Functional characterization of MIMP for its adhesion to the intestinal epithelium

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

doi:10.2741/3842

Functional characterization of MIMP for its adhesion to the intestinal epithelium

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

Research output: Contribution to journal › Article › peer-review

13 Scopus citations

Abstract

The micro integral membrane protein (MIMP), the domain within the integral membrane protein of Lactobacillus plantarum CGMCC 1258, has been shown to adhere to mucin and antagonize the adhesion of enteroinvasive E. coli and enteropathogenic E. coli. To further characterize the functions of MIMP, we investigated its effects on the intestinal permeability, expression of tight junction (TJ) proteins and TJ ultrastructure in vitro and in vivo. We also determined the interaction between MIMP and dendritic cells (DCs). We observed that MIMP reduced intestinal permeability and restored the expression and distribution of TJ proteins in both NCM460 cell monolayers and in IL-10 ^-/- mice. MIMP adhered to immature (i) DCs by binding to DC-SIGN, and induced DCs to produce anti-inflammatory cytokines and to mediate Th2 differentiation. Moreover, MIMP stimulated the expression of anti-inflammatory cytokines in colonic mucosa and attenuated colitis in IL-10^-/- mice. In conclusion, MIMP is the main functional component of L. plantarum that contributes to its protective effects, and thus may be a potential therapeutic agent for intestinal diseases.

Original language	English (US)
Pages (from-to)	2106-2127
Number of pages	22
Journal	Frontiers in Bioscience
Volume	16
Issue number	6
DOIs	https://doi.org/10.2741/3842
State	Published - Jun 1 2011
Externally published	Yes

Keywords

Dendritic cells
Domain
IL-10-/- mice
Lactobacillus plantarum
Micro integral membrane protein
NCM460
Surface layer protein
Tight junction

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology
General Immunology and Microbiology

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10.2741/3842

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title = "Functional characterization of MIMP for its adhesion to the intestinal epithelium",

abstract = "The micro integral membrane protein (MIMP), the domain within the integral membrane protein of Lactobacillus plantarum CGMCC 1258, has been shown to adhere to mucin and antagonize the adhesion of enteroinvasive E. coli and enteropathogenic E. coli. To further characterize the functions of MIMP, we investigated its effects on the intestinal permeability, expression of tight junction (TJ) proteins and TJ ultrastructure in vitro and in vivo. We also determined the interaction between MIMP and dendritic cells (DCs). We observed that MIMP reduced intestinal permeability and restored the expression and distribution of TJ proteins in both NCM460 cell monolayers and in IL-10 -/- mice. MIMP adhered to immature (i) DCs by binding to DC-SIGN, and induced DCs to produce anti-inflammatory cytokines and to mediate Th2 differentiation. Moreover, MIMP stimulated the expression of anti-inflammatory cytokines in colonic mucosa and attenuated colitis in IL-10-/- mice. In conclusion, MIMP is the main functional component of L. plantarum that contributes to its protective effects, and thus may be a potential therapeutic agent for intestinal diseases.",

keywords = "Dendritic cells, Domain, IL-10-/- mice, Lactobacillus plantarum, Micro integral membrane protein, NCM460, Surface layer protein, Tight junction",

author = "Zhihua Liu and Tongyi Shen and Hongqi Chen and Yukun Zhou and Peng Zhang and Yanlei Ma and Moyer, {Mary Pat} and Ming Zhang and Zhaoxin Chu and Huanlong Qin",

year = "2011",

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doi = "10.2741/3842",

language = "English (US)",

volume = "16",

pages = "2106--2127",

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T1 - Functional characterization of MIMP for its adhesion to the intestinal epithelium

AU - Liu, Zhihua

AU - Shen, Tongyi

AU - Chen, Hongqi

AU - Zhou, Yukun

AU - Zhang, Peng

AU - Ma, Yanlei

AU - Moyer, Mary Pat

AU - Zhang, Ming

AU - Chu, Zhaoxin

AU - Qin, Huanlong

PY - 2011/6/1

Y1 - 2011/6/1

N2 - The micro integral membrane protein (MIMP), the domain within the integral membrane protein of Lactobacillus plantarum CGMCC 1258, has been shown to adhere to mucin and antagonize the adhesion of enteroinvasive E. coli and enteropathogenic E. coli. To further characterize the functions of MIMP, we investigated its effects on the intestinal permeability, expression of tight junction (TJ) proteins and TJ ultrastructure in vitro and in vivo. We also determined the interaction between MIMP and dendritic cells (DCs). We observed that MIMP reduced intestinal permeability and restored the expression and distribution of TJ proteins in both NCM460 cell monolayers and in IL-10 -/- mice. MIMP adhered to immature (i) DCs by binding to DC-SIGN, and induced DCs to produce anti-inflammatory cytokines and to mediate Th2 differentiation. Moreover, MIMP stimulated the expression of anti-inflammatory cytokines in colonic mucosa and attenuated colitis in IL-10-/- mice. In conclusion, MIMP is the main functional component of L. plantarum that contributes to its protective effects, and thus may be a potential therapeutic agent for intestinal diseases.

AB - The micro integral membrane protein (MIMP), the domain within the integral membrane protein of Lactobacillus plantarum CGMCC 1258, has been shown to adhere to mucin and antagonize the adhesion of enteroinvasive E. coli and enteropathogenic E. coli. To further characterize the functions of MIMP, we investigated its effects on the intestinal permeability, expression of tight junction (TJ) proteins and TJ ultrastructure in vitro and in vivo. We also determined the interaction between MIMP and dendritic cells (DCs). We observed that MIMP reduced intestinal permeability and restored the expression and distribution of TJ proteins in both NCM460 cell monolayers and in IL-10 -/- mice. MIMP adhered to immature (i) DCs by binding to DC-SIGN, and induced DCs to produce anti-inflammatory cytokines and to mediate Th2 differentiation. Moreover, MIMP stimulated the expression of anti-inflammatory cytokines in colonic mucosa and attenuated colitis in IL-10-/- mice. In conclusion, MIMP is the main functional component of L. plantarum that contributes to its protective effects, and thus may be a potential therapeutic agent for intestinal diseases.

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KW - NCM460

KW - Surface layer protein

KW - Tight junction

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Functional characterization of MIMP for its adhesion to the intestinal epithelium

Abstract

Keywords

ASJC Scopus subject areas

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