{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,9]],"date-time":"2026-11-09T22:12:33Z","timestamp":1794262353510,"version":"4.9.0"},"reference-count":58,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2024,4,6]],"date-time":"2024-04-06T00:00:00Z","timestamp":1712361600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2024,4,6]],"date-time":"2024-04-06T00:00:00Z","timestamp":1712361600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nat Commun"],"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Nipah virus (NiV) is a World Health Organization priority pathogen and there are currently no approved drugs for clinical immunotherapy. Through the use of a na\u00efve human phage-displayed Fab library, two neutralizing antibodies (NiV41 and NiV42) targeting the NiV receptor binding protein (RBP) were identified. Following affinity maturation, antibodies derived from NiV41 display cross-reactivity against both NiV and Hendra virus (HeV), whereas the antibody based on NiV42 is only specific to NiV. Results of immunogenetic analysis reveal a correlation between the maturation of antibodies and their antiviral activity. In vivo testing of NiV41 and its mature form (41-6) show protective efficacy against a lethal NiV challenge in hamsters. Furthermore, a 2.88\u2009\u00c5 Cryo-EM structure of the tetrameric RBP and antibody complex demonstrates that 41-6 blocks the receptor binding interface. These findings can be beneficial for the development of antiviral drugs and the design of vaccines with broad spectrum against henipaviruses.<\/jats:p>","DOI":"10.1038\/s41467-024-47213-8","type":"journal-article","created":{"date-parts":[[2024,4,6]],"date-time":"2024-04-06T14:01:59Z","timestamp":1712412119000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":28,"title":["Potent human neutralizing antibodies against Nipah virus derived from two ancestral antibody heavy chains"],"prefix":"10.1038","volume":"15","author":[{"ORCID":"https:\/\/orcid.org\/0009-0005-6304-9738","authenticated-orcid":false,"given":"Li","family":"Chen","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mengmeng","family":"Sun","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8161-3949","authenticated-orcid":false,"given":"Huajun","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xinghai","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6175-8590","authenticated-orcid":false,"given":"Yanfeng","family":"Yao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ming","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kangyin","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7212-231X","authenticated-orcid":false,"given":"Pengfei","family":"Fan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Haiwei","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ye","family":"Qin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhe","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Entao","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhen","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wuxiang","family":"Guan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7041-5960","authenticated-orcid":false,"given":"Shanshan","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0304-4477","authenticated-orcid":false,"given":"Changming","family":"Yu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0414-4776","authenticated-orcid":false,"given":"Kaiming","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9222-5642","authenticated-orcid":false,"given":"Rui","family":"Gong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9034-5755","authenticated-orcid":false,"given":"Sandra","family":"Chiu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2024,4,6]]},"reference":[{"key":"47213_CR1","doi-asserted-by":"publisher","first-page":"e13","DOI":"10.1016\/S1473-3099(21)00400-X","volume":"22","author":"R G\u00f3mez Rom\u00e1n","year":"2022","unstructured":"G\u00f3mez Rom\u00e1n, R. et al. Medical countermeasures against henipaviruses: a review and public health perspective. Lancet Infect. Dis. 22, e13\u2013e27 (2022).","journal-title":"Lancet Infect. Dis."},{"key":"47213_CR2","doi-asserted-by":"publisher","first-page":"23","DOI":"10.1038\/nrmicro1323","volume":"4","author":"BT Eaton","year":"2006","unstructured":"Eaton, B. T., Broder, C. C., Middleton, D. & Wang, L. F. Hendra and Nipah viruses: different and dangerous. Nat. Rev. Microbiol. 4, 23\u201335 (2006).","journal-title":"Nat. Rev. Microbiol."},{"key":"47213_CR3","doi-asserted-by":"publisher","first-page":"1432","DOI":"10.1126\/science.288.5470.1432","volume":"288","author":"KB Chua","year":"2000","unstructured":"Chua, K. B. et al. Nipah virus: a recently emergent deadly paramyxovirus. Science 288, 1432\u20131435 (2000).","journal-title":"Science"},{"key":"47213_CR4","doi-asserted-by":"publisher","first-page":"1804","DOI":"10.1056\/NEJMoa1805376","volume":"380","author":"B Nikolay","year":"2019","unstructured":"Nikolay, B. et al. Transmission of Nipah Virus - 14 years of investigations in Bangladesh. N. Engl. J. Med. 380, 1804\u20131814 (2019).","journal-title":"N. Engl. J. Med."},{"key":"47213_CR5","doi-asserted-by":"publisher","first-page":"1257","DOI":"10.1016\/S0140-6736(99)04299-3","volume":"354","author":"KB Chua","year":"1999","unstructured":"Chua, K. B. et al. Fatal encephalitis due to Nipah virus among pig-farmers in Malaysia. Lancet 354, 1257\u20131259 (1999).","journal-title":"Lancet"},{"key":"47213_CR6","doi-asserted-by":"publisher","first-page":"1229","DOI":"10.3201\/eid1508.081237","volume":"15","author":"SP Luby","year":"2009","unstructured":"Luby, S. P. et al. Recurrent zoonotic transmission of Nipah virus into humans, Bangladesh, 2001-2007. Emerg. Infect. Dis. 15, 1229\u20131235 (2009).","journal-title":"Emerg. Infect. Dis."},{"key":"47213_CR7","doi-asserted-by":"publisher","first-page":"e01875","DOI":"10.1128\/JCM.01875-17","volume":"56","author":"BSP Ang","year":"2018","unstructured":"Ang, B. S. P., Lim, T. C. C. & Wang, L. Nipah virus infection. J. Clin. Microbiol. 56, e01875\u201317 (2018).","journal-title":"J. Clin. Microbiol."},{"key":"47213_CR8","doi-asserted-by":"publisher","first-page":"144","DOI":"10.1016\/j.ijid.2020.10.041","volume":"102","author":"MZ Rahman","year":"2021","unstructured":"Rahman, M. Z. et al. Genetic diversity of Nipah virus in Bangladesh. Int. J. Infect. Dis. 102, 144\u2013151 (2021).","journal-title":"Int. J. Infect. Dis."},{"key":"47213_CR9","doi-asserted-by":"publisher","first-page":"449","DOI":"10.1146\/annurev-pathol-012414-040501","volume":"10","author":"D Safronetz","year":"2015","unstructured":"Safronetz, D., Feldmann, H. & de Wit, E. Birth and pathogenesis of rogue respiratory viruses. Annu. Rev. Pathol. 10, 449\u2013471 (2015).","journal-title":"Annu. Rev. Pathol."},{"key":"47213_CR10","doi-asserted-by":"publisher","first-page":"1167085","DOI":"10.3389\/fmicb.2023.1167085","volume":"14","author":"H Li","year":"2023","unstructured":"Li, H., Kim, J.-Y. V. & Pickering, B. S. Henipavirus zoonosis: outbreaks, animal hosts and potential new emergence. Front. Microbiol. 14, 1167085 (2023).","journal-title":"Front. Microbiol."},{"key":"47213_CR11","doi-asserted-by":"publisher","first-page":"1593","DOI":"10.1099\/jgv.0.001328","volume":"100","author":"B Rima","year":"2019","unstructured":"Rima, B. et al. ICTV virus taxonomy profile: Paramyxoviridae. J. Gen. Virol. 100, 1593\u20131594 (2019).","journal-title":"J. Gen. Virol."},{"key":"47213_CR12","doi-asserted-by":"publisher","first-page":"401","DOI":"10.1038\/nature03838","volume":"436","author":"OA Negrete","year":"2005","unstructured":"Negrete, O. A. et al. EphrinB2 is the entry receptor for Nipah virus, an emergent deadly paramyxovirus. Nature 436, 401\u2013405 (2005).","journal-title":"Nature"},{"key":"47213_CR13","doi-asserted-by":"publisher","first-page":"10652","DOI":"10.1073\/pnas.0504887102","volume":"102","author":"MI Bonaparte","year":"2005","unstructured":"Bonaparte, M. I. et al. Ephrin-B2 ligand is a functional receptor for Hendra virus and Nipah virus. Proc. Natl Acad. Sci. USA 102, 10652\u201310657 (2005).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"47213_CR14","doi-asserted-by":"publisher","first-page":"10762","DOI":"10.1128\/JVI.01469-16","volume":"90","author":"JA Stone","year":"2016","unstructured":"Stone, J. A., Vemulapati, B. M., Bradel-Tretheway, B. & Aguilar, H. C. Multiple strategies reveal a bidentate interaction between the Nipah virus attachment and fusion glycoproteins. J. Virol. 90, 10762\u201310773 (2016).","journal-title":"J. Virol."},{"key":"47213_CR15","doi-asserted-by":"publisher","DOI":"10.1128\/mbio.03222-21","volume":"13","author":"V Ortega","year":"2022","unstructured":"Ortega, V. et al. Novel roles of the Nipah virus attachment glycoprotein and its mobility in early and late membrane fusion steps. mBio 13, e0322221 (2022).","journal-title":"mBio"},{"key":"47213_CR16","doi-asserted-by":"publisher","first-page":"e1003770","DOI":"10.1371\/journal.ppat.1003770","volume":"9","author":"Q Liu","year":"2013","unstructured":"Liu, Q. et al. Unraveling a three-step spatiotemporal mechanism of triggering of receptor-induced Nipah virus fusion and cell entry. PLoS Pathog. 9, e1003770 (2013).","journal-title":"PLoS Pathog."},{"key":"47213_CR17","doi-asserted-by":"publisher","first-page":"11628","DOI":"10.1128\/JVI.01344-08","volume":"82","author":"TA Bowden","year":"2008","unstructured":"Bowden, T. A. et al. Crystal structure and carbohydrate analysis of Nipah virus attachment glycoprotein: a template for antiviral and vaccine design. J. Virol. 82, 11628\u201311636 (2008).","journal-title":"J. Virol."},{"key":"47213_CR18","doi-asserted-by":"publisher","first-page":"1373","DOI":"10.1126\/science.abm5561","volume":"375","author":"Z Wang","year":"2022","unstructured":"Wang, Z. et al. Architecture and antigenicity of the Nipah virus attachment glycoprotein. Science 375, 1373\u20131378 (2022).","journal-title":"Science"},{"key":"47213_CR19","doi-asserted-by":"publisher","first-page":"6632","DOI":"10.1128\/JVI.00076-12","volume":"86","author":"D Maar","year":"2012","unstructured":"Maar, D. et al. Cysteines in the stalk of the nipah virus G glycoprotein are located in a distinct subdomain critical for fusion activation. J. Virol. 86, 6632\u20136642 (2012).","journal-title":"J. Virol."},{"key":"47213_CR20","doi-asserted-by":"publisher","first-page":"11398","DOI":"10.1128\/JVI.02654-07","volume":"82","author":"KA Bishop","year":"2008","unstructured":"Bishop, K. A. et al. Residues in the stalk domain of the hendra virus g glycoprotein modulate conformational changes associated with receptor binding. J. Virol. 82, 11398\u201311409 (2008).","journal-title":"J. Virol."},{"key":"47213_CR21","doi-asserted-by":"publisher","first-page":"567","DOI":"10.1038\/nsmb.1435","volume":"15","author":"TA Bowden","year":"2008","unstructured":"Bowden, T. A. et al. Structural basis of Nipah and Hendra virus attachment to their cell-surface receptor ephrin-B2. Nat. Struct. Mol. Biol. 15, 567\u2013572 (2008).","journal-title":"Nat. Struct. Mol. Biol."},{"key":"47213_CR22","doi-asserted-by":"publisher","first-page":"e1003684","DOI":"10.1371\/journal.ppat.1003684","volume":"9","author":"K Xu","year":"2013","unstructured":"Xu, K. et al. Crystal structure of the Hendra virus attachment G glycoprotein bound to a potent cross-reactive neutralizing human monoclonal antibody. PLoS Pathog. 9, e1003684 (2013).","journal-title":"PLoS Pathog."},{"key":"47213_CR23","unstructured":"Research CfDEa. FDA approves treatment for ebola virus (U.S. Food and Drug Administration, 2020)."},{"key":"47213_CR24","unstructured":"Research CfDEa. FDA approves first treatment for ebola virus (U.S. Food and Drug Administration, 2020)."},{"key":"47213_CR25","doi-asserted-by":"publisher","first-page":"112","DOI":"10.1038\/s41579-022-00809-7","volume":"21","author":"M Cox","year":"2023","unstructured":"Cox, M. et al. SARS-CoV-2 variant evasion of monoclonal antibodies based on in vitro studies. Nat. Rev. Microbiol. 21, 112\u2013124 (2023).","journal-title":"Nat. Rev. Microbiol."},{"key":"47213_CR26","doi-asserted-by":"publisher","first-page":"382","DOI":"10.1038\/s41577-021-00542-x","volume":"21","author":"PC Taylor","year":"2021","unstructured":"Taylor, P. C. et al. Neutralizing monoclonal antibodies for treatment of COVID-19. Nat. Rev. Immunol. 21, 382\u2013393 (2021).","journal-title":"Nat. Rev. Immunol."},{"key":"47213_CR27","doi-asserted-by":"publisher","first-page":"891","DOI":"10.1128\/JVI.80.2.891-899.2006","volume":"80","author":"Z Zhu","year":"2006","unstructured":"Zhu, Z. et al. Potent neutralization of Hendra and Nipah viruses by human monoclonal antibodies. J. Virol. 80, 891\u2013899 (2006).","journal-title":"J. Virol."},{"key":"47213_CR28","doi-asserted-by":"publisher","first-page":"445","DOI":"10.1016\/S1473-3099(19)30634-6","volume":"20","author":"EG Playford","year":"2020","unstructured":"Playford, E. G. et al. Safety, tolerability, pharmacokinetics, and immunogenicity of a human monoclonal antibody targeting the G glycoprotein of henipaviruses in healthy adults: a first-in-human, randomised, controlled, phase 1 study. Lancet Infect. Dis. 20, 445\u2013454 (2020).","journal-title":"Lancet Infect. Dis."},{"key":"47213_CR29","doi-asserted-by":"publisher","first-page":"1536","DOI":"10.1016\/j.cell.2020.11.023","volume":"183","author":"J Dong","year":"2020","unstructured":"Dong, J. et al. Potent Henipavirus neutralization by antibodies recognizing diverse sites on Hendra and Nipah virus receptor binding protein. Cell 183, 1536\u20131550.e1517 (2020).","journal-title":"Cell"},{"key":"47213_CR30","doi-asserted-by":"publisher","DOI":"10.1038\/srep30916","volume":"6","author":"CE Mire","year":"2016","unstructured":"Mire, C. E. et al. Pathogenic differences between Nipah virus Bangladesh and Malaysia strains in primates: iplications for antibody therapy. Sci. Rep. 6, 30916 (2016).","journal-title":"Sci. Rep."},{"key":"47213_CR31","first-page":"779","volume":"10","author":"JD Marks","year":"1992","unstructured":"Marks, J. D. et al. By-passing immunization: building high affinity human antibodies by chain shuffling. Biotechnology 10, 779\u2013783 (1992).","journal-title":"Biotechnology"},{"key":"47213_CR32","doi-asserted-by":"publisher","first-page":"55","DOI":"10.1038\/nature13036","volume":"509","author":"NA Doria-Rose","year":"2014","unstructured":"Doria-Rose, N. A. et al. Developmental pathway for potent V1V2-directed HIV-neutralizing antibodies. Nature 509, 55\u201362 (2014).","journal-title":"Nature"},{"key":"47213_CR33","doi-asserted-by":"publisher","first-page":"469","DOI":"10.1038\/nature12053","volume":"496","author":"HX Liao","year":"2013","unstructured":"Liao, H. X. et al. Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus. Nature 496, 469\u2013476 (2013).","journal-title":"Nature"},{"key":"47213_CR34","doi-asserted-by":"publisher","first-page":"210","DOI":"10.1097\/COH.0000000000000057","volume":"9","author":"CA Derdeyn","year":"2014","unstructured":"Derdeyn, C. A., Moore, P. L. & Morris, L. Development of broadly neutralizing antibodies from autologous neutralizing antibody responses in HIV infection. Curr. Opin. HIV AIDS 9, 210\u2013216 (2014).","journal-title":"Curr. Opin. HIV AIDS"},{"key":"47213_CR35","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-021-25153-x","volume":"12","author":"S Zhao","year":"2021","unstructured":"Zhao, S. et al. Identification of potent human neutralizing antibodies against SARS-CoV-2 implications for development of therapeutics and prophylactics. Nat. Commun. 12, 4887 (2021).","journal-title":"Nat. Commun."},{"key":"47213_CR36","doi-asserted-by":"publisher","first-page":"846","DOI":"10.1086\/528801","volume":"197","author":"Z Zhu","year":"2008","unstructured":"Zhu, Z. et al. Exceptionally potent cross-reactive neutralization of Nipah and Hendra viruses by a human monoclonal antibody. J. Infect. Dis. 197, 846\u2013853 (2008).","journal-title":"J. Infect. Dis."},{"key":"47213_CR37","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-020-75056-y","volume":"10","author":"P Tit-Oon","year":"2020","unstructured":"Tit-Oon, P. et al. Prediction of the binding interface between monoclonal antibody m102.4 and Nipah attachment glycoprotein using structure-guided alanine scanning and computational docking. Sci. Rep. 10, 18256 (2020).","journal-title":"Sci. Rep."},{"key":"47213_CR38","doi-asserted-by":"publisher","first-page":"279","DOI":"10.1016\/S1286-4579(01)01381-8","volume":"3","author":"L Wang","year":"2001","unstructured":"Wang, L. et al. Molecular biology of Hendra and Nipah viruses. Microbes Infect. 3, 279\u2013287 (2001).","journal-title":"Microbes Infect."},{"key":"47213_CR39","doi-asserted-by":"publisher","DOI":"10.1016\/j.celrep.2021.109628","volume":"36","author":"MP Doyle","year":"2021","unstructured":"Doyle, M. P. et al. Cooperativity mediated by rationally selected combinations of human monoclonal antibodies targeting the henipavirus receptor binding protein. Cell Rep. 36, 109628 (2021).","journal-title":"Cell Rep."},{"key":"47213_CR40","doi-asserted-by":"publisher","first-page":"a038786","DOI":"10.1101\/cshperspect.a038786","volume":"11","author":"JW Yewdell","year":"2021","unstructured":"Yewdell, J. W. & Santos, J. J. S. Original antigenic sin: how original? how sinful? Cold Spring Harb. Perspect. Med. 11, a038786 (2021).","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"47213_CR41","doi-asserted-by":"publisher","first-page":"70","DOI":"10.1016\/j.it.2017.08.003","volume":"39","author":"C Henry","year":"2018","unstructured":"Henry, C., Palm, A.-K. E., Krammer, F. & Wilson, P. C. From original antigenic sin to the universal influenza virus vaccine. Trends Immunol. 39, 70\u201379 (2018).","journal-title":"Trends Immunol."},{"key":"47213_CR42","doi-asserted-by":"publisher","first-page":"149","DOI":"10.1016\/j.coviro.2019.02.004","volume":"34","author":"F Chen","year":"2019","unstructured":"Chen, F., Tzarum, N., Wilson, I. A. & Law, M. VH1-69 antiviral broadly neutralizing antibodies: genetics, structures, and relevance to rational vaccine design. Curr. Opin. Virol. 34, 149\u2013159 (2019).","journal-title":"Curr. Opin. Virol."},{"key":"47213_CR43","doi-asserted-by":"publisher","first-page":"531","DOI":"10.1016\/S0022-2836(02)01237-8","volume":"325","author":"S Ewert","year":"2003","unstructured":"Ewert, S., Huber, T., Honegger, A. & Pl\u00fcckthun, A. Biophysical properties of human antibody variable domains. J. Mol. Biol. 325, 531\u2013553 (2003).","journal-title":"J. Mol. Biol."},{"key":"47213_CR44","doi-asserted-by":"publisher","first-page":"e1000642","DOI":"10.1371\/journal.ppat.1000642","volume":"5","author":"KN Bossart","year":"2009","unstructured":"Bossart, K. N. et al. A neutralizing human monoclonal antibody protects against lethal disease in a new ferret model of acute nipah virus infection. PLoS Pathog. 5, e1000642 (2009).","journal-title":"PLoS Pathog."},{"key":"47213_CR45","doi-asserted-by":"publisher","first-page":"242ra82","DOI":"10.1126\/scitranslmed.3008929","volume":"6","author":"TW Geisbert","year":"2014","unstructured":"Geisbert, T. W. et al. Therapeutic treatment of Nipah virus infection in nonhuman primates with a neutralizing human monoclonal antibody. Sci. Transl. Med. 6, 242ra82 (2014).","journal-title":"Sci. Transl. Med."},{"key":"47213_CR46","doi-asserted-by":"publisher","first-page":"105ra103","DOI":"10.1126\/scitranslmed.3002901","volume":"3","author":"KN Bossart","year":"2011","unstructured":"Bossart, K. N. et al. A neutralizing human monoclonal antibody protects african green monkeys from hendra virus challenge. Sci. Transl. Med. 3, 105ra103 (2011).","journal-title":"Sci. Transl. Med."},{"key":"47213_CR47","doi-asserted-by":"publisher","first-page":"2127","DOI":"10.1016\/S0002-9440(10)63569-9","volume":"163","author":"KT Wong","year":"2003","unstructured":"Wong, K. T. et al. A golden hamster model for human acute Nipah virus infection. Am. J. Pathol. 163, 2127\u20132137 (2003).","journal-title":"Am. J. Pathol."},{"key":"47213_CR48","doi-asserted-by":"publisher","first-page":"834","DOI":"10.1128\/JVI.78.2.834-840.2004","volume":"78","author":"V Guillaume","year":"2004","unstructured":"Guillaume, V. et al. Nipah virus: vaccination and passive protection studies in a hamster model. J. Virol. 78, 834\u2013840 (2004).","journal-title":"J. Virol."},{"key":"47213_CR49","doi-asserted-by":"publisher","first-page":"S493","DOI":"10.1093\/infdis\/jiz553","volume":"221","author":"MK Lo","year":"2020","unstructured":"Lo, M. K. et al. Evaluation of a single-dose nucleoside-modified messenger RNA vaccine encoding Hendra virus-soluble glycoprotein against lethal Nipah virus challenge in Syrian hamsters. J. Infect. Dis. 221, S493\u2013S498 (2020).","journal-title":"J. Infect. Dis."},{"key":"47213_CR50","doi-asserted-by":"publisher","first-page":"e2024","DOI":"10.1371\/journal.pntd.0002024","volume":"7","author":"BL DeBuysscher","year":"2013","unstructured":"DeBuysscher, B. L. et al. Comparison of the pathogenicity of Nipah virus isolates from Bangladesh and Malaysia in the Syrian hamster. PLoS Negl. Trop. Dis. 7, e2024 (2013).","journal-title":"PLoS Negl. Trop. Dis."},{"key":"47213_CR51","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1016\/j.jviromet.2009.04.037","volume":"160","author":"Y Kaku","year":"2009","unstructured":"Kaku, Y. et al. A neutralization test for specific detection of Nipah virus antibodies using pseudotyped vesicular stomatitis virus expressing green fluorescent protein. J. Virol. Methods 160, 7\u201313 (2009).","journal-title":"J. Virol. Methods"},{"key":"47213_CR52","doi-asserted-by":"publisher","DOI":"10.1186\/1743-422X-7-312","volume":"7","author":"D Khetawat","year":"2010","unstructured":"Khetawat, D. & Broder, C. C. A functional henipavirus envelope glycoprotein pseudotyped lentivirus assay system. Virol. J. 7, 312 (2010).","journal-title":"Virol. J."},{"key":"47213_CR53","doi-asserted-by":"publisher","first-page":"W296","DOI":"10.1093\/nar\/gky427","volume":"46","author":"A Waterhouse","year":"2018","unstructured":"Waterhouse, A. et al. SWISS-MODEL: homology modelling of protein structures and complexes. Nucleic Acids Res. 46, W296\u2013W303 (2018).","journal-title":"Nucleic Acids Res."},{"key":"47213_CR54","doi-asserted-by":"publisher","first-page":"679","DOI":"10.1038\/s41592-022-01488-1","volume":"19","author":"M Mirdita","year":"2022","unstructured":"Mirdita, M. et al. ColabFold: making protein folding accessible to all. Nat. Methods 19, 679\u2013682 (2022).","journal-title":"Nat. Methods"},{"key":"47213_CR55","doi-asserted-by":"publisher","first-page":"673","DOI":"10.1016\/j.str.2008.03.005","volume":"16","author":"LG Trabuco","year":"2008","unstructured":"Trabuco, L. G., Villa, E., Mitra, K., Frank, J. & Schulten, K. Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics. Structure 16, 673\u2013683 (2008).","journal-title":"Structure"},{"key":"47213_CR56","doi-asserted-by":"publisher","first-page":"486","DOI":"10.1107\/S0907444910007493","volume":"66","author":"P Emsley","year":"2010","unstructured":"Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D. Biol. Crystallogr. 66, 486\u2013501 (2010).","journal-title":"Acta Crystallogr. D. Biol. Crystallogr."},{"key":"47213_CR57","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1107\/S0907444909052925","volume":"66","author":"PD Adams","year":"2010","unstructured":"Adams, P. D. et al. 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":"47213_CR58","doi-asserted-by":"publisher","first-page":"12","DOI":"10.1107\/S0907444909042073","volume":"66","author":"VB Chen","year":"2010","unstructured":"Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D. Biol. Crystallogr. 66, 12\u201321 (2010).","journal-title":"Acta Crystallogr. D. Biol. Crystallogr."}],"container-title":["Nature Communications"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41467-024-47213-8.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41467-024-47213-8","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41467-024-47213-8.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,4,6]],"date-time":"2024-04-06T15:02:42Z","timestamp":1712415762000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41467-024-47213-8"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,4,6]]},"references-count":58,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2024,12]]}},"alternative-id":["47213"],"URL":"https:\/\/doi.org\/10.1038\/s41467-024-47213-8","relation":{},"ISSN":["2041-1723"],"issn-type":[{"value":"2041-1723","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,4,6]]},"assertion":[{"value":"14 August 2023","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"18 March 2024","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"6 April 2024","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"R.G. and his colleagues are listed as inventors on pending patent applications for the identified neutralizing antibodies in this work (CN202310743583.6 and CN202310743574.7). The remaining authors declare no competing interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"2987"}}