Cargando…
Escherichia coli Maltose-Binding Protein Induces M1 Polarity of RAW264.7 Macrophage Cells via a TLR2- and TLR4-Dependent Manner
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 stud...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4463623/ https://www.ncbi.nlm.nih.gov/pubmed/25941931 http://dx.doi.org/10.3390/ijms16059896 |
_version_ | 1782375802502905856 |
---|---|
author | Wang, Wan Yuan, Hong-Yan Liu, Guo-Mu Ni, Wei-Hua Wang, Fang Tai, Gui-Xiang |
author_facet | Wang, Wan Yuan, Hong-Yan Liu, Guo-Mu Ni, Wei-Hua Wang, Fang Tai, Gui-Xiang |
author_sort | Wang, Wan |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-4463623 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-44636232015-06-16 Escherichia coli Maltose-Binding Protein Induces M1 Polarity of RAW264.7 Macrophage Cells via a TLR2- and TLR4-Dependent Manner Wang, Wan Yuan, Hong-Yan Liu, Guo-Mu Ni, Wei-Hua Wang, Fang Tai, Gui-Xiang Int J Mol Sci Article 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. MDPI 2015-04-30 /pmc/articles/PMC4463623/ /pubmed/25941931 http://dx.doi.org/10.3390/ijms16059896 Text en © 2015 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Wang, Wan Yuan, Hong-Yan Liu, Guo-Mu Ni, Wei-Hua Wang, Fang Tai, Gui-Xiang Escherichia coli Maltose-Binding Protein Induces M1 Polarity of RAW264.7 Macrophage Cells via a TLR2- and TLR4-Dependent Manner |
title | Escherichia coli Maltose-Binding Protein Induces M1 Polarity of RAW264.7 Macrophage Cells via a TLR2- and TLR4-Dependent Manner |
title_full | Escherichia coli Maltose-Binding Protein Induces M1 Polarity of RAW264.7 Macrophage Cells via a TLR2- and TLR4-Dependent Manner |
title_fullStr | Escherichia coli Maltose-Binding Protein Induces M1 Polarity of RAW264.7 Macrophage Cells via a TLR2- and TLR4-Dependent Manner |
title_full_unstemmed | Escherichia coli Maltose-Binding Protein Induces M1 Polarity of RAW264.7 Macrophage Cells via a TLR2- and TLR4-Dependent Manner |
title_short | Escherichia coli Maltose-Binding Protein Induces M1 Polarity of RAW264.7 Macrophage Cells via a TLR2- and TLR4-Dependent Manner |
title_sort | escherichia coli maltose-binding protein induces m1 polarity of raw264.7 macrophage cells via a tlr2- and tlr4-dependent manner |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4463623/ https://www.ncbi.nlm.nih.gov/pubmed/25941931 http://dx.doi.org/10.3390/ijms16059896 |
work_keys_str_mv | AT wangwan escherichiacolimaltosebindingproteininducesm1polarityofraw2647macrophagecellsviaatlr2andtlr4dependentmanner AT yuanhongyan escherichiacolimaltosebindingproteininducesm1polarityofraw2647macrophagecellsviaatlr2andtlr4dependentmanner AT liuguomu escherichiacolimaltosebindingproteininducesm1polarityofraw2647macrophagecellsviaatlr2andtlr4dependentmanner AT niweihua escherichiacolimaltosebindingproteininducesm1polarityofraw2647macrophagecellsviaatlr2andtlr4dependentmanner AT wangfang escherichiacolimaltosebindingproteininducesm1polarityofraw2647macrophagecellsviaatlr2andtlr4dependentmanner AT taiguixiang escherichiacolimaltosebindingproteininducesm1polarityofraw2647macrophagecellsviaatlr2andtlr4dependentmanner |