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鉴定与胃粘液结合的乳杆菌 SLP 结构域。

Identification of the Lactobacillus SLP domain that binds gastric mucin.

机构信息

Department of Surgery, Shanghai Jiao Tong University Affiliated Sixth People's Hospital, Shanghai, 200233, China.

出版信息

Front Biosci (Landmark Ed). 2011 Jun 1;16(6):2128-43. doi: 10.2741/3843.

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.

摘要

乳酸菌表面层蛋白 (SLP) 具有一些结构区域,负责与肠道上皮细胞黏附。为了鉴定 SLP 和负责细菌与肠道上皮细胞黏附的蛋白质内最小结构域,本研究对植物乳杆菌 CGMCC1258 进行了研究。利用生物信息学和分子技术,我们首先鉴定并纯化了一种新型蛋白,即负责黏附胃粘蛋白的完整膜蛋白-2(IMP-2,33-45 kDa)。然后构建并表达了 IMP-2 的截断形式,并鉴定出 515 到 575 个氨基酸(命名为微 IMP,MIMP)是负责黏附胃粘蛋白的最小结构域。竞争测定进一步证实了 MIMP 与侵袭性大肠埃希菌和肠致病性大肠埃希菌竞争黏附正常结肠细胞系 NCM460 细胞的能力。此外,MIMP 可以成熟树突状细胞。这些发现为进一步研究 MIMP 在治疗和预防肠道炎症相关疾病中的作用奠定了基础。

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