Evidence map›Paper›PMID 35524776›Full record

ArticleApplied microbiology and biotechnology2022

Designing a novel E2-IFN-γ fusion protein against CSFV by immunoinformatics and structural vaccinology approaches.

Yanmin Zhang, Weijian Zhang, Jun Cheng, Xuping Liu, Shiwei Miao, Wen-Song Tan, Liang Zhao

Abstract read
PubMed Publisher
In one paragraph

Article in Applied microbiology and biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 37% of its field
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

3 citing papers in PubMed, 2 citations in OpenAlex.

  1. Review
  2. Strategies of Classical Swine Fever Immune Evasion.International journal of molecular sciences · 2025
    Review
  3. 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

7 authors at 3 institutions in 1 country.

Yanmin ZhangThe State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, P. O. Box 309#, Shanghai, 200237, China.
Weijian ZhangThe State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, P. O. Box 309#, Shanghai, 200237, China.
Jun ChengThe State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, P. O. Box 309#, Shanghai, 200237, China.
Xuping LiuShanghai Bioengine Sci-Tech Co., Ltd, Shanghai, 201203, China.
Shiwei MiaoHangzhou Sumgen Biotech Co., Ltd, Zhejiang, 310056, China.
Wen-Song TanThe State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, P. O. Box 309#, Shanghai, 200237, China.
Liang ZhaoThe State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, P. O. Box 309#, Shanghai, 200237, China. zhaoliang@ecust.edu.cn.ORCID http://orcid.org/0000-0001-8077-3617
East China University of Science and Technology · CNHangzhou DAC Biotech (China) · CNViva Biotech (China) · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Subunit vaccines with high purity and safety are gradually becoming a main trend in vaccinology. However, adjuvants such as interferon-gamma (IFN-γ) are required to enhance immune responses of subunit vaccines due to their poor immunogenicity. The conjugation of antigen with adjuvant can induce more potent immune responses compared to the mixture of antigen and adjuvant. At the same time, the selection of linker, indispensable in the construction of the stable and bioactive fusion proteins, is complicated and time-consuming. The development of immunoinformatics and structural vaccinology approaches provides a means to address the abovementioned problem. Therefore, in this study, a E2-IFN-γ fusion protein with an optimal linker (E2-R2-PIFN) was designed by bioinformatics approaches to improve the immunogenicity of the classical swine fever virus (CSFV) E2 subunit vaccine. Moreover, the E2-R2-PIFN fusion protein was expressed in HEK293T cells and the biological effects of IFN-γ in E2-R2-PIFN were confirmed in vitro via Western blotting. Here, an alternative method is utilized to simplify the design and validation of the antigen-adjuvant fusion protein, providing a potential subunit vaccine candidate against CSFV. KEY POINTS: • An effective and simple workflow of antigen-adjuvant fusion protein design and validation was established by immunoinformatics and structural vaccinology. • A novel E2-IFN-γ fusion protein with an optimal linker was designed as a potential CSFV vaccine. • The bioactivity of the newly designed fusion protein was preliminarily validated through in vitro experiments.

Indexed as

Classical Swine FeverClassical Swine Fever VirusViral VaccinesAdjuvants, ImmunologicAnimalsAntibodies, ViralHEK293 CellsHumansInterferon-gammaSwineVaccines, SubunitVaccinologyViral Envelope ProteinsAdjuvants, ImmunologicAntibodies, ViralInterferon-gammaVaccines, SubunitViral Envelope ProteinsViral VaccinesCSFV E2 proteinFusion proteinIFN-γImmunoinformaticsLinkerStructural vaccinology

Identifiers

PMID35524776
OpenAlexW4229008811

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.