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Structure paper

TitleCryo-EM structures of HCV E2 glycoprotein bound to neutralizing and non-neutralizing antibodies determined using bivalent Fabs as fiducial markers.
Journal, issue, pagesCommun Biol, Vol. 8, Issue 1, Page 825, Year 2025
Publish dateMay 29, 2025
AuthorsSalman Shahid / Sharanbasappa S Karade / S Saif Hasan / Rui Yin / Liqun Jiang / Yanxin Liu / Nathaniel Felbinger / Liudmila Kulakova / Eric A Toth / Zhen-Yong Keck / Steven K H Foung / Thomas R Fuerst / Brian G Pierce / Roy A Mariuzza /
PubMed AbstractGlobal elimination of hepatitis C virus (HCV) will require an effective cross-genotype vaccine. The HCV E2 envelope glycoprotein is the main target of neutralizing antibodies but also contains ...Global elimination of hepatitis C virus (HCV) will require an effective cross-genotype vaccine. The HCV E2 envelope glycoprotein is the main target of neutralizing antibodies but also contains epitopes that elicit non-neutralizing antibodies which may provide protection through Fc effector functions rather than direct neutralization. We determined cryo-EM structures of a broadly neutralizing antibody, a moderately neutralizing antibody, and a non-neutralizing antibody bound to E2 to resolutions of 3.8, 3.3, and 3.7 Å, respectively. Whereas the broadly neutralizing antibody targeted the front layer of E2 and the non-neutralizing antibody targeted the back layer, the moderately neutralizing antibody straddled both front and back layers, and thereby defined a new neutralizing epitope on E2. The small size of complexes between conventional (monovalent) Fabs and E2 (~110 kDa) presented a challenge for cryo-EM. Accordingly, we engineered bivalent versions of E2-specific Fabs that doubled the size of Fab-E2 complexes and conferred highly identifiable shapes to the complexes that facilitated particle selection and orientation for image processing. This study validates bivalent Fabs as new fiducial markers for cryo-EM analysis of small proteins such as HCV E2 and identifies a new target epitope for vaccine development.
External linksCommun Biol / PubMed:40442315 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.62 - 3.8 Å
Structure data

41245

8tgv

EMDB-41245, PDB-8tgv:
CryoEM structure of Fab HC84.26-HCV E2 complex
Method: EM (single particle) / Resolution: 3.75 Å

41247

8tgz

EMDB-41247, PDB-8tgz:
CryoEM structure of neutralizing antibody HC84.26 in complex with Hepatitis C virus envelope glycoprotein E2
Method: EM (single particle) / Resolution: 3.78 Å

41275

8thz

EMDB-41275, PDB-8thz:
CryoEM structure of neutralizing antibodies CBH-7 and HC84.26 in complex with Hepatitis C virus envelope glycoprotein E2
Method: EM (single particle) / Resolution: 3.25 Å

41703

8txq

EMDB-41703, PDB-8txq:
CryoEM structure of non-neutralizing antibody CBH-4B in complex with Hepatitis C virus envelope glycoprotein E2
Method: EM (single particle) / Resolution: 3.4 Å

41774

8tzy

EMDB-41774, PDB-8tzy:
CryoEM structure of non-neutralizing bivalent antibody CBH-4B in complex with Hepatitis C virus envelope glycoprotein E2
Method: EM (single particle) / Resolution: 3.8 Å

42041

8u9y

EMDB-42041, PDB-8u9y:
CryoEM structure of neutralizing antibody HC84.26 in complex with Hepatitis C virus envelope glycoprotein E2_New interface
Method: EM (single particle) / Resolution: 3.7 Å

PDB-8tfe:
Crystal structure of Fab fragment of anti-HCV E2 antibody (CBH-7)
Method: X-RAY DIFFRACTION / Resolution: 1.62 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-FLC:
CITRATE ANION

ChemComp-HOH:
WATER

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • homo sapiens (human)
  • hepacivirus c
  • hepatitis c virus (isolate 1)
  • hepacivirus
KeywordsIMMUNE SYSTEM / Antibody / E2 glycoprotein / Fab fragment / ANTIVIRAL PROTEIN / HCV / E2 / Fab / antiviral / complex / vaccine target / ternary complex / VIRAL PROTEIN/IMMUNE SYSTEM / VIRAL PROTEIN-IMMUNE SYSTEM complex

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