4.6 Review

Dietary Nutrients, Proteomes, and Adhesion of Probiotic Lactobacilli to Mucin and Host Epithelial Cells

Journal

MICROORGANISMS
Volume 6, Issue 3, Pages -

Publisher

MDPI
DOI: 10.3390/microorganisms6030090

Keywords

lactobacilli; probiotics; adhesion; mucin; intestinal cells; carbon sources; polyphenols; surface proteomes; protein identification; moonlighting proteins

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Funding

  1. Republic of Turkey, Ministry of National Education
  2. Danish Council for Strategic Research
  3. Danish Council for Independent Research \ Natural Sciences
  4. Center for Advanced Food Studies
  5. committee for Health, Food and Welfare

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The key role of diet and environment in human health receives increasing attention. Thus functional foods, probiotics, prebiotics, and synbiotics with beneficial effects on health and ability to prevent diseases are in focus. The efficacy of probiotic bacteria has been connected with their adherence to the host epithelium and residence in the gut. Several in vitro techniques are available for analyzing bacterial interactions with mucin and intestinal cells, simulating adhesion to the host in vivo. Proteomics has monitored and identified proteins of probiotic bacteria showing differential abundance elicited in vitro by exposure to food components, including potential prebiotics (e.g., certain carbohydrates, and plant polyphenols). While adhesion of probiotic bacteria influenced by various environmental factors relevant to the gastrointestinal tract has been measured previously, this was rarely correlated with changes in the bacterial proteome induced by dietary nutrients. The present mini-review deals with effects of selected emerging prebiotics, food components and ingredients on the adhesion of probiotic lactobacilli to mucin and gut epithelial cells and concomitant abundancy changes of specific bacterial proteins. Applying this in vitro synbiotics-like approach enabled identification of moonlighting and other surface-located proteins of Lactobacillus acidophilus NCFM that are possibly associated with the adhesive mechanism.

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