequence":"first","affiliation":[{"name":"Faculty of Biological and Environmental Sciences, Molecular and Integrative Bioscience Research Programme, University of Helsinki, 00014 Helsinki, Finland"},{"name":"Helsinki Institute of Life Sciences-Institute of Biotechnology, University of Helsinki, 00014 Helsinki, Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7319-6268","authenticated-orcid":false,"given":"Sarah V.","family":"Barrass","sequence":"additional","affiliation":[{"name":"Faculty of Biological and Environmental Sciences, Molecular and Integrative Bioscience Research Programme, University of Helsinki, 00014 Helsinki, Finland"},{"name":"Helsinki Institute of Life Sciences-Institute of Biotechnology, University of Helsinki, 00014 Helsinki, Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3772-6003","authenticated-orcid":false,"given":"Au\u0161ra","family":"Domanska","sequence":"additional","affiliation":[{"name":"Faculty of Biological and Environmental Sciences, Molecular and Integrative Bioscience Research Programme, University of Helsinki, 00014 Helsinki, Finland"},{"name":"Helsinki Institute of Life Sciences-Institute of Biotechnology, University of Helsinki, 00014 Helsinki, Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6553-0940","authenticated-orcid":false,"given":"Anna K.","family":"\u00d6verby","sequence":"additional","affiliation":[{"name":"Department of Clinical Microbiology, Faculty of Medicine, Ume\u00e5 University, 90185 Ume\u00e5, Sweden"},{"name":"The Laboratory for Molecular Infection Medicine Sweden (MIMS), Ume\u00e5 University, 90185 Ume\u00e5, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4555-6446","authenticated-orcid":false,"given":"Maria","family":"Anastasina","sequence":"additional","affiliation":[{"name":"Faculty of Biological and Environmental Sciences, Molecular and Integrative Bioscience Research Programme, University of Helsinki, 00014 Helsinki, Finland"},{"name":"Helsinki Institute of Life Sciences-Institute of Biotechnology, University of Helsinki, 00014 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":"Faculty of Biological and Environmental Sciences, Molecular and Integrative Bioscience Research Programme, University of Helsinki, 00014 Helsinki, Finland"},{"name":"Helsinki Institute of Life Sciences-Institute of Biotechnology, University of Helsinki, 00014 Helsinki, Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,4,11]]},"reference":[{"key":"ref_1","unstructured":"Knipe, D., and Howley, P. (2013). Flaviviridae. Fields Virology, Lippincott Williams & Wilkins."},{"key":"ref_2","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_3","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.antiviral.2019.01.014","article-title":"Tick-borne encephalitis in Europe and Russia: Review of pathogenesis, clinical features, therapy, and vaccines","volume":"164","author":"Ruzek","year":"2019","journal-title":"Antivir. Res."},{"key":"ref_4","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_5","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/0042-6822(89)90044-5","article-title":"Epitope model of tick-borne encephalitis virus envelope glycoprotein E: Analysis of structural properties, role of carbohydrate side chain, and conformational changes occurring at acidic pH","volume":"169","author":"Guirakhoo","year":"1989","journal-title":"Virology"},{"key":"ref_6","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. F\u00fcr Bakteriol."},{"key":"ref_7","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":"Biochem"},{"key":"ref_8","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_9","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_10","doi-asserted-by":"crossref","unstructured":"Barrass, S.V., Pulkkinen, L.I.A., Vapalahti, O., Kuivanen, S., Anastasina, M., Happonen, L., and Butcher, S.J. Proteome-wide cross-linking mass spectrometry to identify specific virus capsid-host interactions between tick-borne encephalitis virus and neuroblastoma cells. BioRxiv, 2021.","DOI":"10.1101\/2021.10.29.464531"},{"key":"ref_11","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_12","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_13","doi-asserted-by":"crossref","first-page":"7888","DOI":"10.1126\/scitranslmed.aax7888","article-title":"A recombinant platform for flavivirus vaccines and diagnostics using chimeras of a new insect-specific virus","volume":"11","author":"Harrison","year":"2019","journal-title":"Sci. Transl. Med."},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Pulkkinen, L.I.A., Butcher, S., and Anastasina, M. (2018). Tick-borne encephalitis virus: A Structural View. Viruses, 10.","DOI":"10.3390\/v10070350"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"4507","DOI":"10.1126\/sciadv.abe4507","article-title":"The structure of an infectious immature flavivirus redefines viral architecture and maturation","volume":"7","author":"Newton","year":"2021","journal-title":"Sci. Adv."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-020-18747-4","article-title":"Identification of a pocket factor that is critical to Zika virus assembly","volume":"11","author":"DiNunno","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"3266","DOI":"10.1038\/s41467-021-22773-1","article-title":"A unified route for flavivirus structures uncovers essential pocket factors conserved across pathogenic viruses","volume":"12","author":"Hardy","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_18","first-page":"118","article-title":"Structure of Usutu virus SAAR-1776 displays fusion loop asymmetry","volume":"9","author":"Khare","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-021-21505-9","article-title":"Flavivirus maturation leads to the formation of an occupied lipid pocket in the surface glycoproteins","volume":"12","author":"Renner","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"946","DOI":"10.3201\/eid2405.171986","article-title":"Fatal tick-borne encephalitis virus infections caused by Siberian and European subtypes, Finland, 2015","volume":"24","author":"Kuivanen","year":"2018","journal-title":"Emerg. Infect. Dis."},{"key":"ref_21","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_22","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/0168-1702(96)01325-1","article-title":"Characterization of Langat virus antigenic determinants defined by monoclonal antibodies to E, NS1 and preM and identification of a protective, non-neutralizing preM-specific monoclonal antibody","volume":"43","author":"Smith","year":"1996","journal-title":"Virus Res."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1016\/j.bioorg.2019.03.028","article-title":"Tick-borne flavivirus reproduction inhibitors based on isoxazole core linked with adamantane","volume":"87","author":"Vasilenko","year":"2019","journal-title":"Bioorg. Chem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.jsb.2016.04.010","article-title":"Scipion: A software framework toward integration, reproducibility and validation in 3D electron microscopy","volume":"195","author":"Quintana","year":"2016","journal-title":"J. Struct. Biol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"e42166","DOI":"10.7554\/eLife.42166","article-title":"New tools for automated high-resolution cryo-EM structure determination in RELION-3","volume":"7","author":"Zivanov","year":"2018","journal-title":"Elife"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1016\/j.jsb.2013.09.015","article-title":"Xmipp 3.0: An improved software suite for image processing in electron microscopy","volume":"184","author":"Marabini","year":"2013","journal-title":"J. Struct. Biol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1007\/978-1-62703-137-0_11","article-title":"Semiautomatic, high-throughput, high-resolution protocol for three-dimensional reconstruction of single particles in electron microscopy","volume":"950","author":"Sorzano","year":"2013","journal-title":"Methods Mol. Biol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1016\/j.jsb.2015.08.008","article-title":"CTFFIND4: Fast and accurate defocus estimation from electron micrographs","volume":"192","author":"Rohou","year":"2015","journal-title":"J. Struct. Biol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1016\/j.str.2017.12.018","article-title":"MonoRes: Automatic and accurate estimation of local resolution for electron microscopy maps","volume":"26","author":"Vilas","year":"2018","journal-title":"Structure"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1093\/bioinformatics\/btz671","article-title":"Automatic local resolution-based sharpening of cryo-EM maps","volume":"36","author":"Vilas","year":"2020","journal-title":"Bioinformatics"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of Coot","volume":"D66","author":"Emsley","year":"2010","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1002\/pro.3235","article-title":"UCSF ChimeraX: Meeting modern challenges in visualization and analysis","volume":"27","author":"Goddard","year":"2018","journal-title":"Protein Sci."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1002\/pro.3943","article-title":"UCSF ChimeraX: Structure visualization for researchers, educators, and developers","volume":"30","author":"Pettersen","year":"2021","journal-title":"Protein Sci."},{"key":"ref_34","first-page":"861","article-title":"Macromolecular structure determination using X-rays, neutrons and electrons: Recent developments in Phenix","volume":"75","author":"Liebschner","year":"2019","journal-title":"Acta Cryst."},{"key":"ref_35","first-page":"519","article-title":"ISOLDE: A physically realistic environment for model building into low-resolution electron-density maps","volume":"74","author":"Croll","year":"2018","journal-title":"Res. Pap. Acta Cryst."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1002\/pro.3330","article-title":"MolProbity: More and better reference data for improved all-atom structure validation","volume":"27","author":"Williams","year":"2018","journal-title":"Protein Sci."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1016\/j.jmb.2007.05.022","article-title":"Inference of macromolecular assemblies from crystalline state","volume":"372","author":"Krissinel","year":"2007","journal-title":"J. Mol. Biol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"2295","DOI":"10.1093\/nar\/gkn072","article-title":"V PROMALS3D: A tool for multiple protein sequence and structure alignments","volume":"36","author":"Pei","year":"2008","journal-title":"Nucleic Acids Res."},{"key":"ref_39","first-page":"2983","article-title":"Pre-calculated protein structure alignments at the RCSB PDB website","volume":"26","author":"Bliven","year":"2010","journal-title":"Bioinforma. Appl. Note"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1188","DOI":"10.1101\/gr.849004","article-title":"WebLogo: A sequence logo generator","volume":"14","author":"Crooks","year":"2004","journal-title":"Genome Res."},{"key":"ref_41","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_42","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1038\/nature17994","article-title":"Structure of the thermally stable Zika virus","volume":"533","author":"Kostyuchenko","year":"2016","journal-title":"Nature"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"6067","DOI":"10.1016\/j.cell.2021.11.009","article-title":"Human antibody C10 neutralizes by diminishing Zika but enhancing dengue virus dynamics","volume":"184","author":"Lim","year":"2021","journal-title":"Cell"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1169","DOI":"10.1016\/j.str.2018.05.006","article-title":"Refinement and analysis of the mature Zika virus cryo-EM structure at 3.1 \u00c5 resolution","volume":"26","author":"Sevvana","year":"2018","journal-title":"Structure"},{"key":"ref_45","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_46","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_47","doi-asserted-by":"crossref","first-page":"12041","DOI":"10.1128\/JVI.02061-14","article-title":"The composition of West Nile virus lipid envelope unveils a role of sphingolipid metabolism in flavivirus biogenesis","volume":"88","author":"Casas","year":"2014","journal-title":"J. Virol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"1504S","DOI":"10.1093\/jn\/137.6.1504S","article-title":"Cation-p interactions involving aromatic amino acids","volume":"137","author":"Dougherty","year":"2007","journal-title":"J. Nutr."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/0042-6822(88)90161-4","article-title":"Sequence of the structural proteins of tick-borne encephalitis virus (Western subtype) and comparative analysis with other flaviviruses","volume":"166","author":"Mandl","year":"1988","journal-title":"Virology"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"13204","DOI":"10.1038\/s41598-020-70082-2","article-title":"comprehensive N-glycosylation mapping of envelope glycoprotein from tick-borne encephalitis virus grown in human and tick cells","volume":"10","author":"Grubhoffer","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1006\/jmbi.1994.1022","article-title":"Planar stacking interactions of arginine and aromatic side-chains in proteins","volume":"235","author":"Flocco","year":"1994","journal-title":"J. Mol. Biol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"2655","DOI":"10.1039\/C7SC04905F","article-title":"Cation-\u03c0 interactions in protein-ligand binding: Theory and data-mining reveal different roles for lysine and arginine","volume":"9","author":"Duarte","year":"2018","journal-title":"Chem. Sci."},{"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":"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_56","doi-asserted-by":"crossref","first-page":"1065","DOI":"10.1242\/jcs.114454","article-title":"Membrane curvature at a glance","volume":"128","author":"Mcmahon","year":"2015","journal-title":"J. Cell Sci."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"2250","DOI":"10.1016\/j.bbamem.2014.05.013","article-title":"The role of spontaneous lipid curvature in the interaction of interfacially active peptides with membranes","volume":"1838","author":"Koller","year":"2014","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1038\/42408","article-title":"Functional rafts in cell membranes","volume":"387","author":"Simons","year":"1997","journal-title":"Nature"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"1819","DOI":"10.1016\/j.str.2005.08.020","article-title":"Membrane proteins modulate the bilayer curvature in the bacterial virus Bam35","volume":"13","author":"Huiskonen","year":"2005","journal-title":"Structure"},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Medits, I., Heinz, F.X., and Stiasny, K. (2021). An absolutely conserved tryptophan in the stem of the envelope protein E of flaviviruses is essential for the formation of stable particles. Viruses, 13.","DOI":"10.3390\/v13091727"},{"key":"ref_61","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_62","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_63","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1016\/j.bbrc.2017.01.022","article-title":"Role of N-glycosylation on Zika virus E protein secretion, viral assembly and infectivity","volume":"492","author":"Mossenta","year":"2017","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_64","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_65","doi-asserted-by":"crossref","first-page":"13262","DOI":"10.1128\/JVI.79.21.13262-13274.2005","article-title":"N-linked glycosylation of West Nile virus envelope proteins influences particle assembly and infectivity","volume":"79","author":"Hanna","year":"2005","journal-title":"J. Virol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"8339","DOI":"10.1128\/JVI.79.13.8339-8347.2005","article-title":"Envelope protein glycosylation status influences mouse neuroinvasion phenotype of genetic lineage 1 West Nile virus strains","volume":"79","author":"Beasley","year":"2005","journal-title":"J. Virol."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"e01348-17","DOI":"10.1128\/JVI.01348-17","article-title":"Zika virus encoding nonglycosylated envelope protein is attenuated and defective in neuroinvasion","volume":"91","author":"Annamalai","year":"2017","journal-title":"J. Virol."}],"container-title":["Viruses"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1999-4915\/14\/4\/792\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T22:52:04Z","timestamp":1760136724000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1999-4915\/14\/4\/792"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,4,11]]},"references-count":67,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2022,4]]}},"alternative-id":["v14040792"],"URL":"https:\/\/doi.org\/10.3390\/v14040792","relation":{"has-preprint":[{"id-type":"doi","id":"10.20944\/preprints202204.0001.v1","asserted-by":"object"}]},"ISSN":["1999-4915"],"issn-type":[{"value":"1999-4915","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,4,11]]}}}