Open AccessPurification and characterization of a surface‐binding protein from Lactobacillus fermentum RC‐14 that inhibits adhesion of Enterococcus faecalis 1131
Author(s) -
Heinemann Christine,
Hylckama Vlieg Johan E.T.,
Janssen Dick B.,
Busscher Henk J.,
Mei Henny C.,
Reid Gregor
Publication year - 2000
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2000.tb09282.x
Subject(s) - lactobacillus fermentum , enterococcus faecalis , adhesion , microbiology and biotechnology , chemistry , enterococcus , streptococcaceae , lactobacillus , bacteria , biochemistry , biology , lactobacillus plantarum , lactic acid , escherichia coli , organic chemistry , antibiotics , genetics , gene , fermentation
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.