Purification and characterization of a surface-binding protein from Lactobacillus fermentum RC-14 that inhibits adhesion of Enterococcus faecalis 1131.
- 2000-09
- FEMS Microbiology Letters 190(1)
- C. Heinemann
- J. V. H. Vlieg
- D. Janssen
- H. Busscher
- H. C. Mei
- G. Reid
- G. Reid
- PubMed: 10981710
- DOI: 10.1111/J.1574-6968.2000.TB09282.X
Abstract
Lactobacilli have been shown to be important in the maintenance of the healthy urogenital flora. One strain, Lactobacillus fermentum RC-14, releases surface-active components which can inhibit adhesion of uropathogenic bacteria. Using a quantitative method for determining inhibition of adhesion, a protein with high anti-adhesive properties against Enterococcus faecalis 1131 was purified. The N-terminal sequence of the 29-kDa protein was identical to that of a collagen-binding protein from Lactobacillus reuteri NCIB 11951, and exhibited close homology with a basic surface protein from L. fermentum BR11. The results suggest that this anti-adhesive cell surface protein of Lactobacillus could protect against uropathogens by preventing their adhesion. the Federation of European Microbiological Societies.
Research Insights
Supplement | Health Outcome | Effect Type | Effect Size |
---|---|---|---|
Lactobacillus reuteri RC-14 | Reduced Uropathogenic Bacterial Adhesion | Beneficial | Moderate |