In vivo expression of the 25-kDa laminin-binding protein of Helicobacter pylori |
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Authors: | Moran Anthony P Broaders Samantha A Rapa Anna Oderda Giuseppina |
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Institution: | Laboratory of Molecular Biochemistry, Department of Microbiology, National University of Ireland, Galway, University Road, Galway, Ireland. anthony.moran@nuigalway.ie |
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Abstract: | The gastroduodenal pathogen Helicobacter pylori has been shown to inhibit the interaction between the extracellular matrix protein laminin and its receptor on gastric epithelial cells, potentially contributing to a loss of mucosal integrity. As a 25-kDa outer membrane protein of H. pylori in association with the bacterial lipopolysaccharides (LPS) mediates attachment to laminin, the aim of this study was to determine whether the 25-kDa protein is produced by H. pylori in infected hosts. We examined the immune response to the 25-kDa laminin binding protein in 12 paediatric patients; samples from a H. pylori-negative healthy adult were used as controls. In immunoblotting, antibodies to a 25-kDa protein were found in the serum and saliva of H. pylori-positive individuals only, and using the positive sera and saliva, laminin binding to the 25-kDa protein was inhibited. Thus, the 25-kDa laminin-binding protein is produced by H. pylori in infected hosts. |
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Keywords: | Helicobacter pylori Laminin Outer membrane protein Adhesin Immune response |
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