Purification and characterization of a surface-binding protein from Lactobacillus fermentum RC-14 that inhibits adhesion of Enterococcus faecalis 1131
Purification and characterization of a surface-binding protein from Lactobacillus fermentum RC-14 that inhibits adhesion of Enterococcus faecalis 1131
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DOI：
10.1111/j.1574-6968.2000.tb09282.x
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发表时间：
2000-09-01
影响因子：
2.1
通讯作者：
Reid, G
中科院分区：
文献类型：
--
作者：
Heinemann, C;Vlieg, JETV;Reid, G
乳酸杆菌在维持泌尿生殖道植物群的健康方面具有重要作用。一种菌株，发酵乳杆菌RC-14。释放出抑制尿路致病菌粘附的表面活性成分。使用测定粘附抑制的定量方法，纯化了对粪肠球菌1131具有高抗粘附特性的蛋白质。该29-kDa蛋白的N-末端序列与来自罗伊氏乳杆菌NCIB 11951的胶原结合蛋白的N-末端序列相同，并且与来自L.发酵菌BR 11。结果表明，这种抗粘附细胞表面蛋白的乳酸杆菌可以保护对尿路病原体通过防止其粘附。(C)2000年由Elsevier Science B. V.代表欧洲微生物学会联合会出版。
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.