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TitleViral neutralization by antibody-imposed physical disruption.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 116, Issue 52, Page 26933-26940, Year 2019
Publish dateDec 26, 2019
AuthorsQingbing Zheng / Jie Jiang / Maozhou He / Zizheng Zheng / Hai Yu / Tingting Li / Wenhui Xue / Zimin Tang / Dong Ying / Zekai Li / Shuo Song / Xinlin Liu / Kaihang Wang / Zhiqing Zhang / Daning Wang / Yingbin Wang / Xiaodong Yan / Qinjian Zhao / Jun Zhang / Ying Gu / Shaowei Li / Ningshao Xia /
PubMed AbstractIn adaptive immunity, organisms produce neutralizing antibodies (nAbs) to eliminate invading pathogens. Here, we explored whether viral neutralization could be attained through the physical ...In adaptive immunity, organisms produce neutralizing antibodies (nAbs) to eliminate invading pathogens. Here, we explored whether viral neutralization could be attained through the physical disruption of a virus upon nAb binding. We report the neutralization mechanism of a potent nAb 8C11 against the hepatitis E virus (HEV), a nonenveloped positive-sense single-stranded RNA virus associated with abundant acute hepatitis. The 8C11 binding flanks the protrusion spike of the HEV viruslike particles (VLPs) and leads to tremendous physical collision between the antibody and the capsid, dissociating the VLPs into homodimer species within 2 h. Cryo-electron microscopy reconstruction of the dissociation intermediates at an earlier (15-min) stage revealed smeared protrusion spikes and a loss of icosahedral symmetry with the capsid core remaining unchanged. This structural disruption leads to the presence of only a few native HEV virions in the ultracentrifugation pellet and exposes the viral genome. Conceptually, we propose a strategy to raise collision-inducing nAbs against single spike moieties that feature in the context of the entire pathogen at positions where the neighboring space cannot afford to accommodate an antibody. This rationale may facilitate unique vaccine development and antimicrobial antibody design.
External linksProc Natl Acad Sci U S A / PubMed:31818956 / PubMed Central
MethodsEM (single particle)
Resolution3.4 - 7.2 Å
Structure data

EMDB-0861:
The cryo-EM structure of HEV VLP in complex with Fab 3B6
Method: EM (single particle) / Resolution: 7.2 Å

0863

6lat

EMDB-0863, PDB-6lat:
The cryo-EM structure of HEV VLP
Method: EM (single particle) / Resolution: 3.4 Å

0866

6lb0

EMDB-0866, PDB-6lb0:
The cryo-EM structure of HEV VLP in complex with Fab 8C11
Method: EM (single particle) / Resolution: 3.6 Å

Source
  • hepatitis e virus
KeywordsVIRUS LIKE PARTICLE / HEV / T=1 / Neutralizing antibody / immune-complex

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