Evidence map›Paper›PMID 27435429›Full record

ArticleHuman vaccines & immunotherapeutics2016

Immunogenicity and protective efficacy of rotavirus VP8* fused to cholera toxin B subunit in a mouse model.

Miaoge Xue, Linqi Yu, Lianzhi Jia, Yijian Li, Yuanjun Zeng, Tingdong Li, Shengxiang Ge, Ningshao Xia

Abstract read
In one paragraph

Article in Human vaccines & immunotherapeutics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

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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

8 authors.

Miaoge Xuea State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics , National Institute of Diagnostics and Vaccine Development in Infectious Diseases, School of Life Science and School of Public Health, Xiamen University , Xiamen , China.
Linqi Yua State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics , National Institute of Diagnostics and Vaccine Development in Infectious Diseases, School of Life Science and School of Public Health, Xiamen University , Xiamen , China.
Lianzhi Jiaa State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics , National Institute of Diagnostics and Vaccine Development in Infectious Diseases, School of Life Science and School of Public Health, Xiamen University , Xiamen , China.
Yijian Lia State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics , National Institute of Diagnostics and Vaccine Development in Infectious Diseases, School of Life Science and School of Public Health, Xiamen University , Xiamen , China.
Yuanjun Zenga State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics , National Institute of Diagnostics and Vaccine Development in Infectious Diseases, School of Life Science and School of Public Health, Xiamen University , Xiamen , China.
Tingdong Lia State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics , National Institute of Diagnostics and Vaccine Development in Infectious Diseases, School of Life Science and School of Public Health, Xiamen University , Xiamen , China.
Shengxiang Gea State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics , National Institute of Diagnostics and Vaccine Development in Infectious Diseases, School of Life Science and School of Public Health, Xiamen University , Xiamen , China.
Ningshao Xiaa State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics , National Institute of Diagnostics and Vaccine Development in Infectious Diseases, School of Life Science and School of Public Health, Xiamen University , Xiamen , China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In attempts to develop recombinant subunit vaccines against rotavirus disease, it was previously shown that the N-terminal truncated VP8* protein, VP8-1 (aa26-231), is a good vaccine candidate when used for immunization in combination with Freund's adjuvant. However, this protein stimulated only weak immune response when aluminum hydroxide was used as an adjuvant. In this study, the nontoxic B subunit of cholera toxin (CTB) was employed as intra-molecular adjuvant to improve the immunogenicity of VP8-1. Both, the N-terminal and C-terminal fusion proteins, were purified to homogeneity, at which stage they formed pentamers, and showed significantly higher immunogenicity and protective efficacy than a VP8-1/aluminum hydroxide mixture in a mouse model. Compared to VP8-1-CTB, CTB-VP8-1 showed higher binding activity to both, GM1 and the conformation sensitive neutralizing monoclonal antibodies specific to VP8. More importantly, CTB-VP8-1 elicited higher titers of neutralizing antibodies and conferred higher protective efficacy than VP8-1-CTB. Therefore, the protein CTB-VP8-1, with enhanced immunogenicity and immunoprotectivity, could be considered as a viable candidate for further development of an alternative, replication-incompetent, parenterally administered vaccine against rotavirus disease.

Indexed as

Adjuvants, ImmunologicAnimalsAntibodies, NeutralizingAntibodies, ViralCholera ToxinDisease Models, AnimalMice, Inbred BALB CRecombinant Fusion ProteinsRNA-Binding ProteinsRotavirus InfectionsRotavirus VaccinesVaccines, SubunitVaccines, SyntheticViral Nonstructural ProteinsAdjuvants, ImmunologicAntibodies, NeutralizingAntibodies, ViralCholera ToxinNS35 protein, rotavirusRecombinant Fusion ProteinsRNA-Binding ProteinsRotavirus VaccinesVaccines, SubunitVaccines, SyntheticViral Nonstructural Proteinscholera toxin B subunitdiarrheaneutralizing antibodyrotavirus vaccineVP8-1 protein

Identifiers

PMID27435429
PMCPMC5137547

What OpenQuestion holds

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Registered trials

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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.