Purification and characterization of a surface-binding protein from Lactobacillus fermentum RC-14 that inhibits adhesion of Enterococcus faecalis 1131
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 p...
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Veröffentlicht in: | FEMS microbiology letters 2000-09, Vol.190 (1), p.177-180 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 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. |
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ISSN: | 0378-1097 1574-6968 |
DOI: | 10.1016/S0378-1097(00)00331-1 |