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TitleNative-like soluble E1E2 glycoprotein heterodimers on self-assembling protein nanoparticles for hepatitis C virus vaccine design.
Journal, issue, pagesNat Commun, Vol. 17, Issue 1, Year 2026
Publish dateFeb 11, 2026
AuthorsLinling He / Yi-Zong Lee / Yi-Nan Zhang / Maddy L Newby / Benjamin M Janus / Fabrizio G Gonzalez / Garrett Ward / Connor DesRoberts / Shr-Hau Hung / Erick Giang / Joel D Allen / Liudmila Kulakova / Eric A Toth / Thomas R Fuerst / Mansun Law / Gilad Ofek / Max Crispin / Jiang Zhu /
PubMed AbstractHepatitis C virus (HCV) is a leading cause of chronic liver disease, cirrhosis, and hepatocellular carcinoma worldwide. Development of an E1E2-based HCV vaccine has been hindered by the difficulty of ...Hepatitis C virus (HCV) is a leading cause of chronic liver disease, cirrhosis, and hepatocellular carcinoma worldwide. Development of an E1E2-based HCV vaccine has been hindered by the difficulty of producing a soluble E1E2 (sE1E2) antigen that faithfully recapitulates the native virion-associated heterodimer. Guided by cryo-electron microscopy (cryo-EM) structures, we engineer genotype 1a H77 sE1E2 by truncating the E1 and E2 stems (Cut), deleting a putative fusion peptide-containing region in E1 (Cut), and stabilizing the heterodimer using diverse scaffolds. All H77 sE1E2.Cut scaffolds exhibit native-like E1-E2 association and strong binding to the broadly neutralizing antibody (bNAb) AR4A. A genotype 1a HCV-1 sE1E2.Cut variant scaffolded by a modified SpyTag/SpyCatcher (SPYΔN) is selected for in vitro and in vivo characterization, as well as further construct refinement. The structure of this HCV-1 sE1E2 construct in complex with bNAbs is determined by cryo-EM and negative-stain EM (nsEM), with an nsEM-based strategy established for antibody epitope mapping. HCV-1 sE1E2.Cut.SPYΔN is displayed on self-assembling protein nanoparticles (SApNPs) to enhance immunogenicity. The HCV-1 sE1E2.Cut.SPYΔN heterodimer and SApNPs bearing wildtype or modified glycans are evaluated in mice, alongside E2 core-based immunogens for comparison. Together, these results establish a framework for advancing E1E2-based HCV vaccines toward clinical development.
External linksNat Commun / PubMed:41673395 / PubMed Central
MethodsEM (single particle)
Resolution4.97 - 6.3 Å
Structure data

EMDB-70622: Hepatitis C virus sE1E2.Cut1+2.SPYdeltaN bound to antibodies AR4A and AR3C
Method: EM (single particle) / Resolution: 4.97 Å

EMDB-70623: Hepatitis C virus sE1E2.Cut1+2.SPYdeltaN bound to antibodies AR4A and HEPC74
Method: EM (single particle) / Resolution: 6.3 Å

Source
  • Homo sapiens (human)

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