{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T03:29:01Z","timestamp":1792466941087,"version":"4.5.0"},"reference-count":146,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2026,2,11]],"date-time":"2026-02-11T00:00:00Z","timestamp":1770768000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"},{"start":{"date-parts":[[2026,3,20]],"date-time":"2026-03-20T00:00:00Z","timestamp":1773964800000},"content-version":"vor","delay-in-days":37,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"}],"funder":[{"DOI":"10.13039\/100000060","name":"U.S. Department of Health & Human Services | NIH | National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["AI168251"],"award-info":[{"award-number":["AI168251"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nat Commun"],"DOI":"10.1038\/s41467-026-69418-9","type":"journal-article","created":{"date-parts":[[2026,2,11]],"date-time":"2026-02-11T11:53:54Z","timestamp":1770810834000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Native-like soluble E1E2 glycoprotein heterodimers on self-assembling protein nanoparticles for hepatitis C virus vaccine design"],"prefix":"10.1038","volume":"17","author":[{"given":"Linling","family":"He","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5651-863X","authenticated-orcid":false,"given":"Yi-Zong","family":"Lee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9053-5890","authenticated-orcid":false,"given":"Yi-Nan","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maddy L.","family":"Newby","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6290-8300","authenticated-orcid":false,"given":"Benjamin M.","family":"Janus","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0000-1864-8233","authenticated-orcid":false,"given":"Fabrizio G.","family":"Gonzalez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Garrett","family":"Ward","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Connor","family":"DesRoberts","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9067-2035","authenticated-orcid":false,"given":"Shr-Hau","family":"Hung","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erick","family":"Giang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2547-968X","authenticated-orcid":false,"given":"Joel D.","family":"Allen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Liudmila","family":"Kulakova","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0766-5131","authenticated-orcid":false,"given":"Eric A.","family":"Toth","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9766-9995","authenticated-orcid":false,"given":"Thomas R.","family":"Fuerst","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8934-9756","authenticated-orcid":false,"given":"Mansun","family":"Law","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0677-4467","authenticated-orcid":false,"given":"Gilad","family":"Ofek","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1072-2694","authenticated-orcid":false,"given":"Max","family":"Crispin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0259-7157","authenticated-orcid":false,"given":"Jiang","family":"Zhu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,2,11]]},"reference":[{"key":"69418_CR1","unstructured":"World Health Organization. Global Hepatitis Report 2024 (World Health Organization, 2024)."},{"key":"69418_CR2","doi-asserted-by":"publisher","first-page":"202","DOI":"10.15585\/mmwr.mm7006a4","volume":"70","author":"CL Mattson","year":"2021","unstructured":"Mattson, C. L. et al. Trends and geographic patterns in drug and synthetic opioid overdose deaths - United States, 2013-2019. MMWR Morb. Mortal. Wkly Rep. 70, 202\u2013207 (2021).","journal-title":"MMWR Morb. Mortal. Wkly Rep."},{"key":"69418_CR3","doi-asserted-by":"publisher","first-page":"175","DOI":"10.2105\/AJPH.2017.304132","volume":"108","author":"JE Zibbell","year":"2018","unstructured":"Zibbell, J. E. et al. Increases in acute hepatitis C virus infection related to a growing opioid epidemic and associated injection drug use, United States, 2004 to 2014. Am. J. Public Health 108, 175\u2013181 (2018).","journal-title":"Am. J. Public Health"},{"key":"69418_CR4","doi-asserted-by":"publisher","first-page":"1453","DOI":"10.1016\/S0140-6736(18)32111-1","volume":"393","author":"F Carrat","year":"2019","unstructured":"Carrat, F. et al. Clinical outcomes in patients with chronic hepatitis C after direct-acting antiviral treatment: a prospective cohort study. Lancet 393, 1453\u20131464 (2019).","journal-title":"Lancet"},{"key":"69418_CR5","doi-asserted-by":"publisher","first-page":"g3308","DOI":"10.1136\/bmj.g3308","volume":"348","author":"ER Feeney","year":"2014","unstructured":"Feeney, E. R. & Chung, R. T. Antiviral treatment of hepatitis C. BMJ 348, g3308 (2014).","journal-title":"BMJ"},{"key":"69418_CR6","doi-asserted-by":"publisher","first-page":"1392","DOI":"10.1016\/S0140-6736(18)32326-2","volume":"393","author":"JA Holmes","year":"2019","unstructured":"Holmes, J. A., Rutledge, S. M. & Chung, R. T. Direct-acting antiviral treatment for hepatitis C. Lancet 393, 1392\u20131394 (2019).","journal-title":"Lancet"},{"key":"69418_CR7","doi-asserted-by":"publisher","first-page":"1224","DOI":"10.1016\/j.jhep.2016.01.029","volume":"64","author":"GR Foster","year":"2016","unstructured":"Foster, G. R. et al. Impact of direct acting antiviral therapy in patients with chronic hepatitis C and decompensated cirrhosis. J. Hepatol. 64, 1224\u20131231 (2016).","journal-title":"J. Hepatol."},{"key":"69418_CR8","doi-asserted-by":"publisher","first-page":"741","DOI":"10.1016\/j.jhep.2016.06.019","volume":"65","author":"MCM Cheung","year":"2016","unstructured":"Cheung, M. C. M. et al. Outcomes after successful direct-acting antiviral therapy for patients with chronic hepatitis C and decompensated cirrhosis. J. Hepatol. 65, 741\u2013747 (2016).","journal-title":"J. Hepatol."},{"key":"69418_CR9","doi-asserted-by":"publisher","first-page":"727","DOI":"10.1016\/j.jhep.2016.06.015","volume":"65","author":"F Conti","year":"2016","unstructured":"Conti, F. et al. Early occurrence and recurrence of hepatocellular carcinoma in HCV-related cirrhosis treated with direct-acting antivirals. J. Hepatol. 65, 727\u2013733 (2016).","journal-title":"J. Hepatol."},{"key":"69418_CR10","doi-asserted-by":"publisher","DOI":"10.1038\/ctg.2016.50","volume":"7","author":"MA Konerman","year":"2016","unstructured":"Konerman, M. A. & Lok, A. S. Hepatitis C treatment and barriers to eradication. Clin. Transl. Gastroenterol. 7, e193 (2016).","journal-title":"Clin. Transl. Gastroenterol."},{"key":"69418_CR11","doi-asserted-by":"publisher","first-page":"734","DOI":"10.1016\/j.jhep.2016.05.045","volume":"65","author":"S Pol","year":"2016","unstructured":"Pol, S. Lack of evidence of an effect of direct-acting antivirals on the recurrence of hepatocellular carcinoma: data from three ANRS cohorts. J. Hepatol. 65, 734\u2013740 (2016).","journal-title":"J. Hepatol."},{"key":"69418_CR12","doi-asserted-by":"publisher","DOI":"10.1186\/s13036-024-00443-2","volume":"18","author":"AS Baber","year":"2024","unstructured":"Baber, A. S., Suganthan, B. & Ramasamy, R. P. Current advances in hepatitis C diagnostics. J. Biol. Eng. 18, 48 (2024).","journal-title":"J. Biol. Eng."},{"key":"69418_CR13","doi-asserted-by":"publisher","first-page":"28","DOI":"10.1038\/nrgastro.2013.179","volume":"11","author":"M Thursz","year":"2014","unstructured":"Thursz, M. & Fontanet, A. HCV transmission in industrialized countries and resource-constrained areas. Nat. Rev. Gastroenterol. Hepatol. 11, 28\u201335 (2014).","journal-title":"Nat. Rev. Gastroenterol. Hepatol."},{"key":"69418_CR14","doi-asserted-by":"publisher","first-page":"4959","DOI":"10.3748\/wjg.v24.i44.4959","volume":"24","author":"Y Waheed","year":"2018","unstructured":"Waheed, Y., Siddiq, M., Jamil, Z. & Najmi, M. H. Hepatitis elimination by 2030: Progress and challenges. World J. Gastroenterol. 24, 4959\u20134961 (2018).","journal-title":"World J. Gastroenterol."},{"key":"69418_CR15","doi-asserted-by":"publisher","first-page":"533","DOI":"10.1038\/s41575-020-0332-6","volume":"17","author":"AL Cox","year":"2020","unstructured":"Cox, A. L. et al. Progress towards elimination goals for viral hepatitis. Nat. Rev. Gastroenterol. Hepatol. 17, 533\u2013542 (2020).","journal-title":"Nat. Rev. Gastroenterol. Hepatol."},{"key":"69418_CR16","doi-asserted-by":"publisher","DOI":"10.1038\/emi.2014.19","volume":"3","author":"S Pfaender","year":"2014","unstructured":"Pfaender, S., Brown, R. J. P., Pietschmann, T. & Steinmann, E. Natural reservoirs for homologs of hepatitis C virus. Emerg. Microbes Infect. 3, e21 (2014).","journal-title":"Emerg. Microbes Infect."},{"key":"69418_CR17","first-page":"1","volume":"369","author":"P Simmonds","year":"2013","unstructured":"Simmonds, P. The origin of hepatitis C virus. Curr. Top. Microbiol. Immunol. 369, 1\u201315 (2013).","journal-title":"Curr. Top. Microbiol. Immunol."},{"key":"69418_CR18","doi-asserted-by":"publisher","first-page":"S3","DOI":"10.1016\/j.jhep.2014.06.031","volume":"61","author":"J Dubuisson","year":"2014","unstructured":"Dubuisson, J. & Cosset, F. L. Virology and cell biology of the hepatitis C virus life cycle - an update. J. Hepatol. 61, S3\u2013S13 (2014).","journal-title":"J. Hepatol."},{"key":"69418_CR19","first-page":"113","volume":"369","author":"D Moradpour","year":"2013","unstructured":"Moradpour, D. & Penin, F. Hepatitis C virus proteins: from structure to function. Curr. Top. Microbiol. Immunol. 369, 113\u2013142 (2013).","journal-title":"Curr. Top. Microbiol. Immunol."},{"key":"69418_CR20","doi-asserted-by":"publisher","first-page":"2406","DOI":"10.3748\/wjg.v13.i17.2406","volume":"13","author":"J Dubuisson","year":"2007","unstructured":"Dubuisson, J. Hepatitis C virus proteins. World J. Gastroenterol. 13, 2406\u20132415 (2007).","journal-title":"World J. Gastroenterol."},{"key":"69418_CR21","doi-asserted-by":"publisher","first-page":"688","DOI":"10.1038\/nrmicro3098","volume":"11","author":"BD Lindenbach","year":"2013","unstructured":"Lindenbach, B. D. & Rice, C. M. The ins and outs of hepatitis C virus entry and assembly. Nat. Rev. Microbiol. 11, 688\u2013700 (2013).","journal-title":"Nat. Rev. Microbiol."},{"key":"69418_CR22","doi-asserted-by":"publisher","first-page":"1917","DOI":"10.3389\/fimmu.2018.01917","volume":"9","author":"SA Yost","year":"2018","unstructured":"Yost, S. A., Wang, Y. & Marcotrigiano, J. Hepatitis C virus envelope glycoproteins: a balancing act of order and disorder. Front. Immunol. 9, 1917 (2018).","journal-title":"Front. Immunol."},{"key":"69418_CR23","doi-asserted-by":"publisher","first-page":"749","DOI":"10.1021\/acsinfecdis.6b00110","volume":"2","author":"H Freedman","year":"2016","unstructured":"Freedman, H., Logan, M. R., Law, J. L. M. & Houghton, M. Structure and function of the hepatitis C virus envelope glycoproteins E1 and E2: antiviral and vaccine targets. ACS Infect. Dis. 2, 749\u2013762 (2016).","journal-title":"ACS Infect. Dis."},{"key":"69418_CR24","doi-asserted-by":"publisher","first-page":"535","DOI":"10.3390\/v6020535","volume":"6","author":"L Feneant","year":"2014","unstructured":"Feneant, L., Levy, S. & Cocquerel, L. CD81 and hepatitis C virus (HCV) infection. Viruses 6, 535\u2013572 (2014).","journal-title":"Viruses"},{"key":"69418_CR25","doi-asserted-by":"publisher","first-page":"2146","DOI":"10.3389\/fimmu.2018.02146","volume":"9","author":"J Prentoe","year":"2018","unstructured":"Prentoe, J. & Bukh, J. Hypervariable region 1 in envelope protein 2 of hepatitis C virus: a linchpin in neutralizing antibody evasion and viral entry. Front. Immunol. 9, 2146 (2018).","journal-title":"Front. Immunol."},{"key":"69418_CR26","doi-asserted-by":"publisher","first-page":"1411","DOI":"10.3389\/fimmu.2018.01411","volume":"9","author":"YM Tong","year":"2018","unstructured":"Tong, Y. M., Lavillette, D., Li, Q. C. & Zhong, J. Role of hepatitis C virus envelope glycoprotein E1 in virus entry and assembly. Front. Immunol. 9, 1411 (2018).","journal-title":"Front. Immunol."},{"key":"69418_CR27","doi-asserted-by":"publisher","first-page":"1149","DOI":"10.1002\/hep.24523","volume":"54","author":"B Mazumdar","year":"2011","unstructured":"Mazumdar, B., Banerjee, A., Meyer, K. & Ray, R. Hepatitis C virus E1 envelope glycoprotein interacts with apolipoproteins in facilitating entry into hepatocytes. Hepatology 54, 1149\u20131156 (2011).","journal-title":"Hepatology"},{"key":"69418_CR28","unstructured":"Smith, D. B. et al. Flaviviridae: Hepacivirus C classification. https:\/\/ictv.global\/sg_wiki\/flaviviridae\/hepacivirus (2022)."},{"key":"69418_CR29","doi-asserted-by":"publisher","first-page":"23","DOI":"10.3390\/ijms19010023","volume":"19","author":"K Tsukiyama-Kohara","year":"2018","unstructured":"Tsukiyama-Kohara, K. & Kohara, M. Hepatitis C virus: Viral quasispecies and genotypes. Int. J. Mol. Sci. 19, 23 (2018).","journal-title":"Int. J. Mol. Sci."},{"key":"69418_CR30","doi-asserted-by":"publisher","first-page":"S2","DOI":"10.1016\/j.jhep.2016.07.035","volume":"65","author":"J Bukh","year":"2016","unstructured":"Bukh, J. The history of hepatitis C virus (HCV): basic research reveals unique features in phylogeny, evolution and the viral life cycle with new perspectives for epidemic control. J. Hepatol. 65, S2\u2013S21 (2016).","journal-title":"J. Hepatol."},{"key":"69418_CR31","doi-asserted-by":"publisher","first-page":"408","DOI":"10.1016\/S1473-3099(12)70010-5","volume":"12","author":"J Grebely","year":"2012","unstructured":"Grebely, J. et al. Hepatitis C virus clearance, reinfection, and persistence, with insights from studies of injecting drug users: towards a vaccine. Lancet Infect. Dis. 12, 408\u2013414 (2012).","journal-title":"Lancet Infect. Dis."},{"key":"69418_CR32","doi-asserted-by":"publisher","first-page":"541","DOI":"10.1056\/NEJMoa2023345","volume":"384","author":"K Page","year":"2021","unstructured":"Page, K. et al. Randomized trial of a vaccine regimen to prevent chronic HCV infection. N. Engl. J. Med. 384, 541\u2013549 (2021).","journal-title":"N. Engl. J. Med."},{"key":"69418_CR33","doi-asserted-by":"publisher","first-page":"6205","DOI":"10.1073\/pnas.1114927109","volume":"109","author":"E Giang","year":"2012","unstructured":"Giang, E. et al. Human broadly neutralizing antibodies to the envelope glycoprotein complex of hepatitis C virus. Proc. Natl. Acad. Sci. USA 109, 6205\u20136210 (2012).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"69418_CR34","doi-asserted-by":"publisher","first-page":"25","DOI":"10.1038\/nm1698","volume":"14","author":"M Law","year":"2008","unstructured":"Law, M. et al. Broadly neutralizing antibodies protect against hepatitis C virus quasispecies challenge. Nat. Med. 14, 25\u201327 (2008).","journal-title":"Nat. Med."},{"key":"69418_CR35","doi-asserted-by":"publisher","first-page":"8449","DOI":"10.1073\/pnas.0703039104","volume":"104","author":"P Zhang","year":"2007","unstructured":"Zhang, P. et al. Hepatitis C virus epitope-specific neutralizing antibodies in Igs prepared from human plasma. Proc. Natl. Acad. Sci. USA 104, 8449\u20138454 (2007).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"69418_CR36","doi-asserted-by":"publisher","first-page":"7773","DOI":"10.1016\/j.vaccine.2007.08.053","volume":"25","author":"Z Stamataki","year":"2007","unstructured":"Stamataki, Z. et al. Hepatitis C virus envelope glycoprotein immunization of rodents elicits cross-reactive neutralizing antibodies. Vaccine 25, 7773\u20137784 (2007).","journal-title":"Vaccine"},{"key":"69418_CR37","doi-asserted-by":"publisher","first-page":"12473","DOI":"10.1128\/JVI.01138-09","volume":"83","author":"TJ Broering","year":"2009","unstructured":"Broering, T. J. et al. Identification and characterization of broadly neutralizing human monoclonal antibodies directed against the E2 envelope glycoprotein of hepatitis C virus. J. Virol. 83, 12473\u201312482 (2009).","journal-title":"J. Virol."},{"key":"69418_CR38","doi-asserted-by":"publisher","first-page":"966","DOI":"10.1128\/JVI.01872-07","volume":"82","author":"JC Meunier","year":"2008","unstructured":"Meunier, J. C. et al. Isolation and characterization of broadly neutralizing human monoclonal antibodies to the e1 glycoprotein of hepatitis C virus. J. Virol. 82, 966\u2013973 (2008).","journal-title":"J. Virol."},{"key":"69418_CR39","doi-asserted-by":"publisher","first-page":"10407","DOI":"10.1128\/JVI.74.22.10407-10416.2000","volume":"74","author":"KG Hadlock","year":"2000","unstructured":"Hadlock, K. G. et al. Human monoclonal antibodies that inhibit binding of hepatitis C virus E2 protein to CD81 and recognize conserved conformational epitopes. J. Virol. 74, 10407\u201310416 (2000).","journal-title":"J. Virol."},{"key":"69418_CR40","doi-asserted-by":"publisher","first-page":"1151","DOI":"10.3390\/v15051151","volume":"15","author":"E Gomez-Escobar","year":"2023","unstructured":"Gomez-Escobar, E., Roingeard, P. & Beaumont, E. Current hepatitis C vaccine candidates based on the induction of neutralizing antibodies. Viruses 15, 1151 (2023).","journal-title":"Viruses"},{"key":"69418_CR41","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":"69418_CR42","doi-asserted-by":"publisher","first-page":"1535","DOI":"10.1080\/14760584.2016.1194759","volume":"15","author":"C Fauvelle","year":"2016","unstructured":"Fauvelle, C. et al. Hepatitis C virus vaccine candidates inducing protective neutralizing antibodies. Expert Rev. Vaccines 15, 1535\u20131544 (2016).","journal-title":"Expert Rev. Vaccines"},{"key":"69418_CR43","doi-asserted-by":"publisher","first-page":"100","DOI":"10.1016\/j.antiviral.2014.02.013","volume":"105","author":"JK Ball","year":"2014","unstructured":"Ball, J. K., Tarr, A. W. & McKeating, J. A. The past, present and future of neutralizing antibodies for hepatitis C virus. Antiviral Res. 105, 100\u2013111 (2014).","journal-title":"Antiviral Res."},{"key":"69418_CR44","doi-asserted-by":"publisher","first-page":"369","DOI":"10.1111\/jvh.12094","volume":"20","author":"A Wahid","year":"2013","unstructured":"Wahid, A. & Dubuisson, J. Virus-neutralizing antibodies to hepatitis C virus. J. Viral Hepat. 20, 369\u2013376 (2013).","journal-title":"J. Viral Hepat."},{"key":"69418_CR45","doi-asserted-by":"publisher","first-page":"837","DOI":"10.3390\/v13050837","volume":"13","author":"JD Guest","year":"2021","unstructured":"Guest, J. D. & Pierce, B. G. Structure-based and rational design of a hepatitis C virus vaccine. Viruses 13, 837 (2021).","journal-title":"Viruses"},{"key":"69418_CR46","doi-asserted-by":"publisher","first-page":"1194","DOI":"10.3389\/fimmu.2018.01194","volume":"9","author":"ML Keck","year":"2018","unstructured":"Keck, M. L., Wrensch, F., Pierce, B. G., Baumert, T. F. & Foung, S. K. H. Mapping determinants of virus neutralization and viral escape for rational design of a hepatitis C virus vaccine. Front. Immunol. 9, 1194 (2018).","journal-title":"Front. Immunol."},{"key":"69418_CR47","doi-asserted-by":"publisher","first-page":"148","DOI":"10.1016\/j.coviro.2015.04.001","volume":"11","author":"L Kong","year":"2015","unstructured":"Kong, L., Jackson, K. N., Wilson, I. A. & Law, M. Capitalizing on knowledge of hepatitis C virus neutralizing epitopes for rational vaccine design. Curr. Opin. Virol. 11, 148\u2013157 (2015).","journal-title":"Curr. Opin. Virol."},{"key":"69418_CR48","doi-asserted-by":"publisher","first-page":"12923","DOI":"10.1128\/JVI.02052-12","volume":"86","author":"JA Potter","year":"2012","unstructured":"Potter, J. A. et al. Toward a hepatitis C virus vaccine: the structural basis of hepatitis C virus neutralization by AP33, a broadly neutralizing antibody. J. Virol. 86, 12923\u201312932 (2012).","journal-title":"J. Virol."},{"key":"69418_CR49","doi-asserted-by":"publisher","first-page":"9499","DOI":"10.1073\/pnas.1202924109","volume":"109","author":"L Kong","year":"2012","unstructured":"Kong, L. et al. Structural basis of hepatitis C virus neutralization by broadly neutralizing antibody HCV1. Proc. Natl. Acad. Sci. USA 109, 9499\u20139504 (2012).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"69418_CR50","doi-asserted-by":"publisher","first-page":"2617","DOI":"10.1016\/j.jmb.2015.06.012","volume":"427","author":"L Kong","year":"2015","unstructured":"Kong, L. et al. Structure of hepatitis C virus envelope glycoprotein E1 antigenic site 314-324 in complex with antibody IGH526. J. Mol. Biol. 427, 2617\u20132628 (2015).","journal-title":"J. Mol. Biol."},{"key":"69418_CR51","doi-asserted-by":"publisher","first-page":"2170","DOI":"10.1128\/JVI.02190-14","volume":"89","author":"A Meola","year":"2015","unstructured":"Meola, A. et al. Structural flexibility of a conserved antigenic region in hepatitis C virus glycoprotein E2 recognized by broadly neutralizing antibodies. J. Virol. 89, 2170\u20132181 (2015).","journal-title":"J. Virol."},{"key":"69418_CR52","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1003364","volume":"9","author":"T Krey","year":"2013","unstructured":"Krey, T. et al. Structural basis of HCV neutralization by human monoclonal antibodies resistant to viral neutralization escape. PLoS Pathog. 9, e1003364 (2013).","journal-title":"PLoS Pathog."},{"key":"69418_CR53","doi-asserted-by":"publisher","DOI":"10.1038\/srep12501","volume":"5","author":"L He","year":"2015","unstructured":"He, L. et al. Approaching rational epitope vaccine design for hepatitis C virus with meta-server and multivalent scaffolding. Sci. Rep. 5, 12501 (2015).","journal-title":"Sci. Rep."},{"key":"69418_CR54","doi-asserted-by":"publisher","DOI":"10.1126\/sciadv.ado2600","volume":"10","author":"K Nagarathinam","year":"2024","unstructured":"Nagarathinam, K. et al. Epitope-focused immunogens targeting the hepatitis C virus glycoproteins induce broadly neutralizing antibodies. Sci. Adv. 10, eado2600 (2024).","journal-title":"Sci. Adv."},{"key":"69418_CR55","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.01032-17","volume":"91","author":"BG Pierce","year":"2017","unstructured":"Pierce, B. G. et al. Structure-based design of hepatitis C virus vaccines that elicit neutralizing antibody responses to a conserved epitope. J. Virol. 91, e01032-17 (2017).","journal-title":"J. Virol."},{"key":"69418_CR56","doi-asserted-by":"publisher","first-page":"1090","DOI":"10.1126\/science.1243876","volume":"342","author":"L Kong","year":"2013","unstructured":"Kong, L. et al. Hepatitis C virus E2 envelope glycoprotein core structure. Science 342, 1090\u20131094 (2013).","journal-title":"Science"},{"key":"69418_CR57","doi-asserted-by":"publisher","first-page":"381","DOI":"10.1038\/nature13117","volume":"509","author":"AG Khan","year":"2014","unstructured":"Khan, A. G. et al. Structure of the core ectodomain of the hepatitis C virus envelope glycoprotein 2. Nature 509, 381\u2013384 (2014).","journal-title":"Nature"},{"key":"69418_CR58","doi-asserted-by":"publisher","first-page":"53","DOI":"10.1016\/j.coviro.2015.02.004","volume":"12","author":"AG Khan","year":"2015","unstructured":"Khan, A. G., Miller, M. T. & Marcotrigiano, J. HCV glycoprotein structures: what to expect from the unexpected. Curr. Opin. Virol. 12, 53\u201358 (2015).","journal-title":"Curr. Opin. Virol."},{"key":"69418_CR59","doi-asserted-by":"publisher","first-page":"703","DOI":"10.1016\/j.chom.2018.10.009","volume":"24","author":"AI Flyak","year":"2018","unstructured":"Flyak, A. I. et al. HCV broadly neutralizing antibodies use a CDRH3 disulfide motif to recognize an E2 glycoprotein site that can be targeted for vaccine design. Cell Host Microbe 24, 703\u2013716.e3 (2018).","journal-title":"Cell Host Microbe"},{"key":"69418_CR60","doi-asserted-by":"publisher","first-page":"1315","DOI":"10.3389\/fimmu.2018.01315","volume":"9","author":"N Tzarum","year":"2018","unstructured":"Tzarum, N., Wilson, I. A. & Law, M. The neutralizing face of hepatitis C virus E2 envelope glycoprotein. Front. Immunol. 9, 1315 (2018).","journal-title":"Front. Immunol."},{"key":"69418_CR61","doi-asserted-by":"publisher","first-page":"2692","DOI":"10.3389\/fmicb.2017.02692","volume":"8","author":"TR Fuerst","year":"2018","unstructured":"Fuerst, T. R., Pierce, B. G., Keck, Z. Y. & Foung, S. K. H. Designing a B cell-based vaccine against a highly variable hepatitis C virus. Front. Microbiol. 8, 2692 (2018).","journal-title":"Front. Microbiol."},{"key":"69418_CR62","doi-asserted-by":"publisher","first-page":"a036962","DOI":"10.1101\/cshperspect.a036962","volume":"11","author":"M Law","year":"2021","unstructured":"Law, M. Antibody responses in hepatitis C infection. Cold Spring Harb. Perspect. Med. 11, a036962 (2021).","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"69418_CR63","doi-asserted-by":"publisher","DOI":"10.1126\/sciadv.aav1882","volume":"5","author":"N Tzarum","year":"2019","unstructured":"Tzarum, N. et al. Genetic and structural insights into broad neutralization of hepatitis C virus by human VH1-69 antibodies. Sci. Adv. 5, eaav1882 (2019).","journal-title":"Sci. Adv."},{"key":"69418_CR64","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-023-39690-0","volume":"14","author":"J Capella-Pujol","year":"2023","unstructured":"Capella-Pujol, J. et al. Signatures of VH1-69-derived hepatitis C virus neutralizing antibody precursors defined by binding to envelope glycoproteins. Nat. Commun. 14, 4036 (2023).","journal-title":"Nat. Commun."},{"key":"69418_CR65","doi-asserted-by":"publisher","first-page":"341","DOI":"10.1016\/j.immuni.2021.12.003","volume":"55","author":"T Weber","year":"2022","unstructured":"Weber, T. et al. Analysis of antibodies from HCV elite neutralizers identifies genetic determinants of broad neutralization. Immunity 55, 341\u2013354.e7 (2022).","journal-title":"Immunity"},{"key":"69418_CR66","doi-asserted-by":"publisher","first-page":"781","DOI":"10.1016\/j.immuni.2021.02.013","volume":"54","author":"F Chen","year":"2021","unstructured":"Chen, F. et al. Functional convergence of a germline-encoded neutralizing antibody response in rhesus macaques immunized with HCV envelope glycoproteins. Immunity 54, 781\u2013796.e4 (2021).","journal-title":"Immunity"},{"key":"69418_CR67","doi-asserted-by":"publisher","DOI":"10.1126\/sciadv.abb5642","volume":"6","author":"N Tzarum","year":"2020","unstructured":"Tzarum, N. et al. An alternate conformation of HCV E2 neutralizing face as an additional vaccine target. Sci. Adv. 6, eabb5642 (2020).","journal-title":"Sci. Adv."},{"key":"69418_CR68","doi-asserted-by":"publisher","DOI":"10.1126\/sciadv.aaz6225","volume":"6","author":"LL He","year":"2020","unstructured":"He, L. L. et al. Proof of concept for rational design of hepatitis C virus E2 core nanoparticle vaccines. Sci. Adv. 6, eaaz6225 (2020).","journal-title":"Sci. Adv."},{"key":"69418_CR69","first-page":"1304","volume":"221","author":"Y Yan","year":"2020","unstructured":"Yan, Y. et al. A nanoparticle-based HCV vaccine with enhanced potency. J. Infect. Dis. 221, 1304\u20131314 (2020).","journal-title":"J. Infect. Dis."},{"key":"69418_CR70","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.00704-20","volume":"94","author":"BG Pierce","year":"2020","unstructured":"Pierce, B. G. et al. Structure-based design of hepatitis C virus E2 glycoprotein improves serum binding and cross-neutralization. J. Virol. 94, e00704-20 (2020).","journal-title":"J. Virol."},{"key":"69418_CR71","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-023-39659-z","volume":"14","author":"MC Metcalf","year":"2023","unstructured":"Metcalf, M. C. et al. Structure of engineered hepatitis C virus E1E2 ectodomain in complex with neutralizing antibodies. Nat. Commun. 14, 3980 (2023).","journal-title":"Nat. Commun."},{"key":"69418_CR72","doi-asserted-by":"publisher","first-page":"263","DOI":"10.1126\/science.abn9884","volume":"378","author":"AT de la Pe\u00f1a","year":"2022","unstructured":"de la Pe\u00f1a, A. T. et al. Structure of the hepatitis C virus E1E2 glycoprotein complex. Science 378, 263\u2013269 (2022).","journal-title":"Science"},{"key":"69418_CR73","doi-asserted-by":"publisher","first-page":"704","DOI":"10.1038\/s41586-024-07783-5","volume":"633","author":"EH Augestad","year":"2024","unstructured":"Augestad, E. H. et al. The hepatitis C virus envelope protein complex is a dimer of heterodimers. Nature 633, 704\u2013709 (2024).","journal-title":"Nature"},{"key":"69418_CR74","doi-asserted-by":"publisher","first-page":"803","DOI":"10.3390\/v16050803","volume":"16","author":"BG Pierce","year":"2024","unstructured":"Pierce, B. G. et al. Hepatitis C virus E1E2 structure, diversity, and implications for vaccine development. Viruses 16, 803 (2024).","journal-title":"Viruses"},{"key":"69418_CR75","doi-asserted-by":"publisher","first-page":"1337","DOI":"10.3390\/v16081337","volume":"16","author":"AR Garbuglia","year":"2024","unstructured":"Garbuglia, A. R., Pauciullo, S., Zulian, V. & Del Porto, P. Update on hepatitis C vaccine: results and challenges. Viruses 16, 1337 (2024).","journal-title":"Viruses"},{"key":"69418_CR76","doi-asserted-by":"publisher","DOI":"10.1002\/rmv.2474","volume":"33","author":"EA Toth","year":"2023","unstructured":"Toth, E. A., Andrianov, A. K. & Fuerst, T. R. Prospects for developing an hepatitis C virus E1E2-based nanoparticle vaccine. Rev. Med. Virol. 33, e2474 (2023).","journal-title":"Rev. Med. Virol."},{"key":"69418_CR77","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2015149118","volume":"118","author":"JD Guest","year":"2021","unstructured":"Guest, J. D. et al. Design of a native-like secreted form of the hepatitis C virus E1E2 heterodimer. Proc. Natl. Acad. Sci. USA 118, e2015149118 (2021).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"69418_CR78","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2112008119","volume":"119","author":"RX Wang","year":"2022","unstructured":"Wang, R. X. et al. Induction of broadly neutralizing antibodies using a secreted form of the hepatitis C virus E1E2 heterodimer as a vaccine candidate. Proc. Natl. Acad. Sci. USA 119, e2112008119 (2022).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"69418_CR79","doi-asserted-by":"publisher","first-page":"34","DOI":"10.3390\/jfb16010034","volume":"16","author":"TR Fuerst","year":"2025","unstructured":"Fuerst, T. R. et al. Virus-mimicking polymer nanocomplexes co-assembling HCV E1E2 and core proteins with TLR 7\/8 agonist-synthesis, characterization, and in vivo activity. J. Funct. Biomater. 16, 34 (2025).","journal-title":"J. Funct. Biomater."},{"key":"69418_CR80","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-022-34961-8","volume":"13","author":"K Sliepen","year":"2022","unstructured":"Sliepen, K. et al. Induction of cross-neutralizing antibodies by a permuted hepatitis C virus glycoprotein nanoparticle vaccine candidate. Nat. Commun. 13, 7271 (2022).","journal-title":"Nat. Commun."},{"key":"69418_CR81","doi-asserted-by":"publisher","first-page":"189","DOI":"10.1080\/10409230802058320","volume":"43","author":"JM White","year":"2008","unstructured":"White, J. M., Delos, S. E., Brecher, M. & Schornberg, K. Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme. Crit. Rev. Biochem. Mol. Biol. 43, 189\u2013219 (2008).","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"69418_CR82","doi-asserted-by":"publisher","first-page":"690","DOI":"10.1038\/nsmb.1456","volume":"15","author":"SC Harrison","year":"2008","unstructured":"Harrison, S. C. Viral membrane fusion. Nat. Struct. Mol. Biol. 15, 690\u2013698 (2008).","journal-title":"Nat. Struct. Mol. Biol."},{"key":"69418_CR83","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-023-37742-z","volume":"14","author":"YN Zhang","year":"2023","unstructured":"Zhang, Y.-N. et al. Single-component multilayered self-assembling protein nanoparticles presenting glycan-trimmed uncleaved prefusion optimized envelope trimmers as HIV-1 vaccine candidates. Nat. Commun. 14, 1985 (2023).","journal-title":"Nat. Commun."},{"key":"69418_CR84","doi-asserted-by":"publisher","DOI":"10.1126\/sciadv.aau6769","volume":"4","author":"L He","year":"2018","unstructured":"He, L. et al. HIV-1 vaccine design through minimizing envelope metastability. Sci. Adv. 4, eaau6769 (2018).","journal-title":"Sci. Adv."},{"key":"69418_CR85","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms12040","volume":"7","author":"L Kong","year":"2016","unstructured":"Kong, L. et al. Uncleaved prefusion-optimized gp140 trimers derived from analysis of HIV-1 envelope metastability. Nat. Commun. 7, 12040 (2016).","journal-title":"Nat. Commun."},{"key":"69418_CR86","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-025-66367-7","volume":"16","author":"Y-Z Lee","year":"2025","unstructured":"Lee, Y.-Z. et al. Rational design of next-generation filovirus vaccines combining glycoprotein stabilization and nanoparticle display with glycan modification. Nat. Commun. 16, 11368 (2025).","journal-title":"Nat. Commun."},{"key":"69418_CR87","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-021-22867-w","volume":"12","author":"LL He","year":"2021","unstructured":"He, L. L. et al. Single-component multilayered self-assembling nanoparticles presenting rationally designed glycoprotein trimers as Ebola virus vaccines. Nat. Commun. 12, 2633 (2021).","journal-title":"Nat. Commun."},{"key":"69418_CR88","doi-asserted-by":"publisher","DOI":"10.1126\/sciadv.abf1591","volume":"7","author":"LL He","year":"2021","unstructured":"He, L. L. et al. Single-component, self-assembling, protein nanoparticles presenting the receptor binding domain and stabilized spike as SARS-CoV-2 vaccine candidates. Sci. Adv. 7, eabf1591 (2021).","journal-title":"Sci. Adv."},{"key":"69418_CR89","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-024-54287-x","volume":"15","author":"YZ Lee","year":"2024","unstructured":"Lee, Y.-Z. et al. Rational design of uncleaved prefusion-closed trimer vaccines for human respiratory syncytial virus and metapneumovirus. Nat. Commun. 15, 9939 (2024).","journal-title":"Nat. Commun."},{"key":"69418_CR90","doi-asserted-by":"publisher","first-page":"975","DOI":"10.3390\/vaccines12090975","volume":"12","author":"YN Zhang","year":"2024","unstructured":"Zhang, Y.-N. et al. A single-component multilayered self-assembling protein nanoparticle vaccine based on extracellular domains of matrix protein 2 against both influenza A and B. Vaccines 12, 975 (2024).","journal-title":"Vaccines"},{"key":"69418_CR91","doi-asserted-by":"publisher","first-page":"23545","DOI":"10.1021\/acsnano.3c06526","volume":"17","author":"KB Gomes","year":"2023","unstructured":"Gomes, K. B. et al. Single-component multilayered self-assembling protein nanoparticles displaying extracellular domains of matrix protein 2 as a pan-influenza A vaccine. ACS Nano 17, 23545\u201323567 (2023).","journal-title":"ACS Nano"},{"key":"69418_CR92","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms12041","volume":"7","author":"L He","year":"2016","unstructured":"He, L. et al. Presenting native-like trimeric HIV-1 antigens with self-assembling nanoparticles. Nat. Commun. 7, 12041 (2016).","journal-title":"Nat. Commun."},{"key":"69418_CR93","doi-asserted-by":"publisher","DOI":"10.1038\/s41541-025-01161-6","volume":"10","author":"L Kulakova","year":"2025","unstructured":"Kulakova, L. et al. Glycoengineering of the hepatitis C virus E2 glycoprotein improves biochemical properties and enhances immunogenicity. Npj Vaccines 10, 121 (2025).","journal-title":"Npj Vaccines"},{"key":"69418_CR94","doi-asserted-by":"publisher","first-page":"E690","DOI":"10.1073\/pnas.1115485109","volume":"109","author":"B Zakeri","year":"2012","unstructured":"Zakeri, B. et al. Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin. Proc. Natl. Acad. Sci. USA 109, E690\u2013E697 (2012).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"69418_CR95","doi-asserted-by":"publisher","first-page":"5","DOI":"10.1002\/hep.20032","volume":"39","author":"F Penin","year":"2004","unstructured":"Penin, F., Dubuisson, J., Rey, F. A., Moradpour, D. & Pawlotsky, J. M. Structural biology of hepatitis C virus. Hepatology 39, 5\u201319 (2004).","journal-title":"Hepatology"},{"key":"69418_CR96","doi-asserted-by":"publisher","first-page":"6367","DOI":"10.1016\/j.vaccine.2010.06.084","volume":"28","author":"SE Frey","year":"2010","unstructured":"Frey, S. E. et al. Safety and immunogenicity of HCV E1E2 vaccine adjuvanted with MF59 administered to healthy adults. Vaccine 28, 6367\u20136373 (2010).","journal-title":"Vaccine"},{"key":"69418_CR97","doi-asserted-by":"publisher","first-page":"257","DOI":"10.1038\/373257a0","volume":"373","author":"JNM Glover","year":"1995","unstructured":"Glover, J. N. M. & Harrison, S. C. Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA. Nature 373, 257\u2013261 (1995).","journal-title":"Nature"},{"key":"69418_CR98","doi-asserted-by":"publisher","first-page":"118","DOI":"10.1021\/sb200015u","volume":"1","author":"KE Thompson","year":"2012","unstructured":"Thompson, K. E., Bashor, C. J., Lim, W. A. & Keating, A. E. SynZIP protein interaction toolbox: in vitro and in vivo specifications of heterospecific coiled-coil interaction domains. ACS Synth. Biol. 1, 118\u2013129 (2012).","journal-title":"ACS Synth. Biol."},{"key":"69418_CR99","doi-asserted-by":"publisher","first-page":"12436","DOI":"10.1021\/bi048771t","volume":"43","author":"DN Marti","year":"2004","unstructured":"Marti, D. N. & Bosshard, H. R. Inverse electrostatic effect: electrostatic repulsion in the unfolded state stabilizes a leucine zipper. Biochemistry 43, 12436\u201312447 (2004).","journal-title":"Biochemistry"},{"key":"69418_CR100","doi-asserted-by":"publisher","first-page":"367","DOI":"10.1002\/bip.20150","volume":"75","author":"DA Lindhout","year":"2004","unstructured":"Lindhout, D. A., Litowski, J. R., Mercier, P., Hodges, R. S. & Sykes, B. D. NMR solution structure of a highly stable de novo heterodimeric coiled-coil. Biopolymers 75, 367\u2013375 (2004).","journal-title":"Biopolymers"},{"key":"69418_CR101","doi-asserted-by":"publisher","first-page":"180","DOI":"10.1016\/S0958-1669(00)00197-X","volume":"12","author":"L Chu","year":"2001","unstructured":"Chu, L. & Robinson, D. K. Industrial choices for protein production by large-scale cell culture. Curr. Opin. Biotechnol. 12, 180\u2013187 (2001).","journal-title":"Curr. Opin. Biotechnol."},{"key":"69418_CR102","doi-asserted-by":"publisher","first-page":"474","DOI":"10.3892\/etm.2022.11401","volume":"24","author":"QQ Zhao","year":"2022","unstructured":"Zhao, Q. Q. et al. Production and immunogenicity of different prophylactic vaccines for hepatitis C virus (Review). Exp. Ther. Med. 24, 474 (2022).","journal-title":"Exp. Ther. Med."},{"key":"69418_CR103","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1016\/j.tibtech.2010.02.001","volume":"28","author":"AA Shukla","year":"2010","unstructured":"Shukla, A. A. & Th\u00f6mmes, J. Recent advances in large-scale production of monoclonal antibodies and related proteins. Trends Biotechnol. 28, 253\u2013261 (2010).","journal-title":"Trends Biotechnol."},{"key":"69418_CR104","doi-asserted-by":"publisher","first-page":"3288","DOI":"10.1128\/JVI.02700-15","volume":"90","author":"RA Urbanowicz","year":"2016","unstructured":"Urbanowicz, R. A. et al. A diverse panel of hepatitis C virus glycoproteins for use in vaccine research reveals extremes of monoclonal antibody neutralization resistance. J. Virol. 90, 3288\u20133301 (2016).","journal-title":"J. Virol."},{"key":"69418_CR105","doi-asserted-by":"publisher","first-page":"6101","DOI":"10.1002\/anie.201402519","volume":"53","author":"C Schoene","year":"2014","unstructured":"Schoene, C., Fierer, J. O., Bennett, S. P. & Howarth, M. SpyTag\/SpyCatcher cyclization confers resilience to boiling on a mesophilic enzyme. Angew. Chem. Int. Ed. 53, 6101\u20136104 (2014).","journal-title":"Angew. Chem. Int. Ed."},{"key":"69418_CR106","doi-asserted-by":"publisher","first-page":"910","DOI":"10.3389\/fimmu.2018.00910","volume":"9","author":"M Lavie","year":"2018","unstructured":"Lavie, M., Hanoulle, X. & Dubuisson, J. Glycan shielding and modulation of hepatitis C virus neutralizing antibodies. Front. Immunol. 9, 910 (2018).","journal-title":"Front. Immunol."},{"key":"69418_CR107","doi-asserted-by":"publisher","first-page":"1909","DOI":"10.3390\/v3101909","volume":"3","author":"F Helle","year":"2011","unstructured":"Helle, F., Duverlie, G. & Dubuisson, J. The hepatitis C virus glycan shield and evasion of the humoral immune response. Viruses 3, 1909\u20131932 (2011).","journal-title":"Viruses"},{"key":"69418_CR108","doi-asserted-by":"publisher","first-page":"e1006735","DOI":"10.1371\/journal.ppat.1006735","volume":"13","author":"R Gopal","year":"2017","unstructured":"Gopal, R. et al. Probing the antigenicity of hepatitis C virus envelope glycoprotein complex by high-throughput mutagenesis. PLoS Pathog. 13, e1006735 (2017).","journal-title":"PLoS Pathog."},{"key":"69418_CR109","doi-asserted-by":"publisher","first-page":"290","DOI":"10.1038\/nmeth.4169","volume":"14","author":"A Punjani","year":"2017","unstructured":"Punjani, A., Rubinstein, J. L., Fleet, D. J. & Brubaker, M. A. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination. Nat. Methods 14, 290\u2013296 (2017).","journal-title":"Nat. Methods"},{"key":"69418_CR110","doi-asserted-by":"publisher","first-page":"14","DOI":"10.1016\/j.jhep.2019.02.013","volume":"71","author":"SJ Merat","year":"2019","unstructured":"Merat, S. J. et al. Cross-genotype AR3-specific neutralizing antibodies confer long-term protection in injecting drug users after HCV clearance. J. Hepatol. 71, 14\u201324 (2019).","journal-title":"J. Hepatol."},{"key":"69418_CR111","doi-asserted-by":"publisher","DOI":"10.1126\/sciadv.abj3107","volume":"7","author":"YN Zhang","year":"2021","unstructured":"Zhang, Y.-N. et al. Mechanism of a COVID-19 nanoparticle vaccine candidate that elicits a broadly neutralizing antibody response to SARS-CoV-2 variants. Sci. Adv. 7, eabj3107 (2021).","journal-title":"Sci. Adv."},{"key":"69418_CR112","doi-asserted-by":"publisher","first-page":"562","DOI":"10.1053\/j.gastro.2021.10.005","volume":"162","author":"JH Salas","year":"2022","unstructured":"Salas, J. H. et al. An antigenically diverse, representative panel of envelope glycoproteins for hepatitis C virus vaccine development. Gastroenterology 162, 562\u2013574 (2022).","journal-title":"Gastroenterology"},{"key":"69418_CR113","doi-asserted-by":"publisher","first-page":"37","DOI":"10.1038\/s41581-023-00787-w","volume":"20","author":"SE Dunn","year":"2024","unstructured":"Dunn, S. E., Perry, W. A. & Klein, S. L. Mechanisms and consequences of sex differences in immune responses. Nat. Rev. Nephrol. 20, 37\u201355 (2024).","journal-title":"Nat. Rev. Nephrol."},{"key":"69418_CR114","doi-asserted-by":"publisher","first-page":"626","DOI":"10.1038\/nri.2016.90","volume":"16","author":"SL Klein","year":"2016","unstructured":"Klein, S. L. & Flanagan, K. L. Sex differences in immune responses. Nat. Rev. Immunol. 16, 626\u2013638 (2016).","journal-title":"Nat. Rev. Immunol."},{"key":"69418_CR115","doi-asserted-by":"publisher","first-page":"720952","DOI":"10.3389\/fimmu.2021.720952","volume":"12","author":"H Jacobsen","year":"2021","unstructured":"Jacobsen, H. & Klein, S. L. Sex differences in immunity to viral infections. Front. Immunol. 12, 720952 (2021).","journal-title":"Front. Immunol."},{"key":"69418_CR116","doi-asserted-by":"publisher","first-page":"1396","DOI":"10.3389\/fimmu.2018.01396","volume":"9","author":"LJ Stroh","year":"2018","unstructured":"Stroh, L. J., Nagarathinam, K. & Krey, T. Conformational flexibility in the CD81-bindingsite of the hepatitis C virus glycoprotein E2. Front. Immunol. 9, 1396 (2018).","journal-title":"Front. Immunol."},{"key":"69418_CR117","doi-asserted-by":"publisher","first-page":"521","DOI":"10.1038\/s41586-021-03913-5","volume":"598","author":"A Kumar","year":"2021","unstructured":"Kumar, A. et al. Structural insights into hepatitis C virus receptor binding and entry. Nature 598, 521\u2013525 (2021).","journal-title":"Nature"},{"key":"69418_CR118","unstructured":"World Health Organization. Accelerating Access to Hepatitis C Diagnostics and Treatment: Global Progress Report 2020 (World Health Organization, 2021)."},{"key":"69418_CR119","doi-asserted-by":"publisher","first-page":"S58","DOI":"10.1016\/j.jhep.2014.07.012","volume":"61","author":"RH Westbrook","year":"2014","unstructured":"Westbrook, R. H. & Dusheiko, G. Natural history of hepatitis C. J. Hepatol. 61, S58\u2013S68 (2014).","journal-title":"J. Hepatol."},{"key":"69418_CR120","doi-asserted-by":"publisher","first-page":"1169","DOI":"10.1056\/NEJMp1716871","volume":"378","author":"TJ Liang","year":"2018","unstructured":"Liang, T. J. & Ward, J. W. Hepatitis C in Injection-drug Users - A Hidden Danger Of The Opioid Epidemic. N. Engl. J. Med. 378, 1169\u20131171 (2018).","journal-title":"N. Engl. J. Med."},{"key":"69418_CR121","doi-asserted-by":"publisher","first-page":"322","DOI":"10.1016\/j.coviro.2013.05.010","volume":"3","author":"DW Kulp","year":"2013","unstructured":"Kulp, D. W. & Schief, W. R. Advances in structure-based vaccine design. Curr. Opin. Virol. 3, 322\u2013331 (2013).","journal-title":"Curr. Opin. Virol."},{"key":"69418_CR122","doi-asserted-by":"publisher","first-page":"579","DOI":"10.1056\/NEJMp2216358","volume":"388","author":"BS Graham","year":"2023","unstructured":"Graham, B. S. The journey to RSV vaccines - heralding an era of structure-based design. N. Engl. J. Med. 388, 579\u2013581 (2023).","journal-title":"N. Engl. J. Med."},{"key":"69418_CR123","doi-asserted-by":"publisher","first-page":"91","DOI":"10.1146\/annurev-med-121217-094234","volume":"70","author":"BS Graham","year":"2019","unstructured":"Graham, B. S., Gilman, M. S. A. & McLellan, J. S. Structure-based vaccine antigen design. Annu. Rev. Med. 70, 91\u2013104 (2019).","journal-title":"Annu. Rev. Med."},{"key":"69418_CR124","doi-asserted-by":"publisher","DOI":"10.1002\/jia2.25797","volume":"24","author":"R Derking","year":"2021","unstructured":"Derking, R. & Sanders, R. W. Structure-guided envelope trimer design in HIV-1 vaccine development: a narrative review. J. Int. AIDS Soc. 24, e25797 (2021).","journal-title":"J. Int. AIDS Soc."},{"key":"69418_CR125","doi-asserted-by":"publisher","DOI":"10.1038\/s41541-021-00330-7","volume":"6","author":"B Nguyen","year":"2021","unstructured":"Nguyen, B. & Tolia, N. H. Protein-based antigen presentation platforms for nanoparticle vaccines. Npj Vaccines 6, 70 (2021).","journal-title":"Npj Vaccines"},{"key":"69418_CR126","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.coi.2020.01.007","volume":"65","author":"DJ Irvine","year":"2020","unstructured":"Irvine, D. J. & Read, B. J. Shaping humoral immunity to vaccines through antigen-displaying nanoparticles. Curr. Opin. Immunol. 65, 1\u20136 (2020).","journal-title":"Curr. Opin. Immunol."},{"key":"69418_CR127","doi-asserted-by":"publisher","first-page":"1245","DOI":"10.1016\/j.cell.2019.02.008","volume":"176","author":"R Rappuoli","year":"2019","unstructured":"Rappuoli, R. & Serruto, D. Self-assembling nanoparticles usher in a new era of vaccine design. Cell 176, 1245\u20131247 (2019).","journal-title":"Cell"},{"key":"69418_CR128","doi-asserted-by":"publisher","first-page":"2577","DOI":"10.1002\/bip.360221211","volume":"22","author":"W Kabsch","year":"1983","unstructured":"Kabsch, W. & Sander, C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577\u20132637 (1983).","journal-title":"Biopolymers"},{"key":"69418_CR129","doi-asserted-by":"publisher","first-page":"161092","DOI":"10.1098\/rsos.161092","volume":"4","author":"G Indelicato","year":"2017","unstructured":"Indelicato, G., Burkhard, P. & Twarock, R. Classification of self-assembling protein nanoparticle architectures for applications in vaccine design. R. Soc. Open Sci. 4, 161092 (2017).","journal-title":"R. Soc. Open Sci."},{"key":"69418_CR130","doi-asserted-by":"publisher","first-page":"1058","DOI":"10.1053\/j.gastro.2019.11.282","volume":"158","author":"F Chen","year":"2020","unstructured":"Chen, F. et al. Antibody responses to immunization with HCV envelope glycoproteins as a baseline for B-cell-based vaccine development. Gastroenterology 158, 1058\u20131071.e6 (2020).","journal-title":"Gastroenterology"},{"key":"69418_CR131","doi-asserted-by":"publisher","first-page":"288","DOI":"10.1016\/j.immuni.2018.07.009","volume":"49","author":"M Bianchi","year":"2018","unstructured":"Bianchi, M. et al. Electron-microscopy-based epitope mapping defines specificities of polyclonal antibodies elicited during HIV-1 BG505 envelope trimer immunization. Immunity 49, 288\u2013300.e8 (2018).","journal-title":"Immunity"},{"key":"69418_CR132","doi-asserted-by":"publisher","first-page":"18137","DOI":"10.1073\/pnas.0909696106","volume":"106","author":"CC Wang","year":"2009","unstructured":"Wang, C. C. et al. Glycans on influenza hemagglutinin affect receptor binding and immune response. Proc. Natl. Acad. Sci. USA 106, 18137\u201318142 (2009).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"69418_CR133","doi-asserted-by":"publisher","DOI":"10.1126\/scitranslmed.abm0899","volume":"14","author":"HY Huang","year":"2022","unstructured":"Huang, H. Y. et al. Vaccination with SARS-CoV-2 spike protein lacking glycan shields elicits enhanced protective responses in animal models. Sci. Transl. Med. 14, eabm0899 (2022).","journal-title":"Sci. Transl. Med."},{"key":"69418_CR134","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-020-78425-9","volume":"10","author":"J Korn","year":"2020","unstructured":"Korn, J. et al. Baculovirus-free insect cell expression system for high yield antibody and antigen production. Sci. Rep. 10, 21393 (2020).","journal-title":"Sci. Rep."},{"key":"69418_CR135","doi-asserted-by":"publisher","first-page":"1204834","DOI":"10.3389\/fimmu.2023.1204834","volume":"14","author":"M Gonzalez-Hernandez","year":"2023","unstructured":"Gonzalez-Hernandez, M. et al. Preclinical immunogenicity and protective efficacy of a SARS-CoV-2 RBD-based vaccine produced with the thermophilic filamentous fungal expression system Thermothelomyces heterothallica C1. Front. Immunol. 14, 1204834 (2023).","journal-title":"Front. Immunol."},{"key":"69418_CR136","doi-asserted-by":"publisher","first-page":"1162","DOI":"10.1016\/j.vaccine.2022.01.007","volume":"40","author":"L Lazo","year":"2022","unstructured":"Lazo, L. et al. A recombinant SARS-CoV-2 receptor-binding domain expressed in an engineered fungal strain of Thermothelomyces heterothallica induces a functional immune response in mice. Vaccine 40, 1162\u20131169 (2022).","journal-title":"Vaccine"},{"key":"69418_CR137","doi-asserted-by":"publisher","first-page":"a036970","DOI":"10.1101\/cshperspect.a036970","volume":"10","author":"A Ploss","year":"2020","unstructured":"Ploss, A. & Kapoor, A. Animal models of hepatitis C virus infection. Cold Spring Harb. Perspect. Med. 10, a036970 (2020).","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"69418_CR138","doi-asserted-by":"publisher","first-page":"1032","DOI":"10.3389\/fimmu.2018.01032","volume":"9","author":"R Burm","year":"2018","unstructured":"Burm, R., Collignon, L., Mesalam, A. A. & Meuleman, P. Animal models to study hepatitis C virus infection. Front. Immunol. 9, 1032 (2018).","journal-title":"Front. Immunol."},{"key":"69418_CR139","doi-asserted-by":"publisher","first-page":"604","DOI":"10.3390\/cells8060604","volume":"8","author":"KSM Yong","year":"2019","unstructured":"Yong, K. S. M., Her, Z. & Chen, Q. F. Humanized mouse models for the study of hepatitis C and host interactions. Cells 8, 604 (2019).","journal-title":"Cells"},{"key":"69418_CR140","doi-asserted-by":"publisher","first-page":"176","DOI":"10.3390\/v8060176","volume":"8","author":"AA Mesalam","year":"2016","unstructured":"Mesalam, A. A., Vercauteren, K. & Meuleman, P. Mouse systems to model hepatitis C virus treatment and associated resistance. Viruses 8, 176 (2016).","journal-title":"Viruses"},{"key":"69418_CR141","doi-asserted-by":"publisher","first-page":"890","DOI":"10.3390\/vaccines12080890","volume":"12","author":"GL Costa","year":"2024","unstructured":"Costa, G. L. & Sautto, G. A. Exploring T-cell immunity to hepatitis C virus: insights from different vaccine and antigen presentation strategies. Vaccines 12, 890 (2024).","journal-title":"Vaccines"},{"key":"69418_CR142","doi-asserted-by":"publisher","first-page":"220","DOI":"10.1016\/j.jhep.2020.09.022","volume":"74","author":"R Thimme","year":"2021","unstructured":"Thimme, R. T cell immunity to hepatitis C virus: lessons for a prophylactic vaccine. J. Hepatol. 74, 220\u2013229 (2021).","journal-title":"J. Hepatol."},{"key":"69418_CR143","doi-asserted-by":"publisher","first-page":"1605","DOI":"10.1002\/jcc.20084","volume":"25","author":"EF Pettersen","year":"2004","unstructured":"Pettersen, E. F. et al. UCSF chimera - a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605\u20131612 (2004).","journal-title":"J. Comput. Chem."},{"key":"69418_CR144","doi-asserted-by":"publisher","first-page":"1214","DOI":"10.1038\/s41592-020-00990-8","volume":"17","author":"A Punjani","year":"2020","unstructured":"Punjani, A., Zhang, H. W. & Fleet, D. J. Non-uniform refinement: adaptive regularization improves single-particle cryo-EM reconstruction. Nat. Methods 17, 1214\u20131221 (2020).","journal-title":"Nat. Methods"},{"key":"69418_CR145","doi-asserted-by":"publisher","first-page":"38","DOI":"10.1016\/j.jsb.2006.05.009","volume":"157","author":"G Tang","year":"2007","unstructured":"Tang, G. et al. EMAN2: An extensible image processing suite for electron microscopy. J. Struct. Biol. 157, 38\u201346 (2007).","journal-title":"J. Struct. Biol."},{"key":"69418_CR146","doi-asserted-by":"publisher","DOI":"10.1002\/pro.4792","volume":"32","author":"EC Meng","year":"2023","unstructured":"Meng, E. C. et al. UCSF ChimeraX: tools for structure building and analysis. Protein Sci. 32, e4792 (2023).","journal-title":"Protein Sci."}],"updated-by":[{"DOI":"10.1038\/s41467-026-76171-6","type":"correction","label":"Correction","source":"publisher","updated":{"date-parts":[[2026,8,13]],"date-time":"2026-08-13T00:00:00Z","timestamp":1786579200000}}],"container-title":["Nature Communications"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41467-026-69418-9","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41467-026-69418-9.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41467-026-69418-9.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,14]],"date-time":"2026-08-14T07:02:43Z","timestamp":1786690963000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41467-026-69418-9"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,2,11]]},"references-count":146,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2026,12]]}},"alternative-id":["69418"],"URL":"https:\/\/doi.org\/10.1038\/s41467-026-69418-9","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/2025.05.16.654559","asserted-by":"object"}]},"ISSN":["2041-1723"],"issn-type":[{"value":"2041-1723","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,2,11]]},"assertion":[{"value":"22 May 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"30 January 2026","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"11 February 2026","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"13 August 2026","order":6,"name":"change_date","label":"Change Date","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"Correction","order":7,"name":"change_type","label":"Change Type","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"A Correction to this paper has been published:","order":8,"name":"change_details","label":"Change Details","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"https:\/\/doi.org\/10.1038\/s41467-026-76171-6","URL":"https:\/\/doi.org\/10.1038\/s41467-026-76171-6","order":9,"name":"change_details","label":"Change Details","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"J.Z. is the Co-Founder and a Scientific Advisory Board member of Uvax Bio, LLC, and holds associated financial interests. T.R.F. serves as Co-Founder and Chairman of NeuImmune, Inc., and holds associated financial interests. All other authors declare no competing interests.","order":1,"name":"Ethics","label":"Competing interests","group":{"name":"EthicsHeading","label":"Ethics"}}],"article-number":"2633"}}