Purification and characterization of a surface-binding protein from Lactobacillus fermentum RC-14 that inhibits adhesion of Enterococcus faecalis 1131

被引:123
作者
Heinemann, C
Vlieg, JETV
Janssen, DB
Busscher, HJ
van der Mei, HC
Reid, G [1 ]
机构
[1] Univ Western Ontario, Dept Microbiol & Immunol, Hlth Sci Ctr, London, ON N6A 5C1, Canada
[2] Univ Groningen, Dept Biochem, NL-9747 AG Groningen, Netherlands
[3] Univ Groningen, Dept Biomed Engn, NL-9712 KZ Groningen, Netherlands
[4] Lawson Res Inst, London, ON N6A 4V2, Canada
关键词
Lactobacillus; Enterococcus; bacterial adhesion; collagen;
D O I
10.1111/j.1574-6968.2000.tb09282.x
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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. (C) 2000 Published by Elsevier Science B.V. on behalf of the Federation of European Microbiological Societies.
引用
收藏
页码:177 / 180
页数:4
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