IMR Press / FBL / Volume 16 / Issue 6 / DOI: 10.2741/3843

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
Identification of the Lactobacillus SLP domain that binds gastric mucin
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1 Department of Surgery, Shanghai Jiao Tong University Affiliated Sixth People's Hospital, Shanghai, 200233, China
2 Department of Surgery, Shanghai Tenth People’s Hospital, Shanghai, 200072, China
3 INCELL Corporation, San Antonio Texas, 78249, USA

Academic Editor: Jie Zou

Front. Biosci. (Landmark Ed) 2011, 16(6), 2128–2143;
Published: 1 June 2011
(This article belongs to the Special Issue Immunoregulation and inflammatory disease)

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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