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
Hauptverfasser: Heinemann, Christine, van Hylckama Vlieg, Johan E.T., Janssen, Dick B., Busscher, Henk J., van der Mei, Henny C., Reid, Gregor
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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.
ISSN:0378-1097
1574-6968
DOI:10.1016/S0378-1097(00)00331-1