Identification of DC-SIGN as the receptor during the interaction of Lactobacillus plantarum CGMCC 1258 and dendritic cells

Liu, Zhihua; Ma, Yanlei; Shen, Tongyi; Chen, Hongqi; Zhou, Yukun; Zhang, Peng; Zhang, Ming; Chu, Zhaoxin; Qin, Huanlong

doi:10.1007/s11274-010-0495-3

Cited by 13 publications

(13 citation statements)

References 45 publications

(51 reference statements)

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“…Our previous studies have shown that Lactobacillus Plantarum (LP) functions as a probiotic by enhancing the intestinal epithelial barrier [6-8]. We also observed that LP interacts with dendritic cells and regulates several inflammatory cytokines [9]. Clinically, we confirmed that perioperative probiotic treatment can reduce the rate of postoperative septicaemia and is associated with reduced serum concentrations of the intestinal permeability regulator zonulin in colorectal cancer patients undergoing colectomy [10].…”

Section: Introductionsupporting

confidence: 68%

Micro Integral Membrane Protein (MIMP), a Newly Discovered Anti-Inflammatory Protein of Lactobacillus Plantarum, Enhances the Gut Barrier and Modulates Microbiota and Inflammatory Cytokines

Yin¹,

Yan

Weng³

et al. 2018

Cell Physiol Biochem

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Background/Aims: Recent studies have demonstrated that the manipulation of the gut microbiome represents a promising treatment for inflammatory bowel disease (IBD). We previously identified micro integral membrane protein (MIMP) as the smallest domain of surface layer protein from Lactobacillus Plantarum. However, the therapeutic relevance of MIMP in IBD remains unknown. Methods: We initially employed a dextran sodium sulphate (DSS)-induced colitis model and evaluated the effect of MIMP on the inflammation response, intestinal barrier and gut microbiota using histological examination, Fluorescein isothiocyanate-Dextran detection and pyrosequencing analysis respectively. We then established peripheral blood mononuclear cells (PBMCs) and an epithelial CaCO-2 co-culture model to investigate the regulatory role of MIMP in inflammatory cytokines. The level changes of inflammatory cytokines were detected using Enzyme-linked immunosorbent and real-time polymerase chain reaction assay. The involved regulatory mechanisms were investigated mainly using dual luciferase reporter and chromatin immunoprecipitation assay. Results: In the DSS-induced colitis model, we observed that MIMP intervention effectively improved the body weight loss, increased the colon length and decreased disease activity index. Consistently, the inflammation scores in the MIMP treatment group were significantly lower than those in the DSS treatment group. Furthermore, MIMP intervention was found to successfully neutralize DSS treatment by decreasing the expression of pro-inflammatory cytokines (IFN-γ, IL-17 and IL-23) and increasing the expression of anti-inflammatory cytokines (IL-4 and IL-10). Notably, the permeability assay demonstrated that the MIMP treatment group was remarkably lower than that in the DSS treatment group. We also showed that MIMP improved gut microbiota dysbiosis caused by DSS-induced inflammation. Additionally, in PBMCs and the CaCO-2 co-culture model, MIMP showed an obvious suppressive effect on lipopolysaccharide-induced inflammation in a time- and dose-dependent manner. Furthermore, we revealed that MIMP could modulate inflammatory cytokine expression through the toll-like receptor 4 pathway and histone acetylation. Conclusions: Our results suggested that MIMP showed a significant anti-inflammatory effect through regulating the gut barrier, microbiota and inflammatory cytokines. MIMP may have translational relevance as clinically relevant therapy for IBD patients.

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Section: Introductionsupporting

confidence: 68%

Micro Integral Membrane Protein (MIMP), a Newly Discovered Anti-Inflammatory Protein of Lactobacillus Plantarum, Enhances the Gut Barrier and Modulates Microbiota and Inflammatory Cytokines

Yin¹,

Yan

Weng³

et al. 2018

Cell Physiol Biochem

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“…There is growing evidence that those bacterial species closely related and adherent to the mucosa are more relevant to human health than those evacuated in the feces (2)(3). In healthy individuals, there is a homeostasis between commensal microbiota and pathogenic bacteria in the intestines (4)(5). Alterations in this homeostatic mechanism will result in an imbalanced ecological microenvironment and subsequent gut-barrier dysfunction (6)(7).…”

Section: Introductionmentioning

confidence: 99%

Identification of the Lactobacillus SLP domain that binds gastric mucin

Liu

Shen²,

Moyer³

et al. 2011

Front Biosci

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Surface layer proteins (SLPs) of lactobacillus bacteria have some structural regions responsible for adhesion to the intestinal epithelium. To identify the SLP and the smallest domain within the protein that is responsible for the adhesion of the bacterium to the intestinal epithelium, L. plantarum strain CGMCC1258 was investigated in this study. Using bioinformatics and molecular techniques, we first identified and purified a novel protein, integral membrane protein-2 (IMP-2, 33-45 kDa) responsible for adhesion to gastric mucin. Truncated forms of IMP-2 were then constructed and expressed, and the amino acids from 515 to 575 (designated micro IMP, MIMP) was identified as the smallest domain responsible for adhesion to gastric mucin. Competing assay was performed, which further confirmed the ability of MIMP to compete with enteroinvasive E. coli and enteropathogenic E. coli to adhere to cells of a normal colon cell line, NCM460. Furthermore, MIMP could maturate dendritic cells. These findings set a foundation for further investigation on the role of MIMP in the treatment and prevention of inflammation-related diseases of the intestine.

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“…Our previous studies indicated that L. plantarum (LP) conferred therapeutic effects by adhering to epithelial cells, restoring tight junction (TJ) structure and function and improving paracellular permeability both in vivo and in vitro [18][19][20][21][22][23]. Furthermore, our recent study (manuscript in press) describing SLP functional domains indicated that the LP strain CGMCC 1258 integrated membrane protein (IMP) mediated adherance to intestinal epithelial cells (IECs).…”

Section: Introductionmentioning

confidence: 99%

Expression of the <i>Lactobacillus Plantarum</i> Surface Layer MIMP Protein Protected NCM460 Epithelial Cells from Enteroinvasive <i>Escherichia Coli</i> Infection

Liu

Yang

et al. 2011

Cell Physiol Biochem

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Our previous studies demonstrated that the micro integral membrane protein (MIMP) located within the integral membrane protein of Lactobacillus plantarum CGMCC 1258 protected the intestinal barrier from injury. To further analyze the protective effects conferred to intestinal epithelial cells by MIMP, we established transient MIMP-expressing NCM460 cells (NCM460/MIMP) as a means of assessing their susceptibility to infection. We constructed a recombinant eukaryotic expression vector using pcDNA3.1(-) and the MIMP gene. The recombinant vector was then transduced into NCM460 cells and the anti-infective properties of the transient MIMP-expressing NCM460/MIMP cells assessed. Flow cytometric analysis revealed that 82.16% ±12.22% of NCM460/MIMP cells expressed MIMP and Western blot analysis confirmed high levels of MIMP expression. Attachment assays showed that the ability of enteropathogenic Escherichia coli (EPEC) to attach to NCM460/MIMP cells decreased significantly compared to adhesion observed to NCM460 cells. Western blot and quantitative RT-PCR showed that the expression levels of tight junction (TJ) proteins, including claudin-1, occludin, JAM-1 and ZO-1 in NCM460/MIMP cells infected with EPEC were similar to levels observed in uninfected NCM460 cells. Fluorescence further showed that NCM460/MIMP cells had significantly higher TJ protein staining intensity ocompared to NCM460 cells and transmission electron microscopy indicated that TJ structure was unchanged in NCM460/MIMP cells infected with EPEC compared to NCM460 cells after EPEC infection. Expression levels of PKC-η and phosphorylated occludin were also higher after EPEC infection in NCM460/MIMP cells compared to expression levels in EPEC-infected NCM460 cells. These data demonstrated that NCM460/MIMP cells possessed EPEC anti-infective properties related to the activation of protein kinase C-η and occludin phosphorylation.

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Identification of DC-SIGN as the receptor during the interaction of Lactobacillus plantarum CGMCC 1258 and dendritic cells

Cited by 13 publications

References 45 publications

Micro Integral Membrane Protein (MIMP), a Newly Discovered Anti-Inflammatory Protein of Lactobacillus Plantarum, Enhances the Gut Barrier and Modulates Microbiota and Inflammatory Cytokines

Micro Integral Membrane Protein (MIMP), a Newly Discovered Anti-Inflammatory Protein of Lactobacillus Plantarum, Enhances the Gut Barrier and Modulates Microbiota and Inflammatory Cytokines

Identification of the Lactobacillus SLP domain that binds gastric mucin

Expression of the <i>Lactobacillus Plantarum</i> Surface Layer MIMP Protein Protected NCM460 Epithelial Cells from Enteroinvasive <i>Escherichia Coli</i> Infection

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