{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T21:44:49Z","timestamp":1792791889454,"version":"4.5.0"},"reference-count":65,"publisher":"National Academy of Sciences","issue":"5","license":[{"start":{"date-parts":[[2019,7,14]],"date-time":"2019-07-14T00:00:00Z","timestamp":1563062400000},"content-version":"vor","delay-in-days":181,"URL":"https:\/\/www.pnas.org\/site\/aboutpnas\/licenses.xhtml"}],"funder":[{"DOI":"10.13039\/100000002","name":"HHS | National Institutes of Health","doi-asserted-by":"publisher","award":["AI076331"],"award-info":[{"award-number":["AI076331"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"HHS | National Institutes of Health","doi-asserted-by":"publisher","award":["AI127828"],"award-info":[{"award-number":["AI127828"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"HHS | National Institutes of Health","doi-asserted-by":"publisher","award":["AI073755"],"award-info":[{"award-number":["AI073755"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"HHS | National Institutes of Health","doi-asserted-by":"publisher","award":["AI104972"],"award-info":[{"award-number":["AI104972"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"name":"National Institute of Allergy and Infectious Diseases Contract","award":["HHSN272201400024C"],"award-info":[{"award-number":["HHSN272201400024C"]}],"id":[{"id":"https:\/\/ror.org\/043z4tv69","id-type":"ROR","asserted-by":"crossref"}]},{"name":"National Institute of Allergy and Infectious Diseases Contract","award":["HHSN272201400058C"],"award-info":[{"award-number":["HHSN272201400058C"]}],"id":[{"id":"https:\/\/ror.org\/043z4tv69","id-type":"ROR","asserted-by":"crossref"}]}],"content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2019,1,29]]},"abstract":"<jats:p>\n                    Zika virus (ZIKV) is a major human pathogen and member of the\n                    <jats:italic>Flavivirus<\/jats:italic>\n                    genus in the Flaviviridae family. In contrast to most other insect-transmitted flaviviruses, ZIKV also can be transmitted sexually and from mother to fetus in humans. During recent outbreaks, ZIKV infections have been linked to microcephaly, congenital disease, and Guillain-Barr\u00e9 syndrome. Neutralizing antibodies have potential as therapeutic agents. We report here a 4-\u00c5-resolution cryo-electron microscopy structure of the ZIKV virion in complex with Fab fragments of the potently neutralizing human monoclonal antibody ZIKV-195. The footprint of the ZIKV-195 Fab fragment expands across two adjacent envelope (E) protein protomers. ZIKV neutralization by this antibody is presumably accomplished by cross-linking the E proteins, which likely prevents formation of E protein trimers required for fusion of the viral and cellular membranes. A single dose of ZIKV-195 administered 5 days after virus inoculation showed marked protection against lethality in a stringent mouse model of infection.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1815432116","type":"journal-article","created":{"date-parts":[[2019,1,14]],"date-time":"2019-01-14T20:59:37Z","timestamp":1547499577000},"page":"1591-1596","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":58,"title":["Structural basis of a potent human monoclonal antibody against Zika virus targeting a quaternary epitope"],"prefix":"10.1073","volume":"116","author":[{"given":"Feng","family":"Long","sequence":"first","affiliation":[{"name":"Department of Biological Sciences, Purdue University, West Lafayette, IN 47907;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael","family":"Doyle","sequence":"additional","affiliation":[{"name":"Department of Pathology, Microbiology and Immunology, Vanderbilt University, Nashville, TN 37232;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Estefania","family":"Fernandez","sequence":"additional","affiliation":[{"name":"Department of Medicine, Washington University School of Medicine, St. Louis, MO 63110;"},{"name":"Department of Pathology &amp; Immunology, Washington University School of Medicine, St. Louis, MO 63110;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrew S.","family":"Miller","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Purdue University, West Lafayette, IN 47907;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2150-9792","authenticated-orcid":false,"given":"Thomas","family":"Klose","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Purdue University, West Lafayette, IN 47907;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Madhumati","family":"Sevvana","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Purdue University, West Lafayette, IN 47907;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aubrey","family":"Bryan","sequence":"additional","affiliation":[{"name":"Integral Molecular Inc., Philadelphia, PA 19104;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Edgar","family":"Davidson","sequence":"additional","affiliation":[{"name":"Integral Molecular Inc., Philadelphia, PA 19104;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Benjamin J.","family":"Doranz","sequence":"additional","affiliation":[{"name":"Integral Molecular Inc., Philadelphia, PA 19104;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4148-1026","authenticated-orcid":false,"given":"Richard J.","family":"Kuhn","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Purdue University, West Lafayette, IN 47907;"},{"name":"Purdue Institute for Inflammation, Immunology and Infectious Disease, Purdue University, West Lafayette, IN 47907;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael S.","family":"Diamond","sequence":"additional","affiliation":[{"name":"Department of Medicine, Washington University School of Medicine, St. Louis, MO 63110;"},{"name":"Department of Pathology &amp; Immunology, Washington University School of Medicine, St. Louis, MO 63110;"},{"name":"Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO 63110;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0049-1079","authenticated-orcid":false,"suffix":"Jr.","given":"James E.","family":"Crowe","sequence":"additional","affiliation":[{"name":"Department of Pathology, Microbiology and Immunology, Vanderbilt University, Nashville, TN 37232;"},{"name":"Department of Pediatrics, Vanderbilt University Medical Center, Nashville, TN 37232;"},{"name":"The Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN 37232"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael G.","family":"Rossmann","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Purdue University, West Lafayette, IN 47907;"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2019,1,14]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1099\/jgv.0.000672","article-title":"ICTV virus taxonomy profile: Flaviviridae","volume":"98","author":"Simmonds P","year":"2017","unstructured":"P Simmonds, , ICTV virus taxonomy profile: Flaviviridae. J Gen Virol; Ictv Report Consortium 98, 2\u20133 (2017).","journal-title":"J Gen Virol"},{"key":"e_1_3_4_2_2","doi-asserted-by":"crossref","first-page":"S875","DOI":"10.1093\/infdis\/jix396","article-title":"Modes of transmission of Zika virus","volume":"216","author":"Gregory CJ","year":"2017","unstructured":"CJ Gregory, , Modes of transmission of Zika virus. J Infect Dis 216, S875\u2013S883 (2017).","journal-title":"J Infect Dis"},{"key":"e_1_3_4_3_2","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1016\/S0140-6736(16)00257-9","article-title":"Concern over Zika virus grips the world","volume":"387","author":"Samarasekera U","year":"2016","unstructured":"U Samarasekera, M Triunfol, Concern over Zika virus grips the world. Lancet 387, 521\u2013524 (2016).","journal-title":"Lancet"},{"key":"e_1_3_4_4_2","unstructured":"Available at https:\/\/wwwnc.cdc.gov\/travel\/page\/zika-travel-information."},{"key":"e_1_3_4_5_2","doi-asserted-by":"crossref","first-page":"1531","DOI":"10.1016\/S0140-6736(16)00562-6","article-title":"Guillain-Barr\u00e9 syndrome outbreak associated with Zika virus infection in French Polynesia: A case-control study","volume":"387","author":"Cao-Lormeau VM","year":"2016","unstructured":"VM Cao-Lormeau, , Guillain-Barr\u00e9 syndrome outbreak associated with Zika virus infection in French Polynesia: A case-control study. Lancet 387, 1531\u20131539 (2016).","journal-title":"Lancet"},{"key":"e_1_3_4_6_2","doi-asserted-by":"crossref","first-page":"951","DOI":"10.1056\/NEJMoa1600651","article-title":"Zika virus associated with microcephaly","volume":"374","author":"Mlakar J","year":"2016","unstructured":"J Mlakar, , Zika virus associated with microcephaly. N Engl J Med 374, 951\u2013958 (2016).","journal-title":"N Engl J Med"},{"key":"e_1_3_4_7_2","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 D","year":"2016","unstructured":"D Sirohi, , The 3.8 \u00c5 resolution cryo-EM structure of Zika virus. Science 352, 467\u2013470 (2016).","journal-title":"Science"},{"key":"e_1_3_4_8_2","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 X","year":"2017","unstructured":"X Wang, , Near-atomic structure of Japanese encephalitis virus reveals critical determinants of virulence and stability. Nat Commun 8, 14 (2017).","journal-title":"Nat Commun"},{"key":"e_1_3_4_9_2","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1038\/nature17994","article-title":"Structure of the thermally stable Zika virus","volume":"533","author":"Kostyuchenko VA","year":"2016","unstructured":"VA Kostyuchenko, , Structure of the thermally stable Zika virus. Nature 533, 425\u2013428 (2016).","journal-title":"Nature"},{"key":"e_1_3_4_10_2","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 X","year":"2013","unstructured":"X Zhang, , Cryo-EM structure of the mature dengue virus at 3.5-\u00c5 resolution. Nat Struct Mol Biol 20, 105\u2013110 (2013).","journal-title":"Nat Struct Mol Biol"},{"key":"e_1_3_4_11_2","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":"F\u00fczik T","year":"2018","unstructured":"T F\u00fczik, , Structure of tick-borne encephalitis virus and its neutralization by a monoclonal antibody. Nat Commun 9, 436 (2018).","journal-title":"Nat Commun"},{"key":"e_1_3_4_12_2","doi-asserted-by":"crossref","first-page":"6795","DOI":"10.1073\/pnas.1304300110","article-title":"Dengue structure differs at the temperatures of its human and mosquito hosts","volume":"110","author":"Zhang X","year":"2013","unstructured":"X Zhang, , Dengue structure differs at the temperatures of its human and mosquito hosts. Proc Natl Acad Sci USA 110, 6795\u20136799 (2013).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_13_2","doi-asserted-by":"crossref","first-page":"7585","DOI":"10.1128\/JVI.00757-13","article-title":"Structural changes in dengue virus when exposed to a temperature of 37 \u00b0C","volume":"87","author":"Fibriansah G","year":"2013","unstructured":"G Fibriansah, , Structural changes in dengue virus when exposed to a temperature of 37 \u00b0C. J Virol 87, 7585\u20137592 (2013).","journal-title":"J Virol"},{"key":"e_1_3_4_14_2","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1038\/375291a0","article-title":"The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution","volume":"375","author":"Rey FA","year":"1995","unstructured":"FA Rey, FX Heinz, C Mandl, C Kunz, SC Harrison, The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution. Nature 375, 291\u2013298 (1995).","journal-title":"Nature"},{"key":"e_1_3_4_15_2","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 RJ","year":"2002","unstructured":"RJ Kuhn, , Structure of dengue virus: Implications for flavivirus organization, maturation, and fusion. Cell 108, 717\u2013725 (2002).","journal-title":"Cell"},{"key":"e_1_3_4_16_2","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 L","year":"2008","unstructured":"L Li, , The flavivirus precursor membrane-envelope protein complex: Structure and maturation. Science 319, 1830\u20131834 (2008).","journal-title":"Science"},{"key":"e_1_3_4_17_2","doi-asserted-by":"crossref","first-page":"S935","DOI":"10.1093\/infdis\/jix515","article-title":"Zika virus structure, maturation, and receptors","volume":"216","author":"Sirohi D","year":"2017","unstructured":"D Sirohi, RJ Kuhn, Zika virus structure, maturation, and receptors. J Infect Dis 216, S935\u2013S944 (2017).","journal-title":"J Infect Dis"},{"key":"e_1_3_4_18_2","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 Y","year":"2004","unstructured":"Y Zhang, , Conformational changes of the flavivirus E glycoprotein. Structure 12, 1607\u20131618 (2004).","journal-title":"Structure"},{"key":"e_1_3_4_19_2","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 VM","year":"2017","unstructured":"VM Prasad, , Structure of the immature Zika virus at 9 \u00c5 resolution. Nat Struct Mol Biol 24, 184\u2013186 (2017).","journal-title":"Nat Struct Mol Biol"},{"key":"e_1_3_4_20_2","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 IM","year":"2008","unstructured":"IM Yu, , Structure of the immature dengue virus at low pH primes proteolytic maturation. Science 319, 1834\u20131837 (2008).","journal-title":"Science"},{"key":"e_1_3_4_21_2","doi-asserted-by":"crossref","first-page":"369ra179","DOI":"10.1126\/scitranslmed.aai8336","article-title":"Molecular determinants of human neutralizing antibodies isolated from a patient infected with Zika virus","volume":"8","author":"Wang Q","year":"2016","unstructured":"Q Wang, , Molecular determinants of human neutralizing antibodies isolated from a patient infected with Zika virus. Sci Transl Med 8, 369ra179 (2016).","journal-title":"Sci Transl Med"},{"key":"e_1_3_4_22_2","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1038\/nature20564","article-title":"Neutralizing human antibodies prevent Zika virus replication and fetal disease in mice","volume":"540","author":"Sapparapu G","year":"2016","unstructured":"G Sapparapu, , Neutralizing human antibodies prevent Zika virus replication and fetal disease in mice. Nature 540, 443\u2013447 (2016).","journal-title":"Nature"},{"key":"e_1_3_4_23_2","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1126\/science.aaf8505","article-title":"Specificity, cross-reactivity, and function of antibodies elicited by Zika virus infection","volume":"353","author":"Stettler K","year":"2016","unstructured":"K Stettler, , Specificity, cross-reactivity, and function of antibodies elicited by Zika virus infection. Science 353, 823\u2013826 (2016).","journal-title":"Science"},{"key":"e_1_3_4_24_2","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1016\/j.cell.2017.04.024","article-title":"Recurrent potent human neutralizing antibodies to Zika virus in Brazil and Mexico","volume":"169","author":"Robbiani DF","year":"2017","unstructured":"DF Robbiani, , Recurrent potent human neutralizing antibodies to Zika virus in Brazil and Mexico. Cell 169, 597\u2013609.e11 (2017).","journal-title":"Cell"},{"key":"e_1_3_4_25_2","doi-asserted-by":"crossref","first-page":"eaan8184","DOI":"10.1126\/scitranslmed.aan8184","article-title":"Neutralizing human monoclonal antibodies prevent Zika virus infection in macaques","volume":"9","author":"Magnani DM","year":"2017","unstructured":"DM Magnani, , Neutralizing human monoclonal antibodies prevent Zika virus infection in macaques. Sci Transl Med 9, eaan8184 (2017).","journal-title":"Sci Transl Med"},{"key":"e_1_3_4_26_2","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/j.cell.2017.09.002","article-title":"A human bi-specific antibody against Zika virus with high therapeutic potential","volume":"171","author":"Wang J","year":"2017","unstructured":"J Wang, , A human bi-specific antibody against Zika virus with high therapeutic potential. Cell 171, 229\u2013241.e15 (2017).","journal-title":"Cell"},{"key":"e_1_3_4_27_2","doi-asserted-by":"crossref","first-page":"e01123-16","DOI":"10.1128\/mBio.01123-16","article-title":"Dengue virus envelope dimer epitope monoclonal antibodies isolated from dengue patients are protective against Zika virus","volume":"7","author":"Swanstrom JA","year":"2016","unstructured":"JA Swanstrom, , Dengue virus envelope dimer epitope monoclonal antibodies isolated from dengue patients are protective against Zika virus. MBio 7, e01123-16 (2016).","journal-title":"MBio"},{"key":"e_1_3_4_28_2","doi-asserted-by":"crossref","first-page":"7852","DOI":"10.1073\/pnas.1607931113","article-title":"Human antibody responses after dengue virus infection are highly cross-reactive to Zika virus","volume":"113","author":"Priyamvada L","year":"2016","unstructured":"L Priyamvada, , Human antibody responses after dengue virus infection are highly cross-reactive to Zika virus. Proc Natl Acad Sci USA 113, 7852\u20137857 (2016).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_29_2","doi-asserted-by":"crossref","first-page":"696","DOI":"10.1016\/j.chom.2016.04.013","article-title":"Structures of the Zika virus envelope protein and its complex with a flavivirus broadly protective antibody","volume":"19","author":"Dai L","year":"2016","unstructured":"L Dai, , Structures of the Zika virus envelope protein and its complex with a flavivirus broadly protective antibody. Cell Host Microbe 19, 696\u2013704 (2016).","journal-title":"Cell Host Microbe"},{"key":"e_1_3_4_30_2","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1038\/nature18938","article-title":"Structural basis of potent Zika-dengue virus antibody cross-neutralization","volume":"536","author":"Barba-Spaeth G","year":"2016","unstructured":"G Barba-Spaeth, , Structural basis of potent Zika-dengue virus antibody cross-neutralization. Nature 536, 48\u201353 (2016).","journal-title":"Nature"},{"key":"e_1_3_4_31_2","doi-asserted-by":"crossref","first-page":"1261","DOI":"10.1038\/ni.3849","article-title":"Human antibodies to the dengue virus E-dimer epitope have therapeutic activity against Zika virus infection","volume":"18","author":"Fernandez E","year":"2017","unstructured":"E Fernandez, , Human antibodies to the dengue virus E-dimer epitope have therapeutic activity against Zika virus infection. Nat Immunol 18, 1261\u20131269 (2017).","journal-title":"Nat Immunol"},{"key":"e_1_3_4_32_2","doi-asserted-by":"crossref","first-page":"13679","DOI":"10.1038\/ncomms13679","article-title":"Neutralization mechanism of a highly potent antibody against Zika virus","volume":"7","author":"Zhang S","year":"2016","unstructured":"S Zhang, , Neutralization mechanism of a highly potent antibody against Zika virus. Nat Commun 7, 13679 (2016).","journal-title":"Nat Commun"},{"key":"e_1_3_4_33_2","doi-asserted-by":"crossref","first-page":"1016","DOI":"10.1016\/j.cell.2016.07.020","article-title":"Structural basis of Zika virus-specific antibody protection","volume":"166","author":"Zhao H","year":"2016","unstructured":"H Zhao, , Structural basis of Zika virus-specific antibody protection. Cell 166, 1016\u20131027 (2016).","journal-title":"Cell"},{"key":"e_1_3_4_34_2","doi-asserted-by":"crossref","first-page":"14722","DOI":"10.1038\/ncomms14722","article-title":"A human antibody against Zika virus crosslinks the E protein to prevent infection","volume":"8","author":"Hasan SS","year":"2017","unstructured":"SS Hasan, , A human antibody against Zika virus crosslinks the E protein to prevent infection. Nat Commun 8, 14722 (2017).","journal-title":"Nat Commun"},{"key":"e_1_3_4_35_2","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 M","year":"2018","unstructured":"M Sevvana, , Refinement and analysis of the mature Zika virus cryo-EM structure at 3.1 \u00c5 resolution. Structure 26, 1169\u20131177.e3 (2018).","journal-title":"Structure"},{"key":"e_1_3_4_36_2","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1006\/jsbi.2002.4435","article-title":"Combining electron microscopic with x-ray crystallographic structures","volume":"136","author":"Rossmann MG","year":"2001","unstructured":"MG Rossmann, R Bernal, SV Pletnev, Combining electron microscopic with x-ray crystallographic structures. J Struct Biol 136, 190\u2013200 (2001).","journal-title":"J Struct Biol"},{"key":"e_1_3_4_37_2","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1111\/imm.12323","article-title":"A high-throughput shotgun mutagenesis approach to mapping B-cell antibody epitopes","volume":"143","author":"Davidson E","year":"2014","unstructured":"E Davidson, BJ Doranz, A high-throughput shotgun mutagenesis approach to mapping B-cell antibody epitopes. Immunology 143, 13\u201320 (2014).","journal-title":"Immunology"},{"key":"e_1_3_4_38_2","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1038\/nrmicro1067","article-title":"A structural perspective of the flavivirus life cycle","volume":"3","author":"Mukhopadhyay S","year":"2005","unstructured":"S Mukhopadhyay, RJ Kuhn, MG Rossmann, A structural perspective of the flavivirus life cycle. Nat Rev Microbiol 3, 13\u201322 (2005).","journal-title":"Nat Rev Microbiol"},{"key":"e_1_3_4_39_2","doi-asserted-by":"crossref","first-page":"e01348-17","DOI":"10.1128\/JVI.01348-17","article-title":"Zika virus encoding non-glycosylated envelope protein is attenuated and defective in neuroinvasion","volume":"91","author":"Annamalai AS","year":"2017","unstructured":"AS Annamalai, , Zika virus encoding non-glycosylated envelope protein is attenuated and defective in neuroinvasion. J Virol 91, e01348-17 (2017).","journal-title":"J Virol"},{"key":"e_1_3_4_40_2","doi-asserted-by":"crossref","first-page":"1180","DOI":"10.1016\/j.celrep.2017.10.016","article-title":"Functional analysis of glycosylation of Zika virus envelope protein","volume":"21","author":"Fontes-Garfias CR","year":"2017","unstructured":"CR Fontes-Garfias, , Functional analysis of glycosylation of Zika virus envelope protein. Cell Rep 21, 1180\u20131190 (2017).","journal-title":"Cell Rep"},{"key":"e_1_3_4_41_2","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 E","year":"2006","unstructured":"E Pokidysheva, , Cryo-EM reconstruction of dengue virus in complex with the carbohydrate recognition domain of DC-SIGN. Cell 124, 485\u2013493 (2006).","journal-title":"Cell"},{"key":"e_1_3_4_42_2","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 DWC","year":"2005","unstructured":"DWC Beasley, , Envelope protein glycosylation status influences mouse neuroinvasion phenotype of genetic lineage 1 West Nile virus strains. J Virol 79, 8339\u20138347 (2005).","journal-title":"J Virol"},{"key":"e_1_3_4_43_2","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1016\/S0065-3527(03)60011-4","article-title":"Neutralization and antibody-dependent enhancement of dengue viruses","volume":"60","author":"Halstead SB","year":"2003","unstructured":"SB Halstead, Neutralization and antibody-dependent enhancement of dengue viruses. Adv Virus Res 60, 421\u2013467 (2003).","journal-title":"Adv Virus Res"},{"key":"e_1_3_4_44_2","doi-asserted-by":"crossref","first-page":"1102","DOI":"10.1038\/ni.3515","article-title":"Dengue virus sero-cross-reactivity drives antibody-dependent enhancement of infection with zika virus","volume":"17","author":"Dejnirattisai W","year":"2016","unstructured":"W Dejnirattisai, , Dengue virus sero-cross-reactivity drives antibody-dependent enhancement of infection with zika virus. Nat Immunol 17, 1102\u20131108 (2016).","journal-title":"Nat Immunol"},{"key":"e_1_3_4_45_2","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/j.chom.2007.03.002","article-title":"The stoichiometry of antibody-mediated neutralization and enhancement of West Nile virus infection","volume":"1","author":"Pierson TC","year":"2007","unstructured":"TC Pierson, , The stoichiometry of antibody-mediated neutralization and enhancement of West Nile virus infection. Cell Host Microbe 1, 135\u2013145 (2007).","journal-title":"Cell Host Microbe"},{"key":"e_1_3_4_46_2","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1016\/j.chom.2018.04.003","article-title":"An immunocompetent mouse model of Zika virus infection","volume":"23","author":"Gorman MJ","year":"2018","unstructured":"MJ Gorman, , An immunocompetent mouse model of Zika virus infection. Cell Host Microbe 23, 672\u2013685.e6 (2018).","journal-title":"Cell Host Microbe"},{"key":"e_1_3_4_47_2","doi-asserted-by":"crossref","first-page":"15D.3.1","DOI":"10.1002\/9780471729259.mc15d03s31","article-title":"Propagation, quantification, detection, and storage of West Nile virus","volume":"31","author":"Brien JD","year":"2013","unstructured":"JD Brien, HM Lazear, MS Diamond, Propagation, quantification, detection, and storage of West Nile virus. Curr Protoc Microbiol 31, 15D.3.1\u201315D.3.18 (2013).","journal-title":"Curr Protoc Microbiol"},{"key":"e_1_3_4_48_2","volume-title":"Guide for the Care and Use of Laboratory Animals","author":"National Research Council","year":"2011","unstructured":"; National Research Council Guide for the Care and Use of Laboratory Animals (National Academies Press, 8th Ed, Washington, DC, 2011).","edition":"8"},{"key":"e_1_3_4_49_2","doi-asserted-by":"crossref","first-page":"e1003312","DOI":"10.1371\/journal.ppat.1003312","article-title":"Development of a highly protective combination monoclonal antibody therapy against Chikungunya virus","volume":"9","author":"Pal P","year":"2013","unstructured":"P Pal, , Development of a highly protective combination monoclonal antibody therapy against Chikungunya virus. PLoS Pathog 9, e1003312 (2013).","journal-title":"PLoS Pathog"},{"key":"e_1_3_4_50_2","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.jsb.2005.03.010","article-title":"Automated molecular microscopy: The new Leginon system","volume":"151","author":"Suloway C","year":"2005","unstructured":"C Suloway, , Automated molecular microscopy: The new Leginon system. J Struct Biol 151, 41\u201360 (2005).","journal-title":"J Struct Biol"},{"key":"e_1_3_4_51_2","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1038\/nmeth.4193","article-title":"MotionCor2: Anisotropic correction of beam-induced motion for improved cryo-electron microscopy","volume":"14","author":"Zheng SQ","year":"2017","unstructured":"SQ Zheng, , MotionCor2: Anisotropic correction of beam-induced motion for improved cryo-electron microscopy. Nat Methods 14, 331\u2013332 (2017).","journal-title":"Nat Methods"},{"key":"e_1_3_4_52_2","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 A","year":"2015","unstructured":"A Rohou, N Grigorieff, CTFFIND4: Fast and accurate defocus estimation from electron micrographs. J Struct Biol 192, 216\u2013221 (2015).","journal-title":"J Struct Biol"},{"key":"e_1_3_4_53_2","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/j.jsb.2009.01.002","article-title":"Appion: An integrated, database-driven pipeline to facilitate EM image processing","volume":"166","author":"Lander GC","year":"2009","unstructured":"GC Lander, , Appion: An integrated, database-driven pipeline to facilitate EM image processing. J Struct Biol 166, 95\u2013102 (2009).","journal-title":"J Struct Biol"},{"key":"e_1_3_4_54_2","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1016\/j.jsb.2012.09.006","article-title":"RELION: Implementation of a Bayesian approach to cryo-EM structure determination","volume":"180","author":"Scheres SH","year":"2012","unstructured":"SH Scheres, RELION: Implementation of a Bayesian approach to cryo-EM structure determination. J Struct Biol 180, 519\u2013530 (2012).","journal-title":"J Struct Biol"},{"key":"e_1_3_4_55_2","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/j.jsb.2016.06.003","article-title":"An algorithm for estimation and correction of anisotropic magnification distortion of cryo-EM images without need of pre-calibration","volume":"195","author":"Yu G","year":"2016","unstructured":"G Yu, , An algorithm for estimation and correction of anisotropic magnification distortion of cryo-EM images without need of pre-calibration. J Struct Biol 195, 207\u2013215 (2016).","journal-title":"J Struct Biol"},{"key":"e_1_3_4_56_2","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1007\/978-1-62703-776-1_19","article-title":"Single particle cryo-electron microscopy and 3-D reconstruction of viruses","volume":"1117","author":"Guo F","year":"2014","unstructured":"F Guo, W Jiang, Single particle cryo-electron microscopy and 3-D reconstruction of viruses. Methods Mol Biol 1117, 401\u2013443 (2014).","journal-title":"Methods Mol Biol"},{"key":"e_1_3_4_57_2","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1016\/j.jmb.2003.07.013","article-title":"Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy","volume":"333","author":"Rosenthal PB","year":"2003","unstructured":"PB Rosenthal, R Henderson, Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J Mol Biol 333, 721\u2013745 (2003).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_58_2","doi-asserted-by":"crossref","first-page":"1953","DOI":"10.1093\/bioinformatics\/btn341","article-title":"PIGS: Automatic prediction of antibody structures","volume":"24","author":"Marcatili P","year":"2008","unstructured":"P Marcatili, A Rosi, A Tramontano, PIGS: Automatic prediction of antibody structures. Bioinformatics 24, 1953\u20131954 (2008).","journal-title":"Bioinformatics"},{"key":"e_1_3_4_59_2","doi-asserted-by":"crossref","first-page":"2288","DOI":"10.1107\/S0907444904023716","article-title":"Developments in the CCP4 molecular-graphics project","volume":"60","author":"Potterton L","year":"2004","unstructured":"L Potterton, , Developments in the CCP4 molecular-graphics project. Acta Crystallogr D Biol Crystallogr 60, 2288\u20132294 (2004).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_60_2","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: A comprehensive Python-based system for macromolecular structure solution","volume":"66","author":"Adams PD","year":"2010","unstructured":"PD Adams, , PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66, 213\u2013221 (2010).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_61_2","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera\u2013A visualization system for exploratory research and analysis","volume":"25","author":"Pettersen EF","year":"2004","unstructured":"EF Pettersen, , UCSF Chimera\u2013A visualization system for exploratory research and analysis. J Comput Chem 25, 1605\u20131612 (2004).","journal-title":"J Comput Chem"},{"key":"e_1_3_4_62_2","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 E","year":"2007","unstructured":"E Krissinel, K Henrick, Inference of macromolecular assemblies from crystalline state. J Mol Biol 372, 774\u2013797 (2007).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_63_2","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/0022-2836(76)90195-9","article-title":"Exploring structural homology of proteins","volume":"105","author":"Rossmann MG","year":"1976","unstructured":"MG Rossmann, P Argos, Exploring structural homology of proteins. J Mol Biol 105, 75\u201395 (1976).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_64_2","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1016\/j.jsb.2006.10.013","article-title":"Interpretation of electron density with stereographic roadmap projections","volume":"158","author":"Xiao C","year":"2007","unstructured":"C Xiao, MG Rossmann, Interpretation of electron density with stereographic roadmap projections. J Struct Biol 158, 182\u2013187 (2007).","journal-title":"J Struct Biol"},{"key":"e_1_3_4_65_2","doi-asserted-by":"crossref","first-page":"W320","DOI":"10.1093\/nar\/gku316","article-title":"Deciphering key features in protein structures with the new ENDscript server","volume":"42","author":"Robert X","year":"2014","unstructured":"X Robert, P Gouet, Deciphering key features in protein structures with the new ENDscript server. Nucleic Acids Res 42, W320\u2013W24 (2014).","journal-title":"Nucleic Acids Res"}],"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.pnas.org\/syndication\/doi\/10.1073\/pnas.1815432116","content-type":"unspecified","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.1815432116","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,6,7]],"date-time":"2022-06-07T16:41:52Z","timestamp":1654620112000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.1815432116"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,1,14]]},"references-count":65,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2019,1,29]]}},"alternative-id":["10.1073\/pnas.1815432116"],"URL":"https:\/\/doi.org\/10.1073\/pnas.1815432116","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,1,14]]},"assertion":[{"value":"2019-01-14","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}