Evidence map›Paper›PMID 37768347›Full record

ArticleApplied microbiology and biotechnology2023

Production of recombinant human long-acting IL-18 binding protein: inhibitory effect on ulcerative colitis in mice.

Lei Guo, Xiuze Chen, Haifeng Zeng, Na Tian, Weijie Lu, Jizhou Zhang, Yechen Xiao

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Article in Applied microbiology and biotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.5field-weighted citation impact, top 32% 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

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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

0 citing papers in PubMed, 3 citations in OpenAlex.

No citing paper in PubMed yet.

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.

Lei GuoDepartment of Biotechnology, College of Basic Medical Science, Guangdong Medical University, Dongguan, 523808, China.
Xiuze ChenDepartment of Biotechnology, College of Basic Medical Science, Guangdong Medical University, Dongguan, 523808, China.
Haifeng ZengGuangdong Provincial Key Laboratory of Medical Molecular Diagnostics, Guangdong Medical University, Dongguan, 523808, China.
Na TianJilin Tuohua Biotechnology Co., LTD, Siping, 136001, China.
Weijie LuDepartment of Biotechnology, College of Basic Medical Science, Guangdong Medical University, Dongguan, 523808, China.
Jizhou ZhangDepartment of Biochemistry and Molecular Biology, College of Basic Medical Science, Jilin University, Changchun, 130021, China. zhangjizhou7601@yahoo.com.cn.
Yechen XiaoDepartment of Biotechnology, College of Basic Medical Science, Guangdong Medical University, Dongguan, 523808, China. yechenxiao2400@126.com.ORCID http://orcid.org/0000-0002-6238-966X
Guangdong Medical College · CNJilin Normal University · CNJilin University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Interleukin-18 binding protein (IL-18BP) is a natural IL-18 inhibitor in vivo, which can effectively neutralize IL-18 and inhibit the inflammatory signaling pathway induced by IL-18, thus playing an anti-inflammatory role. Traditional production methods primarily rely on eukaryotic animal cell expression systems, which often entail complex processes, lower yields, and increase production costs. In this study, we present a novel approach for expressing IL-18BP fusion protein using the Escherichia coli (E. coli) system. The N-terminal segment of IL-18BP was fused with the small ubiquitin-related modifier (SUMO) tag, enabling soluble expression, while the C-terminal segment was fused with the human IgG1 Fc fragment to prolong its in vivo lifespan. Through screening, we obtained a high-expression engineering strain from a single colony and developed optimized protocols for fermentation and purification of the recombinant SUMO-IL-18BP-Fc protein. The SUMO tag was subsequently cleaved using SUMO protease, and the purified recombinant human IL-18BP-Fc (rhIL-18BP-Fc) exhibited a purity exceeding 90% with a yield of 1 g per liter of bacterial solution. The biological activities and underlying mechanisms of rhIL-18BP-Fc were evaluated using cell lines and a mouse model. Our results demonstrated that rhIL-18BP-Fc effectively inhibited IL-18-stimulated IFN-γ production in KG-1a cells in vitro and ameliorated DSS-induced ulcerative colitis in mice. In conclusion, we successfully employed the SUMO fusion system to achieve high-level production, soluble expression, and prolonged activity of rhIL-18BP-Fc in E. coli. These findings lay the groundwork for future large-scale industrial production and pharmaceutical development of rhIL-18BP-Fc protein. KEY POINTS: • Effective expression, fermentation, and purification of bioactive rhIL-18BP-Fc protein in E. coli. • The rhIL-18BP-Fc protein has a great potential for the therapy of ulcerative colitis by inhibiting the expression of inflammatory factors.

Indexed as

Colitis, UlcerativeInterleukin-18AnimalsEscherichia coliHumansIntercellular Signaling Peptides and ProteinsMiceRecombinant Fusion ProteinsRecombinant ProteinsIntercellular Signaling Peptides and ProteinsInterleukin-18interleukin-18 binding proteinRecombinant Fusion ProteinsRecombinant ProteinsHuman IgG1 Fc fragmentIL-18BPSUMO tagUlcerative colitis

Identifiers

PMID37768347
OpenAlexW4387114825

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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.