Open Access
Article
Identification of the Lactobacillus SLP domain that binds gastric mucin
Zhihua Liu1,Tongyi Shen1,Mary Pat Moyer1,Huanlong Qin1
1
Department of Surgery, Shanghai Jiao Tong University Affiliated Sixth People's Hospital, Shanghai, 200233, China
DOI: 10.2741/3843 Volume 16 Issue 6, pp.2128-2143
Published: 01 June 2011
(This article belongs to the Special Issue Immunoregulation and inflammatory disease)
Abstract

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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Zhihua Liu, Tongyi Shen, Mary Pat Moyer, Huanlong Qin. Identification of the Lactobacillus SLP domain that binds gastric mucin. Frontiers in Bioscience-Landmark. 2011. 16(6); 2128-2143.