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  • Title: Collagen (Cn-I) binding by gut lactobacilli.
    Author: Styriak I, Demecková V, Nemcová R.
    Journal: Berl Munch Tierarztl Wochenschr; 1999 Aug; 112(8):301-4. PubMed ID: 10486988.
    Abstract:
    Four gut Lactobacillus strains displaying the features which make them particularly promising for the preparation of probiotic products were investigated together with 5 fresh isolates and one collection strain of Lactobacillus plantarum for their ability to bind type I collagen (Cn-I). Immobilised Cn-I in microtitre plates was bound only by 3 strains of gut lactobacilli from piglets and the collection strain Lactobacillus plantarum LHI 10 from Prague in range of A570nm readings 0.114-0.221. Six strains (isolates from turkeys and a calf) did not bind Cn-I (A570nm < 0.1) in this assay. An influence of cultivation medium on Cn-I binding was significant (P < 0.001) in all four adherent strains. Significantly higher (P < 0.001) binding of Cn-I was observed for Lactobacillus casei L 81 and Lactobacillus plantarum LHI 10 grown on solid medium (MRS agar) than for MRS broth-grown cells, however, Lactobacillus plantarum L 5 and Lactobacillus fermentum L 435 expressed significantly (P < 0.001) higher Cn-I binding during cultivation in MRS broth. The specificity of the binding was confirmed because the Cn-I binding by lactobacilli after their preincubation with this protein was completely abolished. Three selected inhibitors (fucoidan, heparan sulphate and hyaluronic acid) significantly (P < 0.001) reduced Cn-I binding by the Lactobacillus plantarum L 5 strain. Following up on some earlier strain characteristics, these results suggest that the selected piglets lactobacilli are also able to bind Cn-I and therefore should antagonize collagen niche colonization by various enteropathogens when used for probiotic purposes.
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