Evidence map›Paper›PMID 28228147›Full record

ArticleMicrobial cell factories2017

Artificially designed recombinant protein composed of multiple epitopes of foot-and-mouth disease virus as a vaccine candidate.

Ho-Bin Lee, Da-Chuan Piao, Jun-Yeong Lee, Jae-Yun Choi, Jin-Duck Bok, Chong-Su Cho, Sang-Kee Kang, Yun-Jaie Choi

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
6.5field-weighted citation impact, top 4% 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

17 citing papers in PubMed, 33 citations in OpenAlex.

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  16. Development of Peptide Vaccines in Dengue.Current pharmaceutical design · 2018
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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 at 1 institution in 1 country.

Ho-Bin LeeDepartment of Agricultural Biotechnology, Seoul National University, Seoul, 115-921, Republic of Korea.
Da-Chuan PiaoDepartment of Agricultural Biotechnology, Seoul National University, Seoul, 115-921, Republic of Korea.
Jun-Yeong LeeDepartment of Agricultural Biotechnology, Seoul National University, Seoul, 115-921, Republic of Korea.
Jae-Yun ChoiDepartment of Agricultural Biotechnology, Seoul National University, Seoul, 115-921, Republic of Korea.
Jin-Duck BokInstitute of Green-Bio Science and Technology, Seoul National University, 1447-1 Pyeongchang-Daero, Daehwa-Myeon, Pyeongchang-Gun, Gangwon-Do, 25354, Republic of Korea.
Chong-Su ChoDepartment of Agricultural Biotechnology, Seoul National University, Seoul, 115-921, Republic of Korea.
Sang-Kee KangInstitute of Green-Bio Science and Technology, Seoul National University, 1447-1 Pyeongchang-Daero, Daehwa-Myeon, Pyeongchang-Gun, Gangwon-Do, 25354, Republic of Korea. kangsk01@snu.ac.kr.
Yun-Jaie ChoiDepartment of Agricultural Biotechnology, Seoul National University, Seoul, 115-921, Republic of Korea. cyjcow@snu.ac.kr.
Seoul National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundConcerns regarding the safety of inactivated foot-and-mouth disease (FMD) vaccine have been raised since it is produced from cultured live FMD virus (FMDV). To overcome this issue, recombinant protein has been studied as an alternative vaccine. RESULTS AND

conclusionWe designed a chimerical multi-epitope recombinant protein (5BT), which is comprised of tandem repeats of five B cell epitopes (residue of VP1 136-162) derived from different FMDV variants and one T-cell epitope (residue of 3A 21-35). To increase solubility and stability of 5BT, it was conjugated with BmpB, the membrane protein B of Brachyspira hyodysenteriae (B5BT). Our results indicated that 5BT was susceptible to degradation by host protease and produced with substantial fraction of inclusion body. The stability and solubility of 5BT was greatly increased by conjugating to BmpB. FMDV specific antibodies were observed in the serum of mice immunized with 5BT and B5BT comparable to inactivated FMD vaccine. Sera from 5BT and B5BT groups also exhibited high epitope-specific antibody titers in peptide specific ELISA, indicating that all five epitopes are exposed to the B cell receptor for the antibody reaction. Thus the multi-epitope recombinant protein designed in this study may be a potential candidate as an alternative vaccine against FMDV epidemic variants.

Indexed as

AnimalsAntibodies, NeutralizingAntibodies, ViralBacterial Outer Membrane ProteinsEnzyme-Linked Immunosorbent AssayEpitopes, B-LymphocyteEpitopes, T-LymphocyteFemaleFoot-and-Mouth Disease VirusLipoproteinsMiceRecombinant Fusion ProteinsVaccines, SyntheticViral VaccinesAntibodies, NeutralizingAntibodies, ViralBacterial Outer Membrane ProteinsBmpB protein, Brachyspira hyodysenteriaeEpitopes, B-LymphocyteEpitopes, T-LymphocyteLipoproteinsRecombinant Fusion ProteinsVaccines, SyntheticViral VaccinesArtificial recombinant proteinB cell epitopeFMDVGH loopMulti- epitope

Identifiers

PMID28228147
PMCPMC5322615
OpenAlexW2589879893

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.