Evidence map›Paper›PMID 31758487›Full record

ArticleMolecular biotechnology2020

Prokaryotic Expression, In Vitro Biological Analysis, and In Silico Structural Evaluation of Guinea Pig IL-4.

Madhavan Omanakuttan, Hanumohan R Konatham, Vijaya R Dirisala, Amminikutty Jeevan, Shradha Mawatwal, Rohan Dhiman, Lan H Ly, David McMurray

Abstract read
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In one paragraph

Article in Molecular biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 52% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. 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

8 authors at 4 institutions in 2 countries.

Madhavan OmanakuttanDepartment of Biotechnology, Vignan's Foundation for Science, Technology & Research, Guntur, Andhra Pradesh, 522213, India.
Hanumohan R KonathamDepartment of Biotechnology, Vignan's Foundation for Science, Technology & Research, Guntur, Andhra Pradesh, 522213, India.
Vijaya R DirisalaDepartment of Biotechnology, Vignan's Foundation for Science, Technology & Research, Guntur, Andhra Pradesh, 522213, India. drdirisala@gmail.com.
Amminikutty JeevanDepartment of Microbial Pathogenesis and Immunology, College of Medicine, Texas A&M Health Science Center, College Station, TX, 77843, USA.
Shradha MawatwalLaboratory of Mycobacterial Immunology, Department of Life Science, National Institute of Technology, Rourkela, Odisha, 769008, India.
Rohan DhimanLaboratory of Mycobacterial Immunology, Department of Life Science, National Institute of Technology, Rourkela, Odisha, 769008, India.
Lan H LyDepartment of Microbial Pathogenesis and Immunology, College of Medicine, Texas A&M Health Science Center, College Station, TX, 77843, USA.
David McMurrayDepartment of Microbial Pathogenesis and Immunology, College of Medicine, Texas A&M Health Science Center, College Station, TX, 77843, USA.
Vignan's Foundation for Science, Technology & Research · INNational Institute of Technology Rourkela · INTexas A&M Health Science Center · USTexas A&M Health Science Center · US

Funding

SERB ECR/00304
6 · The paper itself

Abstract

Interleukin-4 is a signature cytokine of T-helper type 2 (Th2) cells that play a major role in shaping immune responses. Its role in highly relevant animal model of tuberculosis (TB) like guinea pig has not been studied till date. In the current study, the guinea pig IL-4 gene was cloned and expressed using a prokaryotic expression vector (pET30 a(+)). This approach yielded a recombinant protein of 19 kDa as confirmed by mass spectrometry analysis and named as recombinant guinea pig (rgp)IL-4 protein. The authenticity of the expression of rgpIL-4 protein was further verified through polyclonal anti-IL4 antiserum raised in rabbits that showed specific and strong binding with the recombinant protein. The biological activity of the rgpIL-4 was ascertained in RAW264.7 cells where LPS-treated nitric oxide (NO) production was found to be suppressed in the presence of this protein. The three-dimensional structure of guinea pig IL-4 was predicted by utilizing the template structure of human interleukin-4, which shared a sequence homology of 58%. The homology modeling result showed clear resemblance of guinea pig IL-4 structure with the human IL-4. Taken together, our study indicates that the newly expressed, biologically active rgpIL-4 protein could provide deeper understanding of the immune responses in guinea pig to different infectious diseases like TB and non-infectious ones.

Indexed as

AnimalsCloning, MolecularComputer SimulationGene ExpressionGenetic VectorsGuinea PigsHumansInterleukin-4Nitric OxideProtein ConformationRecombinant ProteinsIL4 protein, humanInterleukin-4Nitric OxideRecombinant ProteinsAssayGuinea pigHeterologous gene expressionIL-4ProteinTh2

Identifiers

PMID31758487
OpenAlexW2990035750

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.