Evidence map›Paper›PMID 25941931›Full record

ArticleInternational journal of molecular sciences2015

Escherichia coli Maltose-Binding Protein Induces M1 Polarity of RAW264.7 Macrophage Cells via a TLR2- and TLR4-Dependent Manner.

Wan Wang, Hong-Yan Yuan, Guo-Mu Liu, Wei-Hua Ni, Fang Wang, Gui-Xiang Tai

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.4field-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

8 citing papers in PubMed, 16 citations in OpenAlex.

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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

6 authors at 1 institution in 1 country.

Wan WangDepartment of Immunology, College of Basic Medical Science, Jilin University, 126 Xinmin Street, Changchun 130021, China. wangwan0106@yahoo.com.
Hong-Yan YuanDepartment of Immunology, College of Basic Medical Science, Jilin University, 126 Xinmin Street, Changchun 130021, China. yuanhy@jlu.edu.cn.
Guo-Mu LiuDepartment of Immunology, College of Basic Medical Science, Jilin University, 126 Xinmin Street, Changchun 130021, China. liuguomu@126.com.
Wei-Hua NiDepartment of Immunology, College of Basic Medical Science, Jilin University, 126 Xinmin Street, Changchun 130021, China. niwh5566@jlu.edu.cn.
Fang WangDepartment of Immunology, College of Basic Medical Science, Jilin University, 126 Xinmin Street, Changchun 130021, China. fangfang5460@126.com.
Gui-Xiang TaiDepartment of Immunology, College of Basic Medical Science, Jilin University, 126 Xinmin Street, Changchun 130021, China. taiguixiang@163.com.
Jilin University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Maltose-binding protein (MBP) is a critical player of the maltose/maltodextrin transport system in Escherichia coli. Our previous studies have revealed that MBP nonspecifically induces T helper type 1 (Th1) cell activation and activates peritoneal macrophages obtained from mouse. In the present study, we reported a direct stimulatory effect of MBP on RAW264.7 cells, a murine macrophage cell line. When stimulated with MBP, the production of nitric oxide (NO), IL-1β, IL-6 and IL-12p70, and the expressions of CD80, MHC class II and inducible nitric oxide synthase (iNOS) were all increased in RAW264.7 cells, indicating the activation and polarization of RAW264.7 cells into M1 macrophages induced by MBP. Further study showed that MBP stimulation upregulated the expression of TLR2 and TLR4 on RAW264.7 cells, which was accompanied by subsequent phosphorylation of IκB-α and p38 MAPK. Pretreatment with anti-TLR2 or anti-TLR4 antibodies largely inhibited the phosphorylation of IκB-α and p38 MAPK, and greatly reduced MBP-induced NO and IL-12p70 production, suggesting that the MBP-induced macrophage activation and polarization were mediated by TLR2 and TLR4 signaling pathways. The observed results were independent of lipopolysaccharide contamination. Our study provides a new insight into a mechanism by which MBP enhances immune responses and warrants the potential application of MBP as an immune adjuvant in immune therapies.

Indexed as

AnimalsBiomarkersCell PolarityCell SurvivalCytokinesEscherichia coli ProteinsHistocompatibility Antigens Class IInflammation MediatorsMacrophagesMAP Kinase Signaling SystemMiceNF-kappa BNitric OxideNitric Oxide Synthase Type IIp38 Mitogen-Activated Protein KinasesPeriplasmic Binding ProteinsBiomarkersCytokinesEscherichia coli ProteinsHistocompatibility Antigens Class IInflammation MediatorsMalE protein, E coliNF-kappa BNitric OxideNitric Oxide Synthase Type IIp38 Mitogen-Activated Protein KinasesPeriplasmic Binding ProteinsToll-Like Receptor 2Toll-Like Receptor 4

Identifiers

PMID25941931
PMCPMC4463623
OpenAlexW2084735562

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.