Evidence map›Paper›PMID 40841372›Full record

ArticleNature communications2025

Highly scalable prefusion-stabilized RSV F vaccine with enhanced immunogenicity and robust protection.

Qingrui Huang, Qingyun Lang, Yao Li, Fengjie Wang, Xiaonan Han, Ling Luo, Xiaomin Duan, Xuerong Cao, Yue Wang, Yu Bai and 6 more

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026
    Review
  5. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

16 authors.

Qingrui Huang *Changping Laboratory, Beijing, China. huangqr@cpl.ac.cn.ORCID http://orcid.org/0009-0007-2076-3805
Qingyun Lang *Changping Laboratory, Beijing, China.
Yao Li *Changping Laboratory, Beijing, China.
Fengjie Wang *Laboratory of Virology, Beijing Key Laboratory of Etiology of Viral Diseases in Children, Capital Institute of Pediatrics, Beijing, China.
Xiaonan HanCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.
Ling LuoChangping Laboratory, Beijing, China.
Xiaomin DuanChangping Laboratory, Beijing, China.
Xuerong CaoChangping Laboratory, Beijing, China.
Yue WangCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.ORCID http://orcid.org/0000-0001-6946-2666
Yu BaiChangping Laboratory, Beijing, China.
Yaxin SongChangping Laboratory, Beijing, China.
Yanpeng XuLaboratory of Virology, Beijing Key Laboratory of Etiology of Viral Diseases in Children, Capital Institute of Pediatrics, Beijing, China.ORCID http://orcid.org/0000-0001-8764-4412
Lianlian BianChangping Laboratory, Beijing, China.
Chenyan GaoChangping Laboratory, Beijing, China.
Linqing ZhaoLaboratory of Virology, Beijing Key Laboratory of Etiology of Viral Diseases in Children, Capital Institute of Pediatrics, Beijing, China. zhaolinqing@shouer.com.cn.ORCID http://orcid.org/0000-0002-5622-1959
Jinghua YanChangping Laboratory, Beijing, China. yanjh@cpl.ac.cn.ORCID http://orcid.org/0009-0003-3238-255X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Stabilizing the RSV F protein in its prefusion conformation is crucial for effective vaccine development but has remained a significant challenge. Traditional stabilization methods, such as disulfide bonds and cavity-filling mutations, have been labor-intensive and have often resulted in suboptimal expression levels. Here, we report the design of an RSV prefusion F (preF) antigen using a proline-scanning strategy, incorporating seven proline substitutions to achieve stabilization. The resulting variant, preF7P, is structurally and biochemically validated to maintain the correct prefusion state. PreF7P demonstrates superior immunogenicity with a 1.8-fold increase in neutralizing antibody titers when compared to DS-cav2, and provides protection from clinical disease against both RSV A and B strains in female murine and female cotton rat models. In clinical development, preF7P exhibits high expression levels (~10 g/L) in clinical-grade CHO cells. The clinical-grade vaccine elicits robust immunogenic responses across female mice, female SD rats, and both male and female cynomolgus macaques, significantly boosting RSV pre-infection neutralizing antibody titers, and providing sustained protection for at least six months in female mice. This proline-scanning strategy offers a streamlined approach for stabilizing class I fusion proteins, potentially accelerating the development of vaccines for other pathogens.

Indexed as

Immunogenicity, VaccineRespiratory Syncytial Virus, HumanRespiratory Syncytial Virus InfectionsRespiratory Syncytial Virus VaccinesViral Fusion ProteinsAnimalsAntibodies, NeutralizingAntibodies, ViralCHO CellsCricetulusFemaleHumansMacaca fascicularisMaleMiceRatsAntibodies, NeutralizingAntibodies, ViralRespiratory Syncytial Virus VaccinesViral Fusion Proteins

Identifiers

PMID40841372
PMCPMC12370985

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.