A single residue switch mediates the broad neutralization of Rotaviruses Article Swipe
Yang Huang
,
Feibo Song
,
Yuanjun Zeng
,
Hui Sun
,
Roufang Sheng
,
Xuechun Wang
,
Liqin Liu
,
Guoxing Luo
,
Yanan Jiang
,
Yaling Chen
,
Mengxuan Zhang
,
Shiyin Zhang
,
Ying Gu
,
Hai Yu
,
Shaowei Li
,
Tingdong Li
,
Qingbing Zheng
,
Shengxiang Ge
,
Jun Zhang
,
Ningshao Xia
·
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.1038/s41467-025-56114-3
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.1038/s41467-025-56114-3
Broadly neutralizing antibodies (bNAbs) could offer escape-tolerant and lasting protection against viral infections and therefore guide development of broad-spectrum vaccines. The increasing challenge posed by viral evolution and immune evasion intensifies the importance of the discovery of bNAbs and their underlying neutralization mechanism. Here, focusing on the pivotal viral protein VP4 of rotavirus (RV), we identify a potent bNAb, 7H13, exhibiting broad-spectrum neutralization across diverse RV genotypes and demonstrating strong prevention of virus infection in female mice. A combination of time-resolved cryo-electron microscopy (cryo-EM) and in situ cryo-electron tomography (cryo-ET) analysis reveals a counterintuitive dynamic process of virus inactivation, in which 7H13 asymmetrically binds to a conserved epitope in the capsid-proximal aspect of VP4, triggers a conformational switch in a critical residue-F418-thereby disrupts the meta-stable conformation of VP4 essential for normal viral infection. Structure-guided mutagenesis corroborates the essential role of the 7H13 heavy chain I54 in activating F418 switch and destabilizing VP4. These findings define an atypical NAbs' neutralization mechanism and reveal a potential type of virus vulnerable site for universal vaccine and therapeutics design.
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Metadata
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1038/s41467-025-56114-3
- https://www.nature.com/articles/s41467-025-56114-3.pdf
- OA Status
- gold
- Cited By
- 3
- References
- 69
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4406619953
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
-
https://openalex.org/W4406619953Canonical identifier for this work in OpenAlex
- DOI
-
https://doi.org/10.1038/s41467-025-56114-3Digital Object Identifier
- Title
-
A single residue switch mediates the broad neutralization of RotavirusesWork title
- Type
-
articleOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2025Year of publication
- Publication date
-
2025-01-20Full publication date if available
- Authors
-
Yang Huang, Feibo Song, Yuanjun Zeng, Hui Sun, Roufang Sheng, Xuechun Wang, Liqin Liu, Guoxing Luo, Yanan Jiang, Yaling Chen, Mengxuan Zhang, Shiyin Zhang, Ying Gu, Hai Yu, Shaowei Li, Tingdong Li, Qingbing Zheng, Shengxiang Ge, Jun Zhang, Ningshao XiaList of authors in order
- Landing page
-
https://doi.org/10.1038/s41467-025-56114-3Publisher landing page
- PDF URL
-
https://www.nature.com/articles/s41467-025-56114-3.pdfDirect link to full text PDF
- Open access
-
YesWhether a free full text is available
- OA status
-
goldOpen access status per OpenAlex
- OA URL
-
https://www.nature.com/articles/s41467-025-56114-3.pdfDirect OA link when available
- Concepts
-
Neutralization, Virology, Rotavirus, Virus, Capsid, Epitope, Biology, Mutagenesis, Viral protein, Viral entry, Neutralizing antibody, Immune escape, Antibody, Viral replication, Biophysics, Cell biology, Immune system, Mutation, Genetics, GeneTop concepts (fields/topics) attached by OpenAlex
- Cited by
-
3Total citation count in OpenAlex
- Citations by year (recent)
-
2025: 3Per-year citation counts (last 5 years)
- References (count)
-
69Number of works referenced by this work
- Related works (count)
-
10Other works algorithmically related by OpenAlex
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| corresponding_author_ids | https://openalex.org/A5078732636 |
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| corresponding_institution_ids | https://openalex.org/I200296433 |
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| citation_normalized_percentile.is_in_top_10_percent | True |