{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,24]],"date-time":"2026-10-24T11:01:38Z","timestamp":1792839698316,"version":"4.5.0"},"reference-count":56,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,8,1]],"date-time":"2021-08-01T00:00:00Z","timestamp":1627776000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,8,1]],"date-time":"2021-08-01T00:00:00Z","timestamp":1627776000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,6,3]],"date-time":"2022-06-03T00:00:00Z","timestamp":1654214400000},"content-version":"am","delay-in-days":306,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,8,1]],"date-time":"2021-08-01T00:00:00Z","timestamp":1627776000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2021,8,1]],"date-time":"2021-08-01T00:00:00Z","timestamp":1627776000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2021,8,1]],"date-time":"2021-08-01T00:00:00Z","timestamp":1627776000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2021,8,1]],"date-time":"2021-08-01T00:00:00Z","timestamp":1627776000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2021,8,1]],"date-time":"2021-08-01T00:00:00Z","timestamp":1627776000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["R21-AI126582"],"award-info":[{"award-number":["R21-AI126582"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["HHSN272201700060 C"],"award-info":[{"award-number":["HHSN272201700060 C"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Current Opinion in Virology"],"published-print":{"date-parts":[[2021,8]]},"DOI":"10.1016\/j.coviro.2021.05.002","type":"journal-article","created":{"date-parts":[[2021,6,3]],"date-time":"2021-06-03T11:35:59Z","timestamp":1622720159000},"page":"92-101","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":21,"special_numbering":"C","title":["Structural perspectives on HCV humoral immune evasion mechanisms"],"prefix":"10.1016","volume":"49","author":[{"given":"Madhumati","family":"Sevvana","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1275-7495","authenticated-orcid":false,"given":"Zhenyong","family":"Keck","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Steven KH","family":"Foung","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard J","family":"Kuhn","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.coviro.2021.05.002_bib0005","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1126\/science.2523562","article-title":"Isolation of a Cdna clone derived from a blood-borne non-A, non-B viral-hepatitis genome","volume":"244","author":"Choo","year":"1989","journal-title":"Science"},{"key":"10.1016\/j.coviro.2021.05.002_bib0010","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1111\/j.1478-3231.2008.01925.x","article-title":"Discovery of the hepatitis C virus","volume":"29","author":"Houghton","year":"2009","journal-title":"Liver Int"},{"key":"10.1016\/j.coviro.2021.05.002_bib0015","doi-asserted-by":"crossref","first-page":"S2","DOI":"10.1016\/j.jhep.2016.07.035","article-title":"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","volume":"65","author":"Bukh","year":"2016","journal-title":"J Hepatol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0020","doi-asserted-by":"crossref","first-page":"399","DOI":"10.15585\/mmwr.mm6914a2","article-title":"Vital signs: newly reported acute and chronic hepatitis C cases \u2014 United States, 2009\u20132018","volume":"69","author":"Ryerson","year":"2020","journal-title":"Morb Mortal Wkly Rep"},{"key":"10.1016\/j.coviro.2021.05.002_bib0025","doi-asserted-by":"crossref","first-page":"162","DOI":"10.15585\/mmwr.mm7005a3","article-title":"Racial and ethnic disparities in the prevalence of stress and worry, mental health conditions, and increased substance use among adults during the COVID-19 pandemic \u2014 United States, April and May 2020","volume":"70","author":"McKnight-Eily","year":"2021","journal-title":"Morb Mortal Wkly Rep"},{"key":"10.1016\/j.coviro.2021.05.002_bib0030","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1002\/hep.27259","article-title":"Global distribution and prevalence of hepatitis C virus genotypes","volume":"61","author":"Messina","year":"2015","journal-title":"Hepatology"},{"key":"10.1016\/j.coviro.2021.05.002_bib0035","doi-asserted-by":"crossref","first-page":"5018","DOI":"10.3390\/v7092857","article-title":"Genetic diversity and selective pressure in hepatitis C virus genotypes 1-6: significance for direct-acting antiviral treatment and drug resistance","volume":"7","author":"Cuypers","year":"2015","journal-title":"Viruses-Basel"},{"key":"10.1016\/j.coviro.2021.05.002_bib0040","doi-asserted-by":"crossref","first-page":"1176","DOI":"10.1053\/j.gastro.2014.03.003","article-title":"New hepatitis C therapies: the toolbox, strategies, and challenges","volume":"146","author":"Pawlotsky","year":"2014","journal-title":"Gastroenterology"},{"key":"10.1016\/j.coviro.2021.05.002_bib0045","doi-asserted-by":"crossref","first-page":"1020","DOI":"10.1016\/j.jhep.2016.01.001","article-title":"Hepatitis C reinfection after sustained virological response","volume":"64","author":"Midgard","year":"2016","journal-title":"J Hepatol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0050","doi-asserted-by":"crossref","first-page":"684","DOI":"10.1016\/S0168-8278(02)00308-2","article-title":"The challenge of developing a vaccine against hepatitis C virus","volume":"37","author":"Forns","year":"2002","journal-title":"J Hepatol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0055","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1038\/nature04081","article-title":"Prospects for a vaccine against the hepatitis C virus","volume":"436","author":"Houghton","year":"2005","journal-title":"Nature"},{"key":"10.1016\/j.coviro.2021.05.002_bib0060","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1111\/j.1600-065X.2010.00977.x","article-title":"Prospects for prophylactic and therapeutic vaccines against the hepatitis C viruses","volume":"239","author":"Houghton","year":"2011","journal-title":"Immunol Rev"},{"key":"10.1016\/j.coviro.2021.05.002_sbref0065","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/j.coviro.2016.09.004","article-title":"Viral evasion and challenges of hepatitis C virus vaccine development","volume":"20","author":"Pierce","year":"2016","journal-title":"Curr Opin Virol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0070","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1002\/hep.20032","article-title":"Structural biology of hepatitis C virus","volume":"39","author":"Penin","year":"2004","journal-title":"Hepatology"},{"key":"10.1016\/j.coviro.2021.05.002_sbref0075","doi-asserted-by":"crossref","DOI":"10.3389\/fimmu.2018.01194","article-title":"Mapping determinants of virus neutralization and viral escape for rational design of a hepatitis C virus vaccine","volume":"9","author":"Keck","year":"2018","journal-title":"Front Immunol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0080","doi-asserted-by":"crossref","DOI":"10.3389\/fimmu.2018.01436","article-title":"Hepatitis C virus (HCV)-apolipoprotein interactions and immune evasion and their impact on HCV vaccine design","volume":"9","author":"Wrensch","year":"2018","journal-title":"Front Immunol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0085","doi-asserted-by":"crossref","first-page":"9505","DOI":"10.1073\/pnas.1307527110","article-title":"Ultrastructural analysis of hepatitis C virus particles","volume":"110","author":"Catanese","year":"2013","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.coviro.2021.05.002_bib0090","doi-asserted-by":"crossref","first-page":"3018","DOI":"10.1074\/jbc.M110.175018","article-title":"Biochemical and morphological properties of hepatitis C virus particles and determination of their lipidome","volume":"286","author":"Merz","year":"2011","journal-title":"J Biol Chem"},{"key":"10.1016\/j.coviro.2021.05.002_bib0095","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1021\/acsinfecdis.6b00110","article-title":"Structure and function of the hepatitis C virus envelope glycoproteins E1 and E2: antiviral and vaccine targets","volume":"2","author":"Freedman","year":"2016","journal-title":"ACS Infect Dis"},{"key":"10.1016\/j.coviro.2021.05.002_bib0100","doi-asserted-by":"crossref","first-page":"6147","DOI":"10.1128\/jvi.68.10.6147-6160.1994","article-title":"Formation and intracellular localization of hepatitis C virus envelope glycoprotein complexes expressed by recombinant vaccinia and Sindbis viruses","volume":"68","author":"Dubuisson","year":"1994","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0105","doi-asserted-by":"crossref","first-page":"10333","DOI":"10.1128\/JVI.00991-15","article-title":"Hepatitis C virus envelope glycoprotein E1 forms trimers at the surface of the virion","volume":"89","author":"Falson","year":"2015","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0110","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.coviro.2020.07.006","article-title":"Mapping the diverse structural landscape of the flavivirus antibody repertoire","volume":"45","author":"Sevvana","year":"2020","journal-title":"Curr Opin Virol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0115","doi-asserted-by":"crossref","first-page":"1090","DOI":"10.1126\/science.1243876","article-title":"Hepatitis C virus E2 envelope glycoprotein core structure","volume":"342","author":"Kong","year":"2013","journal-title":"Science"},{"key":"10.1016\/j.coviro.2021.05.002_sbref0120","doi-asserted-by":"crossref","first-page":"E6946","DOI":"10.1073\/pnas.1614942113","article-title":"Global mapping of antibody recognition of the hepatitis C virus E2 glycoprotein: implications for vaccine design","volume":"113","author":"Pierce","year":"2016","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.coviro.2021.05.002_sbref0125","doi-asserted-by":"crossref","DOI":"10.3389\/fimmu.2018.01315","article-title":"The neutralizing face of hepatitis C virus E2 envelope glycoprotein","volume":"9","author":"Tzarum","year":"2018","journal-title":"Front Immunol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0130","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1038\/nature13117","article-title":"Structure of the core ectodomain of the hepatitis C virus envelope glycoprotein 2","volume":"509","author":"Khan","year":"2014","journal-title":"Nature"},{"key":"10.1016\/j.coviro.2021.05.002_bib0135","doi-asserted-by":"crossref","first-page":"10117","DOI":"10.1074\/jbc.M115.643528","article-title":"Structural basis for penetration of the glycan shield of hepatitis C virus E2 glycoprotein by a broadly neutralizing human antibody","volume":"290","author":"Li","year":"2015","journal-title":"J Biol Chem"},{"key":"10.1016\/j.coviro.2021.05.002_bib0140","doi-asserted-by":"crossref","first-page":"1899","DOI":"10.1016\/j.jmb.2013.02.025","article-title":"Glycan shifting on hepatitis C virus (HCV) E2 glycoprotein is a mechanism for escape from broadly neutralizing antibodies","volume":"425","author":"Pantua","year":"2013","journal-title":"J Mol Biol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0145","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1003364","article-title":"Structural basis of HCV neutralization by human monoclonal antibodies resistant to viral neutralization escape","volume":"9","author":"Krey","year":"2013","journal-title":"PLoS Pathog"},{"key":"10.1016\/j.coviro.2021.05.002_sbref0150","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.02070-18","article-title":"Broadly neutralizing antibodies targeting new sites of vulnerability in hepatitis C virus E1E2","volume":"93","author":"Colbert","year":"2019","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0155","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1007759","article-title":"Functional expression and characterization of the envelope glycoprotein E1E2 heterodimer of hepatitis C virus","volume":"15","author":"Cao","year":"2019","journal-title":"PLoS Pathog"},{"key":"10.1016\/j.coviro.2021.05.002_sbref0160","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1016\/j.chom.2018.10.009","article-title":"HCV broadly neutralizing antibodies use a CDRH3 disulfide motif to recognize an E2 glycoprotein site that can be targeted for vaccine design","volume":"24","author":"Flyak","year":"2018","journal-title":"Cell Host Microbe"},{"key":"10.1016\/j.coviro.2021.05.002_bib0165","doi-asserted-by":"crossref","first-page":"1682","DOI":"10.1080\/07391102.2014.967300","article-title":"Structure-function analysis of hepatitis C virus envelope glycoproteins E1 and E2","volume":"33","author":"Nayak","year":"2015","journal-title":"J Biomol Struct Dyn"},{"key":"10.1016\/j.coviro.2021.05.002_bib0170","doi-asserted-by":"crossref","first-page":"2170","DOI":"10.1128\/JVI.02190-14","article-title":"Structural flexibility of a conserved antigenic region in hepatitis C virus glycoprotein E2 recognized by broadly neutralizing antibodies","volume":"89","author":"Meola","year":"2015","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0175","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.53169","article-title":"An ultralong CDRH2 in HCV neutralizing antibody demonstrates structural plasticity of antibodies against E2 glycoprotein","volume":"9","author":"Flyak","year":"2020","journal-title":"eLife"},{"key":"10.1016\/j.coviro.2021.05.002_bib0180","doi-asserted-by":"crossref","first-page":"12923","DOI":"10.1128\/JVI.02052-12","article-title":"Toward a hepatitis C virus vaccine: the structural basis of hepatitis C virus neutralization by AP33, a broadly neutralizing antibody","volume":"86","author":"Potter","year":"2012","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0185","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1016\/j.jhep.2010.10.014","article-title":"Hepatitis C virus entry into hepatocytes: molecular mechanisms and targets for antiviral therapies","volume":"54","author":"Zeisel","year":"2011","journal-title":"J Hepatol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0190","doi-asserted-by":"crossref","first-page":"41624","DOI":"10.1074\/jbc.M305289200","article-title":"Cell entry of hepatitis C virus requires a set of co-receptors that include the CD81 tetraspanin and the SR-B1 scavenger receptor","volume":"278","author":"Bartosch","year":"2003","journal-title":"J Biol Chem"},{"key":"10.1016\/j.coviro.2021.05.002_bib0195","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1016\/S0300-9084(03)00004-X","article-title":"Glycosylation of hepatitis C virus envelope proteins","volume":"85","author":"Goffard","year":"2003","journal-title":"Biochimie"},{"key":"10.1016\/j.coviro.2021.05.002_bib0200","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1038\/s41598-017-00320-7","article-title":"A biologically-validated HCV E1E2 heterodimer structural model","volume":"7","author":"Castelli","year":"2017","journal-title":"Sci Rep"},{"key":"10.1016\/j.coviro.2021.05.002_bib0205","first-page":"71","article-title":"Assembly of a functional HCV glycoprotein heterodimer","volume":"9","author":"Lavie","year":"2007","journal-title":"Curr Issues Mol Biol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0210","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms5874","article-title":"Unexpected structure for the N-terminal domain of hepatitis C virus envelope glycoprotein E1","volume":"5","author":"El Omari","year":"2014","journal-title":"Nat Commun"},{"key":"10.1016\/j.coviro.2021.05.002_sbref0215","doi-asserted-by":"crossref","DOI":"10.3389\/fimmu.2018.02146","article-title":"Hypervariable region 1 in envelope protein 2 of hepatitis c virus: a linchpin in neutralizing antibody evasion and viral entry","volume":"9","author":"Prentoe","year":"2018","journal-title":"Front Immunol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0220","doi-asserted-by":"crossref","DOI":"10.3389\/fimmu.2018.00910","article-title":"Glycan shielding and modulation of hepatitis C virus neutralizing antibodies","volume":"9","author":"Lavie","year":"2018","journal-title":"Front Immunol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0225","doi-asserted-by":"crossref","first-page":"1881","DOI":"10.1002\/hep.28705","article-title":"Hypervariable region 1 shielding of hepatitis C virus is a main contributor to genotypic differences in neutralization sensitivity","volume":"64","author":"Prentoe","year":"2016","journal-title":"Hepatology"},{"key":"10.1016\/j.coviro.2021.05.002_bib0230","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.02141-17","article-title":"Role of the E2 hypervariable region (HVR1) in the immunogenicity of a recombinant hepatitis C virus vaccine","volume":"92","author":"Law","year":"2018","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0235","doi-asserted-by":"crossref","first-page":"966","DOI":"10.1128\/JVI.01872-07","article-title":"Isolation and characterization of broadly neutralizing human monoclonal antibodies to the E1 glycoprotein of hepatitis C virus","volume":"82","author":"Meunier","year":"2008","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0240","doi-asserted-by":"crossref","first-page":"7257","DOI":"10.1128\/JVI.78.13.7257-7263.2004","article-title":"Human monoclonal antibody to hepatitis C virus El glycoprotein that blocks virus attachment and viral infectivity","volume":"78","author":"Keck","year":"2004","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0245","doi-asserted-by":"crossref","first-page":"2617","DOI":"10.1016\/j.jmb.2015.06.012","article-title":"Structure of hepatitis C virus envelope glycoprotein E1 antigenic site 314-324 in complex with antibody IGH526","volume":"427","author":"Kong","year":"2015","journal-title":"J Mol Biol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0250","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.abb5642","article-title":"An alternate conformation of HCV E2 neutralizing face as an additional vaccine target","volume":"6","author":"Tzarum","year":"2020","journal-title":"Sci Adv"},{"key":"10.1016\/j.coviro.2021.05.002_bib0255","doi-asserted-by":"crossref","first-page":"6067","DOI":"10.1128\/JVI.00252-08","article-title":"A point mutation leading to hepatitis C virus escape from neutralization by a monoclonal antibody to a conserved conformational epitope","volume":"82","author":"Keck","year":"2008","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0260","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1002653","article-title":"Human monoclonal antibodies to a novel cluster of conformational epitopes on HCV E2 with resistance to neutralization escape in a genotype 2a isolate","volume":"8","author":"Keck","year":"2012","journal-title":"PLoS Pathog"},{"key":"10.1016\/j.coviro.2021.05.002_bib0265","doi-asserted-by":"crossref","first-page":"1922","DOI":"10.1002\/hep.28850","article-title":"Affinity maturation of a broadly neutralizing human monoclonal antibody that prevents acute hepatitis C virus infection in mice","volume":"64","author":"Keck","year":"2016","journal-title":"Hepatology"},{"key":"10.1016\/j.coviro.2021.05.002_bib0270","doi-asserted-by":"crossref","first-page":"5494","DOI":"10.1128\/JVI.02153-09","article-title":"Mutations within a conserved region of the hepatitis C virus E2 glycoprotein that influence virus-receptor interactions and sensitivity to neutralizing antibodies","volume":"84","author":"Dhillon","year":"2010","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0275","doi-asserted-by":"crossref","first-page":"3112","DOI":"10.1128\/JVI.02458-15","article-title":"Antibody response to hypervariable region 1 interferes with broadly neutralizing antibodies to hepatitis C virus","volume":"90","author":"Keck","year":"2016","journal-title":"J Virol"},{"key":"10.1016\/j.coviro.2021.05.002_bib0280","doi-asserted-by":"crossref","first-page":"6149","DOI":"10.1128\/JVI.00248-09","article-title":"Mutations in hepatitis C virus E2 located outside the CD81 binding sites lead to escape from broadly neutralizing antibodies but compromise virus infectivity","volume":"83","author":"Keck","year":"2009","journal-title":"J Virol"}],"container-title":["Current Opinion in Virology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1879625721000560?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1879625721000560?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,5,15]],"date-time":"2026-05-15T08:03:24Z","timestamp":1778832204000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1879625721000560"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,8]]},"references-count":56,"alternative-id":["S1879625721000560"],"URL":"https:\/\/doi.org\/10.1016\/j.coviro.2021.05.002","relation":{},"ISSN":["1879-6257"],"issn-type":[{"value":"1879-6257","type":"print"}],"subject":[],"published":{"date-parts":[[2021,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structural perspectives on HCV humoral immune evasion mechanisms","name":"articletitle","label":"Article Title"},{"value":"Current Opinion in Virology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.coviro.2021.05.002","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}