{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,27]],"date-time":"2026-04-27T14:17:05Z","timestamp":1777299425582,"version":"3.51.4"},"reference-count":144,"publisher":"MDPI AG","issue":"6","license":[{"start":{"date-parts":[[2021,6,1]],"date-time":"2021-06-01T00:00:00Z","timestamp":1622505600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Pathogens"],"abstract":"<jats:p>Chronic hepatitis C virus (HCV) infections continue to be a major contributor to liver disease worldwide. HCV treatment has become highly effective, yet there are still no vaccines or prophylactic strategies available to prevent infection and allow effective management of the global HCV burden. Glycan-dependent interactions are crucial to many aspects of the highly complex HCV entry process, and also modulate immune evasion. This review provides an overview of the roles of viral and cellular glycans in HCV infection and highlights glycan-focused advances in the development of entry inhibitors and vaccines to effectively prevent HCV infection.<\/jats:p>","DOI":"10.3390\/pathogens10060685","type":"journal-article","created":{"date-parts":[[2021,6,1]],"date-time":"2021-06-01T23:07:03Z","timestamp":1622588823000},"page":"685","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["Hepatitis C Virus Glycan-Dependent Interactions and the Potential for Novel Preventative Strategies"],"prefix":"10.3390","volume":"10","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4278-0984","authenticated-orcid":false,"given":"Emmanuelle V.","family":"LeBlanc","sequence":"first","affiliation":[{"name":"Department of Biomedical and Molecular Sciences, Queen\u2019s University, Kingston, ON K7L 3N6, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Youjin","family":"Kim","sequence":"additional","affiliation":[{"name":"Department of Biomedical and Molecular Sciences, Queen\u2019s University, Kingston, ON K7L 3N6, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5977-8453","authenticated-orcid":false,"given":"Chantelle J.","family":"Capicciotti","sequence":"additional","affiliation":[{"name":"Department of Biomedical and Molecular Sciences, Queen\u2019s University, Kingston, ON K7L 3N6, Canada"},{"name":"Department of Chemistry, Queen\u2019s University, Kingston, ON K7L 3N6, Canada"},{"name":"Department of Surgery, Queen\u2019s University, Kingston, ON K7L 3N6, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2474-1834","authenticated-orcid":false,"given":"Che C.","family":"Colpitts","sequence":"additional","affiliation":[{"name":"Department of Biomedical and Molecular Sciences, Queen\u2019s University, Kingston, ON K7L 3N6, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2021,6,1]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1056\/NEJM200107053450107","article-title":"Hepatitis C Virus Infection","volume":"345","author":"Lauer","year":"2001","journal-title":"N. Engl. J. Med."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/S2468-1253(16)30181-9","article-title":"Global prevalence and genotype distribution of hepatitis C virus infection in 2015: A modelling study","volume":"2","author":"Blach","year":"2017","journal-title":"Lancet Gastroenterol. Hepatol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"938","DOI":"10.1126\/science.282.5390.938","article-title":"Binding of Hepatitis C Virus to CD81","volume":"282","author":"Pileri","year":"1998","journal-title":"Science"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"5017","DOI":"10.1093\/emboj\/cdf529","article-title":"The human scavenger receptor class B type I is a novel candidate receptor for the hepatitis C virus","volume":"21","author":"Scarselli","year":"2002","journal-title":"EMBO J."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1016\/j.antiviral.2014.02.013","article-title":"The past, present and future of neutralizing antibodies for hepatitis C virus","volume":"105","author":"Ball","year":"2014","journal-title":"Antivir. Res."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/j.ejmech.2019.01.025","article-title":"Hepatitis C\u2014New drugs and treatment prospects","volume":"165","author":"Muszalska","year":"2019","journal-title":"Eur. J. Med. Chem."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.jcv.2016.02.026","article-title":"Direct-acting antiviral treatment in adults infected with hepatitis C virus: Reactivation of hepatitis B virus coinfection as a further challenge","volume":"78","author":"Courjon","year":"2016","journal-title":"J. Clin. Virol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1111\/jvh.12754","article-title":"HBV reactivation in patients with HCV\/HBV cirrhosis on treatment with direct-acting antivirals","volume":"25","author":"Calvaruso","year":"2018","journal-title":"J. Viral Hepat."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1016\/j.cgh.2016.06.023","article-title":"Hepatitis due to Reactivation of Hepatitis B Virus in Endemic Areas Among Patients With Hepatitis C Treated With Direct-acting Antiviral Agents","volume":"15","author":"Wang","year":"2017","journal-title":"Clin. Gastroenterol. Hepatol."},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Frazzoni, L., Sikandar, U., Metelli, F., Sadalla, S., Mazzella, G., Bazzoli, F., Fuccio, L., and Azzaroli, F. (2021). Hepatocellular Carcinoma Recurrence after Hepatitis C Virus Therapy with Direct-Acting Antivirals. A Systematic Review and Meta-Analysis. J. Clin. Med., 10.","DOI":"10.3390\/jcm10081694"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1084\/jem.20021756","article-title":"Infectious hepatitis C virus pseudo-particles containing functional E1-E2 envelope protein complexes","volume":"197","author":"Bartosch","year":"2003","journal-title":"J. Exp. Med."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1126\/science.285.5424.110","article-title":"Replication of Subgenomic Hepatitis C Virus RNAs in a Hepatoma Cell Line","volume":"285","author":"Lohmann","year":"1999","journal-title":"Science"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1038\/nm1268","article-title":"Production of infectious hepatitis C virus in tissue culture from a cloned viral genome","volume":"11","author":"Wakita","year":"2005","journal-title":"Nat. Med."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1080\/14789450.2017.1344102","article-title":"Hepatitis C virus-apolipoprotein interactions: Molecular mechanisms and clinical impact","volume":"14","author":"Crouchet","year":"2017","journal-title":"Expert Rev. Proteom."},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Colpitts, C.C., Tsai, P.-L., and Zeisel, M.B. (2020). Hepatitis C Virus Entry: An Intriguingly Complex and Highly Regulated Process. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21062091"},{"key":"ref_16","first-page":"87","article-title":"Hepatitis C virus entry","volume":"369","author":"Zeisel","year":"2013","journal-title":"Curr. Top. Microbiol. Immunol."},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Watanabe, Y., Bowden, T.A., Wilson, I.A., and Crispin, M. (2019). Exploitation of glycosylation in enveloped virus pathobiology. Biochim. Biophys. Acta Gen. Subj., 1480\u20131497.","DOI":"10.1016\/j.bbagen.2019.05.012"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/j.tim.2007.03.003","article-title":"Virus glycosylation: Role in virulence and immune interactions","volume":"15","author":"Vigerust","year":"2007","journal-title":"Trends Microbiol."},{"key":"ref_19","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":"ref_20","doi-asserted-by":"crossref","first-page":"8101","DOI":"10.1128\/JVI.00127-07","article-title":"The neutralizing activity of antihepatitis C virus antibodies is modulated by specific glycans on the E2 envelope protein","volume":"81","author":"Helle","year":"2007","journal-title":"J. Virol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1099\/0022-1317-80-4-887","article-title":"Analysis of the glycosylation sites of hepatitis C virus (HCV) glycoprotein E1 and the influence of E1 glycans on the formation of the HCV glycoprotein complex","volume":"80","author":"Meunier","year":"1999","journal-title":"J. Gen. Virol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"8400","DOI":"10.1128\/JVI.79.13.8400-8409.2005","article-title":"Role of N-linked glycans in the functions of hepatitis C virus envelope glycoproteins","volume":"79","author":"Goffard","year":"2005","journal-title":"J. Virol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"11905","DOI":"10.1128\/JVI.01548-10","article-title":"Role of N-linked glycans in the functions of HCV envelope proteins incorporated into infectious virions","volume":"84","author":"Helle","year":"2010","journal-title":"J. Virol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1888","DOI":"10.1093\/infdis\/jit376","article-title":"Additional glycosylation within a specific hypervariable region of subtype 3a of hepatitis C virus protects against virus neutralization","volume":"208","author":"Anjum","year":"2013","journal-title":"J. Infect. Dis."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"8346","DOI":"10.1128\/JVI.00192-15","article-title":"New insights into the understanding of hepatitis C virus entry and cell to cell transmission by using the ionophore monensin A","volume":"89","author":"Potel","year":"2015","journal-title":"J. Virol."},{"key":"ref_26","first-page":"17","article-title":"Cell culture systems for hepatitis C virus","volume":"Volume 369","author":"Ralf","year":"2013","journal-title":"Hepatitis C Virus: From Molecular Virology to Antiviral Therapy. Current Topics in Microbiology and Immunology"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"2994","DOI":"10.1128\/JVI.78.6.2994-3002.2004","article-title":"Characterization of functional hepatitis C virus envelope glycoproteins","volume":"78","author":"Voisset","year":"2004","journal-title":"J. Virol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1016\/j.virol.2004.03.039","article-title":"Influence of N-linked glycans on intracellular transport of hepatitis C virus E1 chimeric glycoprotein and its role in pseudotype virus infectivity","volume":"324","author":"Beyene","year":"2004","journal-title":"Virology"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"6875","DOI":"10.1128\/JVI.78.13.6875-6882.2004","article-title":"Characterization of infectious retroviral pseudotype particles bearing hepatitis C virus glycoproteins","volume":"78","author":"Flint","year":"2004","journal-title":"J. Virol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1016\/j.jasms.2007.11.022","article-title":"Mass spectrometric characterization of glycosylation of hepatitis C virus E2 envelope glycoprotein reveals extended microheterogeneity of N-glycans","volume":"19","author":"Iacob","year":"2007","journal-title":"J. Am. Soc. Mass Spectrom."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1093\/glycob\/cws171","article-title":"Mass spectrometric analysis of hepatitis C viral envelope protein E2 reveals extended microheterogeneity of mucin-type O-linked glycosylation","volume":"23","author":"Scheidig","year":"2013","journal-title":"Glycobiology"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1089","DOI":"10.1038\/ncb1631","article-title":"The lipid droplet is an important organelle for hepatitis C virus production","volume":"9","author":"Miyanari","year":"2007","journal-title":"Nat. Cell Biol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"3189","DOI":"10.1099\/vir.0.81428-0","article-title":"Assembly of functional hepatitis C virus glycoproteins on infectious pseudoparticles occurs intracellularly and requires concomitant incorporation of E1 and E2 glycoproteins","volume":"86","author":"Sandrin","year":"2005","journal-title":"J. Gen. Virol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"892","DOI":"10.3390\/biology3040892","article-title":"Hepatitis C virus life cycle and lipid metabolism","volume":"3","author":"Popescu","year":"2014","journal-title":"Biology"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"e0208","DOI":"10.1097\/MD.0000000000010208","article-title":"Lectin microarray and mass spectrometric analysis of hepatitis C proteins reveals N-linked glycosylation","volume":"97","author":"Guo","year":"2018","journal-title":"Medicine"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"11078","DOI":"10.1128\/JVI.00800-09","article-title":"Blocking hepatitis C virus infection with recombinant form of envelope protein 2 ectodomain","volume":"83","author":"Whidby","year":"2009","journal-title":"J. Virol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"8072","DOI":"10.1128\/JVI.00459-07","article-title":"Hepatitis C virus envelope glycoprotein E2 glycans modulate entry, CD81 binding, and neutralization","volume":"81","author":"Falkowska","year":"2007","journal-title":"J. Virol."},{"key":"ref_38","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":"ref_39","doi-asserted-by":"crossref","first-page":"2495","DOI":"10.1099\/vir.0.82872-0","article-title":"Robust production of infectious viral particles in Huh7 cells by introducing mutations in hepatitis C virus structural proteins","volume":"88","author":"Delgrange","year":"2007","journal-title":"J. Gen. Virol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1681","DOI":"10.1099\/vir.0.010983-0","article-title":"Efficient production of infectious hepatitis C virus with adaptive mutations in cultured hepatoma cells","volume":"90","author":"Bungyoku","year":"2009","journal-title":"J. Gen. Virol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"10039","DOI":"10.1073\/pnas.1822002116","article-title":"Hypervariable region 1 and N-linked glycans of HCV regulate viron neutralization by modulating envelope conformations","volume":"116","author":"Prentoe","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"5848","DOI":"10.1073\/pnas.0700760104","article-title":"Hepatitis C virus production by human hepatocytes dependent on assembly and secretion of very low density lipoproteins","volume":"104","author":"Huang","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"2120","DOI":"10.1128\/JVI.02053-07","article-title":"Cellular determinants of hepatitis C virus assembly, maturation, degradation, and secretion","volume":"82","author":"Gastaminza","year":"2008","journal-title":"J. Virol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"2883","DOI":"10.1099\/jgv.0.000608","article-title":"Hepatitis C virus resistance to broadly neutralizing antibodies measured using replication competent virus and pseudo particles","volume":"97","author":"Wasilewski","year":"2016","journal-title":"J. Gen. Virol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"P10117","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":"ref_46","doi-asserted-by":"crossref","first-page":"1229","DOI":"10.1093\/glycob\/cwh106","article-title":"Tracking global patterns of N-linked glycosylation site variation in highly variable viral glycoproteins: HIV, SIV, and HCV envelopes and influenza hemagglutinin","volume":"14","author":"Zhang","year":"2004","journal-title":"Glycobiology"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"910","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":"ref_48","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1146\/annurev.immunol.25.022106.141602","article-title":"Flying under the radar: The immunobiology of hepatitis C","volume":"25","author":"Dustin","year":"2007","journal-title":"Annu. Rev. Immunol."},{"key":"ref_49","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. USA"},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Gopal, R., Jackson, K., Tzarum, N., Kong, L., Ettenger, A., Guest, J., Pfaff, J.M., Barnes, T., Honda, A., and Giang, E. (2017). Probing the antigenicity of hepatitis C virus envelope glycoprotein complex by high-throughput mutagenesis. PLoS Pathog., 13.","DOI":"10.1371\/journal.ppat.1006735"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1909","DOI":"10.3390\/v3101909","article-title":"The hepatitis C virus glycan shield and evasion of the humoral immune response","volume":"3","author":"Helle","year":"2011","journal-title":"Viruses"},{"key":"ref_52","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":"ref_53","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1016\/j.chom.2018.10.009","article-title":"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":"ref_54","doi-asserted-by":"crossref","first-page":"eaav1882","DOI":"10.1126\/sciadv.aav1882","article-title":"Genetic and structural insights into broad neutralization of hepatitis C virus by human VH1-69 antibodies","volume":"5","author":"Tzarum","year":"2019","journal-title":"Sci. Adv."},{"key":"ref_55","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 E1 glycoprotein that blocks virus attachment and viral infectivity","volume":"78","author":"Keck","year":"2004","journal-title":"J. Virol."},{"key":"ref_56","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":"ref_57","doi-asserted-by":"crossref","first-page":"2224","DOI":"10.1128\/JVI.01594-10","article-title":"Hypervariable region 1 differentially impacts viability of hepatitis C virus strains of genotypes 1 to 6 and impairs virus neutralization","volume":"85","author":"Prentoe","year":"2011","journal-title":"J. Virol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1988","DOI":"10.1136\/gutjnl-2015-310300","article-title":"HVR1-mediated antibody evasion of highly infectious in vivo adapted HCV in humanised mice","volume":"65","author":"Prentoe","year":"2016","journal-title":"Gut"},{"key":"ref_59","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":"ref_60","doi-asserted-by":"crossref","first-page":"2146","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":"ref_61","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1016\/j.jhep.2018.11.003","article-title":"Functional and immunogenic characterization of diverse HCV glycoprotein E2 variants","volume":"70","author":"Khera","year":"2019","journal-title":"J. Hepatol."},{"key":"ref_62","doi-asserted-by":"crossref","unstructured":"Dowd, K.A., Jost, C.A., Durbin, A.P., Whitehead, S.S., and Pierson, T.C. (2011). A dynamic landscape for antibody binding modulates antibody-mediated neutralization of West Nile virus. PLoS Pathog., 7.","DOI":"10.1371\/journal.ppat.1002111"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"11726","DOI":"10.1128\/JVI.01140-14","article-title":"Combined effects of the structural heterogeneity and dynamics of flaviviruses on antibody recognition","volume":"88","author":"Dowd","year":"2014","journal-title":"J. Virol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1016\/j.virol.2011.10.023","article-title":"Hepatitis C virus epitope exposure and neutralization by antibodies is affected by time and temperature","volume":"422","author":"Sabo","year":"2012","journal-title":"Virology"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"10159","DOI":"10.1128\/JVI.01180-10","article-title":"Characterization of the envelope glycoproteins associated with infectious hepatitis C virus","volume":"84","author":"Vieyres","year":"2010","journal-title":"J. Virol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1734","DOI":"10.1128\/JVI.80.4.1734-1741.2006","article-title":"Time- and temperature-dependent activation of hepatitis C virus for low-pH-triggered entry","volume":"80","author":"Tscherne","year":"2006","journal-title":"J. Virol."},{"key":"ref_67","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":"ref_68","doi-asserted-by":"crossref","first-page":"10999","DOI":"10.1128\/JVI.00526-10","article-title":"Ultrastructural and biophysical characterization of hepatitis C virus particles produced in cell culture","volume":"84","author":"Gastaminza","year":"2010","journal-title":"J. Virol."},{"key":"ref_69","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. USA"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"508","DOI":"10.1016\/j.virol.2015.03.025","article-title":"Shake, rattle, and roll: Impact of the dynamics of flavivirus particles on their interactions with the host","volume":"479\u2013480","author":"Kuhn","year":"2015","journal-title":"Virology"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"4070","DOI":"10.1128\/JVI.77.7.4070-4080.2003","article-title":"Hepatitis C Virus Glycoproteins Interact with DC-SIGN and DC-SIGNR","volume":"77","author":"Zhang","year":"2003","journal-title":"J. Virol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"4498","DOI":"10.1073\/pnas.0831128100","article-title":"L-SIGN (CD 209L) is a liver-specific capture receptor for hepatitis C virus","volume":"100","author":"Gardner","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"20358","DOI":"10.1074\/jbc.M301284200","article-title":"DC-SIGN and L-SIGN Are High Affinity Binding Receptors for Hepatitis C Virus Glycoprotein E2","volume":"278","author":"Lozach","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"546","DOI":"10.1128\/JVI.77.1.546-559.2003","article-title":"Role of the asialoglycoprotein receptor in binding and entry of hepatitis C virus structural proteins in cultured human hepatocytes","volume":"77","author":"Saunier","year":"2003","journal-title":"J. Virol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1038\/cmi.2009.32","article-title":"Specifically binding of L-ficolin to N-glycans of HCV envelope glycoproteins E1 and E2 leads to complement activation","volume":"6","author":"Liu","year":"2009","journal-title":"Cell. Mol. Immunol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"676","DOI":"10.1159\/000362209","article-title":"Recombinant human L-ficolin directly neutralizes hepatitis C virus entry","volume":"6","author":"Hamed","year":"2014","journal-title":"J. Innate Immun."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1007\/s11010-009-0056-y","article-title":"C-type lectin LSECtin interacts with DC-SIGNR and is involved in hepatitis C virus binding","volume":"327","author":"Li","year":"2009","journal-title":"Mol. Cell. Biochem."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"664","DOI":"10.1007\/s13238-010-0088-9","article-title":"Specific interaction of hepatitis C virus glycoproteins with mannan binding lectin inhibits virus entry","volume":"1","author":"Brown","year":"2010","journal-title":"Protein Cell"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1016\/j.virol.2005.06.026","article-title":"LSECtin interacts with filovirus glycoproteins and the spike protein of SARS coronavirus","volume":"340","author":"Gramberg","year":"2005","journal-title":"Virology"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"1437","DOI":"10.1021\/cb500121c","article-title":"Role of N-Linked Glycans in the Interactions of Recombinant HCV Envelope Glycoproteins with Cellular Receptors","volume":"9","author":"Chen","year":"2014","journal-title":"ACS Chem. Biol."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"32035","DOI":"10.1074\/jbc.M402296200","article-title":"C-type Lectins L-SIGN and DC-SIGN Capture and Transmit Infectious Hepatitis C Virus Pseudotype Particles","volume":"279","author":"Lozach","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"14067","DOI":"10.1073\/pnas.0405695101","article-title":"L-SIGN (CD209L) and DC-SIGN (CD209) mediate transinfection of liver cells by hepatitis C virus","volume":"101","author":"Cormier","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"2949","DOI":"10.1007\/s00705-014-2150-z","article-title":"CLEC4M-positive and CD81-negative Huh7 cells are not susceptible to JFH-1 HCVcc infection but mediate transinfection","volume":"159","author":"Ishibashi","year":"2014","journal-title":"Arch. Virol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"41003","DOI":"10.1074\/jbc.M302267200","article-title":"Cellular Binding of Hepatitis C Virus Envelope Glycoprotein E2 Requires Cell Surface Heparan Sulfate","volume":"278","author":"Barth","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"10579","DOI":"10.1128\/JVI.00941-06","article-title":"Viral and Cellular Determinants of the Hepatitis C Virus Envelope-Heparan Sulfate Interaction","volume":"80","author":"Barth","year":"2006","journal-title":"J. Virol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"3933","DOI":"10.1128\/JVI.02622-06","article-title":"Sulfated Homologues of Heparin Inhibit Hepatitis C Virus Entry into Mammalian Cells","volume":"81","author":"Basu","year":"2007","journal-title":"J. Virol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"7256","DOI":"10.1128\/JVI.07222-11","article-title":"Hepatitis C Virus Attachment Mediated by Apolipoprotein E Binding to Cell Surface Heparan Sulfate","volume":"86","author":"Jiang","year":"2012","journal-title":"J. Virol."},{"key":"ref_88","doi-asserted-by":"crossref","unstructured":"Lef\u00e8vre, M., Felmlee, D.J., Parnot, M., Baumert, T.F., and Schuster, C. (2014). Syndecan 4 Is Involved in Mediating HCV Entry through Interaction with Lipoviral Particle-Associated Apolipoprotein E. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0095550"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"3846","DOI":"10.1128\/JVI.03647-14","article-title":"Characterization of Hepatitis C Virus Interaction with Heparan Sulfate Proteoglycans","volume":"89","author":"Xu","year":"2015","journal-title":"J. Virol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"11208","DOI":"10.1016\/S0021-9258(19)78112-5","article-title":"Liver heparan sulfate structure. A novel molecular design","volume":"269","author":"Lyon","year":"1994","journal-title":"J. Biol. Chem."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1042\/bj3220499","article-title":"Structural differences and the presence of unsubstituted amino groups in heparan sulphates from different tissues and species","volume":"322","author":"Toida","year":"1997","journal-title":"Biochem. J."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"6866","DOI":"10.1128\/JVI.03475-12","article-title":"Syndecan-1 Serves as the Major Receptor for Attachment of Hepatitis C Virus to the Surfaces of Hepatocytes","volume":"87","author":"Shi","year":"2013","journal-title":"J. Virol."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"e00280-17","DOI":"10.1128\/JVI.00280-17","article-title":"Attachment and Postattachment Receptors Important for Hepatitis C Virus Infection and Cell-to-Cell Transmission","volume":"91","author":"Fan","year":"2017","journal-title":"J. Virol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"e12711","DOI":"10.1111\/cmi.12711","article-title":"Hepatitis C virus infection propagates through interactions between Syndecan-1 and CD81 and impacts the hepatocyte glycocalyx","volume":"19","author":"Grigorov","year":"2017","journal-title":"Cell. Microbiol."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1002\/hep.21959","article-title":"Hepatitis C virus cell-cell transmission in hepatoma cells in the presence of neutralizing antibodies","volume":"47","author":"Timpe","year":"2008","journal-title":"Hepatology"},{"key":"ref_96","doi-asserted-by":"crossref","unstructured":"Vervaeke, P., Alen, M., Noppen, S., Schols, D., Oreste, P., and Liekens, S. (2013). Sulfated Escherichia coli K5 polysaccharide derivatives inhibit dengue virus infection of human microvascular endothelial cells by interacting with the viral envelope protein E domain III. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0074035"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1016\/j.bbrc.2012.07.002","article-title":"3-O-sulfated glucuronide derivative as a potential anti-dengue virus agent","volume":"424","author":"Hidari","year":"2012","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_98","doi-asserted-by":"crossref","unstructured":"Kim, S.Y., Li, B., and Linhardt, R.J. (2017). Pathogenesis and Inhibition of Flaviviruses from a Carbohydrate Perspective. Pharmaceuticals, 10.","DOI":"10.3390\/ph10020044"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"7806","DOI":"10.1128\/JVI.00896-14","article-title":"A Small Molecule Inhibits Virion Attachment to Heparan Sulfate- or Sialic Acid-Containing Glycans","volume":"88","author":"Colpitts","year":"2014","journal-title":"J. Virol."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"1947","DOI":"10.1002\/hep.24610","article-title":"The green tea polyphenol, epigallocatechin-3-gallate, inhibits hepatitis C virus entry","volume":"54","author":"Ciesek","year":"2011","journal-title":"Hepatology"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"720","DOI":"10.1002\/hep.24803","article-title":"(\u2212)-Epigallocatechin-3-gallate is a new inhibitor of hepatitis C virus entry","volume":"55","author":"Calland","year":"2012","journal-title":"Hepatology"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"4162","DOI":"10.1016\/j.bmcl.2014.07.051","article-title":"Structure\u2013activity studies of (\u2212)-epigallocatechin gallate derivatives as HCV entry inhibitors","volume":"24","author":"Bhat","year":"2014","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1002\/lt.24344","article-title":"Prevention of hepatitis C virus infection using a broad cross-neutralizing monoclonal antibody (AR4A) and epigallocatechin gallate","volume":"22","author":"Law","year":"2016","journal-title":"Liver Transpl."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"13593","DOI":"10.1038\/s41598-019-49973-6","article-title":"Addition of Epigallocatechin Gallate 400\u2009mg to Sofosbuvir 400\u2009mg\u2009+\u2009Daclatisvir 60\u2009mg With or Without Ribavirin in Treatment of Patients with Chronic Hepatitis C Improves the Safety Profile: A Pilot Study","volume":"9","author":"Shiha","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1002\/hep.25665","article-title":"Human apolipoprotein E peptides inhibit hepatitis C virus entry by blocking virus binding","volume":"56","author":"Liu","year":"2012","journal-title":"Hepatology"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1172\/JCI1099","article-title":"An apolipoprotein E synthetic peptide targets to lipoproteins in plasma and mediates both cellular lipoprotein interactions in vitro and acute clearance of cholesterol-rich lipoproteins in vivo","volume":"101","author":"Nikoulin","year":"1998","journal-title":"J. Clin. Investig."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"48529","DOI":"10.1074\/jbc.M306923200","article-title":"ApoE Genotype and an ApoE-mimetic Peptide Modify the Systemic and Central Nervous System Inflammatory Response","volume":"278","author":"Lynch","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1016\/j.antiviral.2010.02.314","article-title":"In vitro antiviral activity of some uridine derivatives of 2-deoxy sugars against classical swine fever virus","volume":"86","author":"Krol","year":"2010","journal-title":"Antiviral Res."},{"key":"ref_109","doi-asserted-by":"crossref","unstructured":"Krol, E., Wandzik, I., Krejmer-Rabalska, M., and Szewczyk, B. (2017). Biological Evaluation of Uridine Derivatives of 2-Deoxy Sugars as Potential Antiviral Compounds against Influenza a Virus. Int. J. Mol. Sci., 18.","DOI":"10.3390\/ijms18081700"},{"key":"ref_110","doi-asserted-by":"crossref","unstructured":"Krol, E., Wandzik, I., Pastuch-Gawolek, G., and Szewczyk, B. (2018). Anti-Hepatitis C Virus Activity of Uridine Derivatives of 2-Deoxy Sugars. Molecules, 23.","DOI":"10.3390\/molecules23071547"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"746","DOI":"10.1016\/j.cell.2015.09.056","article-title":"Engineering a Therapeutic Lectin by Uncoupling Mitogenicity from Antiviral Activity","volume":"163","author":"Swanson","year":"2015","journal-title":"Cell"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"2038","DOI":"10.1016\/j.ymthe.2019.07.021","article-title":"Engineering of a Lectibody Targeting High-Mannose-Type Glycans of the HIV Envelope","volume":"27","author":"Hamorsky","year":"2019","journal-title":"Mol. Ther."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/j.jcmgh.2020.08.009","article-title":"Safety and Efficacy of Avaren-Fc Lectibody Targeting HCV High-Mannose Glycans in a Human Liver Chimeric Mouse Model","volume":"11","author":"Dent","year":"2021","journal-title":"Cell. Mol. Gastroenterol. Hepatol."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"1535","DOI":"10.1080\/14760584.2016.1194759","article-title":"Hepatitis C virus vaccine candidates inducing protective neutralizing antibodies","volume":"15","author":"Fauvelle","year":"2016","journal-title":"Expert Rev. Vaccines"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1111\/1469-0691.12493","article-title":"Why is it so difficult to develop a hepatitis C virus preventive vaccine?","volume":"20","author":"Zingaretti","year":"2014","journal-title":"Clin. Microbiol. Infect."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"S34","DOI":"10.1016\/j.jhep.2014.09.009","article-title":"A prophylactic hepatitis C virus vaccine: A distant peak still worth climbing","volume":"61","author":"Baumert","year":"2014","journal-title":"J. Hepatol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"11984","DOI":"10.3748\/wjg.v21.i42.11984","article-title":"Progress in the development of vaccines for hepatitis C virus infection","volume":"21","author":"Ghasemi","year":"2015","journal-title":"World J. Gastroenterol."},{"key":"ref_118","doi-asserted-by":"crossref","unstructured":"Ogholikhan, S., and Schwarz, K.B. (2016). Hepatitis Vaccines. Vaccines, 4.","DOI":"10.3390\/vaccines4010006"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1099\/vir.0.028092-0","article-title":"Characterization of antibody-mediated neutralization directed against the hypervariable region 1 of hepatitis C virus E2 glycoprotein","volume":"92","author":"Vieyres","year":"2011","journal-title":"J. Gen. Virol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"eaat4615","DOI":"10.1126\/scitranslmed.aat4615","article-title":"Glycoconjugate vaccines: Principles and mechanisms","volume":"10","author":"Rappuoli","year":"2018","journal-title":"Sci. Transl. Med."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"13372","DOI":"10.1073\/pnas.0505763102","article-title":"Dissection of the carbohydrate specificity of the broadly neutralizing anti-HIV-1 antibody 2G12","volume":"102","author":"Calarese","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1093\/glycob\/cwu123","article-title":"Crystal structure of the HIV neutralizing antibody 2G12 in complex with a bacterial oligosaccharide analog of mammalian oligomannose","volume":"25","author":"Stanfield","year":"2015","journal-title":"Glycobiology"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"13232","DOI":"10.1128\/JVI.78.23.13232-13252.2004","article-title":"Comprehensive cross-clade neutralization analysis of a panel of anti-human immunodeficiency virus type 1 monoclonal antibodies","volume":"78","author":"Binley","year":"2004","journal-title":"J. Virol."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/j.ddtec.2020.09.004","article-title":"Synthetic carbohydrate-based HIV-1 vaccines","volume":"35\u201336","author":"Bastida","year":"2020","journal-title":"Drug Discov. Today Technol."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"12088","DOI":"10.1128\/JVI.75.24.12088-12097.2001","article-title":"Induction of hepatitis C virus E1 envelope protein-specific immune response can be enhanced by mutation of N-glycosylation sites","volume":"75","author":"Fournillier","year":"2001","journal-title":"J. Virol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"6572","DOI":"10.1016\/j.vaccine.2007.07.003","article-title":"Deletion of N-glycosylation sites of hepatitis C virus envelope protein E1 enhances specific cellular and humoral immune responses","volume":"25","author":"Liu","year":"2007","journal-title":"Vaccine"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"1544","DOI":"10.1016\/j.vaccine.2006.09.091","article-title":"Engineering of N-glycosylation of hepatitis C virus envelope protein E2 enhances T cell responses for DNA immunization","volume":"25","author":"Li","year":"2007","journal-title":"Vaccine"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"1764","DOI":"10.1016\/j.bbagen.2015.08.007","article-title":"N-glycosylation mutated HCV envelope glycoprotein complex enhances antigen presenting activity and cellular and neutralizing antibody responses","volume":"1860","author":"Ren","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"1611","DOI":"10.1111\/pbi.12743","article-title":"Lettuce produced hepatitis C virus E1E2 heterodimer triggers immune responses in mice and antibody production after oral vaccination","volume":"15","author":"Liu","year":"2017","journal-title":"Plant Biotechnol. J."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"e00704-20","DOI":"10.1128\/JVI.00704-20","article-title":"Structure-Based Design of Hepatitis C Virus E2 Glycoprotein Improves Serum Binding and Cross-Neutralization","volume":"94","author":"Pierce","year":"2020","journal-title":"J. Virol."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"1396","DOI":"10.3389\/fimmu.2018.01396","article-title":"Conformational Flexibility in the CD81-Binding Site of the Hepatitis C virus Glycoprotein E2","volume":"9","author":"Nagarathinam","year":"2018","journal-title":"Front. Immunol."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"2170","DOI":"10.1128\/JVI.02190-14","article-title":"Structural flexibility of a conserved broadly neutralizing epitope in hepatitis C virus glycoprotein E2","volume":"89","author":"Meola","year":"2015","journal-title":"J. Virol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"1123","DOI":"10.1126\/science.1175868","article-title":"Structural Basis of Immune Evasion at the Site of CD4 Attachment on HIV-1 gp120","volume":"326","author":"Chen","year":"2009","journal-title":"Science"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"10486","DOI":"10.1128\/JVI.01462-16","article-title":"Altered glycosylation patterns increase immunogenicity of a subunit hepatitis C virus vaccine, inducing neutralizing antibodies which confer protection in mice","volume":"90","author":"Li","year":"2016","journal-title":"J. Virol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"e01403-18","DOI":"10.1128\/JVI.01403-18","article-title":"Antigenicity and immunogenicity of differentially glycosylated HCV E2 envelop proteins expressed in mammalian and insect cells","volume":"93","author":"Urbanowicz","year":"2019","journal-title":"J. Virol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"5889","DOI":"10.1128\/JVI.77.10.5889-5901.2003","article-title":"Hyperglycosylated mutants of human immunodeficiency virus (HIV) type 1 monomeric gp120 as novel antigens for HIV vaccine design","volume":"77","author":"Pantophlet","year":"2003","journal-title":"J. Virol."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"14002","DOI":"10.1128\/JVI.02614-14","article-title":"Hyperglycosylated stable core immunogens designed to present the CD4 binding site are preferentially recognized by broadly neutralizing antibodies","volume":"88","author":"Ingale","year":"2014","journal-title":"J. Virol."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"e00677-17","DOI":"10.1128\/JVI.00677-17","article-title":"Reducing V3 antigenicity and immunogenicity on soluble, native-like HIV-1 Env SOSIP trimers","volume":"91","author":"Ringe","year":"2017","journal-title":"J. Virol."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"1670","DOI":"10.1002\/hep.28108","article-title":"Antibodies to an interfering epitope in hepatitis C virus E2 can mask vaccine-induced neutralizing activity","volume":"62","author":"Kachko","year":"2015","journal-title":"Hepatology"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"7537","DOI":"10.1073\/pnas.0902749106","article-title":"Depletion of interfering antibodies in chronic hepatitis C patients and vaccinated chimpanzees reveals broad cross-genotype neutralizing activity","volume":"106","author":"Zhang","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_141","doi-asserted-by":"crossref","unstructured":"Hajarizadeh, B., Grebely, J., Byrne, M., Marks, P., Amin, J., McManus, H., Butler, T., Cunningham, E.B., Vickerman, P., and Martin, N.K. (2021). Evaluation of hepatitis C treatment-as-prevention within Australian prisons (SToP-C): A prospective cohort study. Lancet Gastroenterol. Hepatol.","DOI":"10.1016\/S2468-1253(21)00077-7"},{"key":"ref_142","doi-asserted-by":"crossref","unstructured":"Hu, T.-H., Su, W.-W., Yang, C.-C., Yang, C.-C., Kuo, W.-H., Chen, Y.-Y., Yeh, Y.-H., Chen, S.-S., Tsao, Y.-Y., and Chen, K.-M. (2021). Elimination of Hepatitis C Virus in a Dialysis Population: A Collaborative Care Model in Taiwan. Am. J. Kidney Dis.","DOI":"10.1053\/j.ajkd.2021.03.017"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"783","DOI":"10.4049\/jimmunol.1302563","article-title":"Ficolin-2 Inhibits Hepatitis C Virus Infection, whereas Apolipoprotein E3 Mediates Viral Immune Escape","volume":"193","author":"Zhao","year":"2014","journal-title":"J. Immunol."},{"key":"ref_144","doi-asserted-by":"crossref","unstructured":"Izquierdo, L., Oliveira, C., Fournier, C., Descamps, V., Morel, V., Dubuisson, J., Brochot, E., Francois, C., Castelain, S., and Duverlie, G. (2016). Hepatitis C Virus Resistance to Carbohydrate-Binding Agents. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0149064"}],"container-title":["Pathogens"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-0817\/10\/6\/685\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T06:09:45Z","timestamp":1760162985000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-0817\/10\/6\/685"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,6,1]]},"references-count":144,"journal-issue":{"issue":"6","published-online":{"date-parts":[[2021,6]]}},"alternative-id":["pathogens10060685"],"URL":"https:\/\/doi.org\/10.3390\/pathogens10060685","relation":{},"ISSN":["2076-0817"],"issn-type":[{"value":"2076-0817","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,6,1]]}}}