Identification by flagellum display of an epithelial cell- and fibronectin-binding function in the SlpA surface protein of Lactobacillus brevis.

@article{Hynnen2002IdentificationBF,
  title={Identification by flagellum display of an epithelial cell- and fibronectin-binding function in the SlpA surface protein of Lactobacillus brevis.},
  author={U. Hyn{\"o}nen and B. Westerlund-Wikstr{\"o}m and A. Palva and Timo K. Korhonen},
  journal={Journal of bacteriology},
  year={2002},
  volume={184 12},
  pages={
          3360-7
        }
}
Depletion of the SlpA protein from the bacterial surface greatly reduced the adhesion of Lactobacillus brevis ATCC 8287 to the human intestinal cell lines Caco-2 and Intestine 407, the endothelial cell line EA-hy926, and the urinary bladder cell line T24, as well as immobilized fibronectin. For functional analysis of the SlpA surface protein, different regions of the slpA gene were expressed as internal in-frame fusions in the variable region of the fliC(H7) gene of Escherichia coli. The… Expand
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