Functional Analysis of an S-Layer-Associated Fibronectin-Binding Protein in Lactobacillus acidophilus NCFM

• Jeffrey P. Hymes ^[1] ; Brant R. Johnson ^[2] ; Rodolphe Barrangou ^[2] ; Todd R. Klaenhammer ^[2]
  1. [1] North Carolina State University

     North Carolina State University

     Township of Raleigh, Estados Unidos

     
  2. [2] aDepartment of Food, Bioprocessing, and Nutrition Sciences, North Carolina State University, Raleigh, North Carolina, USA; bGraduate Program in Microbiology, College of Agriculture and Life Sciences, North Carolina State University, Raleigh, North Carolina, USA
• Localización: Applied and Environmental Microbiology, ISSN 0099-2240, Vol. 82, Nº 9, 2016, págs. 2676-2685
• Idioma: inglés
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• Resumen

  • Bacterial surface layers (S-layers) are crystalline arrays of self-assembling proteinaceous subunits called S-layer proteins (Slps) that comprise the outermost layer of the cell envelope. Many additional proteins that are associated with or embedded within the S-layer have been identified in Lactobacillus acidophilus NCFM, an S-layer-forming bacterium that is widely used in fermented dairy products and probiotic supplements. One putative S-layer-associated protein (SLAP), LBA0191, was predicted to mediate adhesion to fibronectin based on the in silico detection of a fibronectin-binding domain. Fibronectin is a major component of the extracellular matrix (ECM) of intestinal epithelial cells. Adhesion to intestinal epithelial cells is considered an important trait for probiotic microorganisms during transit and potential association with the intestinal mucosa. To investigate the functional role of LBA0191 (designated FbpB) in L. acidophilus NCFM, an fbpB-deficient strain was constructed. The L. acidophilus mutant with a deletion of fbpB lost the ability to adhere to mucin and fibronectin in vitro. Homologues of fbpB were identified in five additional putative S-layer-forming species, but no homologues were detected in species outside the L. acidophilus homology group.