Saccharomyces boulardii produces in rat small intestine a novel protein phosphatase that inhibits Escherichia coli endotoxin by dephosphorylation

被引:89
作者
Buts, JP
Dekeyser, N
Stilmant, C
Delem, E
Smets, F
Sokal, E
机构
[1] Catholic Univ Louvain, Clin St Luc, B-1200 Brussels, Belgium
[2] Catholic Univ Louvain, Fac Med, Lab Pediat Gastroenterol & Nutr, B-1200 Brussels, Belgium
[3] Catholic Univ Louvain, Fac Med, Lab Pediat Hepatol, B-1200 Brussels, Belgium
关键词
D O I
10.1203/01.pdr.0000220322.31940.29
中图分类号
R72 [儿科学];
学科分类号
100202 ;
摘要
Using a polyclonal antibody raised against a highly conserved sequence of 38 amino acids containing the activation site (VTDSAAGAT) common to mammalian and yeast alkaline phosphatases (AP), we identified in decapsidated Saccharomyces boutordii a protein phosphatase detected by autoradiography as a single signal (63 kD). Using an affinity chromatography column, the protein phosphatase could be concentrated 39.1-fold and presented as a doublet of two subunits. Compared with rat and bovine purified intestinal AP, the enzyme front S. boulardii had a greater ability to dephosphorylate the lipopolysaccharide (LPS) of Escherichia coli 055B5. When tested in vivo, intraperitoneal injection of intact LPS to rats produced, after 9 h, 100 ng/mL of circulating tumor necrosis factor-a with inflammatory lesions and apoptotic bodies in the liver and the heart, whereas rats injected with partially dephosphorylated LPS produced only 40 ng/mL tumor necrosis factor-a without organic lesions. In conclusion, S. boulardii is able to inhibit toxicity of E. coli surface endotoxins by the release of a protein phosphatase exhibiting a great capacity of dephosphorylation.
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页码:24 / 29
页数:6
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