Evidence map›Paper›PMID 26555397›Full record

ArticleMicrobial cell factories2015

A new potential secretion pathway for recombinant proteins in Bacillus subtilis.

Guangqiang Wang, Yongjun Xia, Zhennan Gu, Hao Zhang, Yong Q Chen, Haiqin Chen, Lianzhong Ai, Wei Chen

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
4.1field-weighted citation impact, top 7% 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

12 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Article
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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 2 institutions in 1 country.

Guangqiang WangSchool of Medical Instrument and Food Engineering, University of Shanghai for Science and Technology, Shanghai, 200093, People's Republic of China. 1015wanggq@163.com.
Yongjun XiaSchool of Medical Instrument and Food Engineering, University of Shanghai for Science and Technology, Shanghai, 200093, People's Republic of China. dreamup@126.com.
Zhennan GuState Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi, 214122, People's Republic of China. zhennangu@jiangnan.edu.cn.
Hao ZhangState Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi, 214122, People's Republic of China. zhanghao@jiangnan.edu.cn.
Yong Q ChenState Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi, 214122, People's Republic of China. yqchen@jiangnan.edu.cn.
Haiqin ChenState Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi, 214122, People's Republic of China. haiqinchen@jiangnan.edu.cn.
Lianzhong AiSchool of Medical Instrument and Food Engineering, University of Shanghai for Science and Technology, Shanghai, 200093, People's Republic of China. ailianzhong@163.com.
Wei ChenState Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi, 214122, People's Republic of China. chenwei66@jiangnan.edu.cn.
Jiangnan University · CNUniversity of Shanghai for Science and Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundSecretion of cytoplasmic expressed proteins into growth media has significant advantages. Due to the lack of an outer membrane, Bacillus subtilis is considered as a desirable 'cell factory' for the secretion of recombinant proteins. However, bottlenecks in the classical pathway for the secretion of recombinant proteins limit its use on a wide scale. In this study, we attempted to use four typical non-classically secreted proteins as signals to export three recombinant model proteins to the culture medium.

resultsAll four non-classically secreted proteins can direct the export of the intrinsically disordered nucleoskeletal-like protein (Nsp). Two of them can guide the secretion of alkaline phosphatase (PhoA). One can lead the secretion of the thermostable β-galactosidase BgaB, which cannot be secreted with the aid of typical Sec-dependent signal peptides.

conclusionOur results show that the non-classically secreted proteins lead the recombinant proteins to the culture medium, and thus non-classical protein secretion pathways can be exploited as a novel secretion pathway for recombinant proteins.

Indexed as

Alkaline PhosphataseBacillus subtilisBacterial Proteinsbeta-GalactosidaseGenotypePlasmidsProtein Sorting SignalsRecombinant Fusion ProteinsAlkaline PhosphataseBacterial Proteinsbeta-GalactosidaseProtein Sorting SignalsRecombinant Fusion Proteins

Identifiers

PMID26555397
PMCPMC4641360
OpenAlexW2128025835

What OpenQuestion holds

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LicenceCC BY
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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.