OBJECTIVE: To clarify the adhesion mechanism of Lactobacillus acidophilus to Peyer's patches. METHODS: Adhesion of L. acidophilus FN001 to mice Peyer's patches was studied in vitro using a fluorescent quantization method. The nature of adhesion mediator was studied by the differing effects of physical, chemical, and enzymatic pre-treatments of the bacteria and the inhibitory effects of sugars on the adhesion. The presence of lectin-like proteins on the cell surface was determined by hemagglutination assay. The effect of L. acidophilus FN001 on the inhibition of adhesion of pathogens to Peyer's patches was also studied. RESULTS: The adhesion of L. acidophilus FN001 was strongly inhibited in the presence of D-mannose and methyl-α-D-mannoside. Pretreatment of L. acidophilus FN001 with pepsin and trypsin decreased the adhesive capacity indicating that some cell surface proteins might be involved in the adhesion. L. acidophilus FN001 showed agglutinating activity toward the rabbit red cells in a mannose specific manner, which was decreased after protease pretreatment, suggesting possible occurrence of mannose specific lectin(s) on the L. acidophilus FN001 surface. In adhesion inhibition assay, L. acidophilus NF001, when applied to Peyer's patches first or at the same time with pathogen, significantly inhibited adhesion of Escherichia coli ATCC25922 to Peyer's patches. CONCLUSION: L. acidophilus FN001 contains some mannose-specific protein(s) on its surface that mediates its adhesion to the Peyer's patches. FN001 inhibits the adhesion of E. coli, which also contains mannose specific lectin. Crown
OBJECTIVE: To clarify the adhesion mechanism of Lactobacillus acidophilus to Peyer's patches. METHODS: Adhesion of L. acidophilus FN001 to mice Peyer's patches was studied in vitro using a fluorescent quantization method. The nature of adhesion mediator was studied by the differing effects of physical, chemical, and enzymatic pre-treatments of the bacteria and the inhibitory effects of sugars on the adhesion. The presence of lectin-like proteins on the cell surface was determined by hemagglutination assay. The effect of L. acidophilus FN001 on the inhibition of adhesion of pathogens to Peyer's patches was also studied. RESULTS: The adhesion of L. acidophilus FN001 was strongly inhibited in the presence of D-mannose and methyl-α-D-mannoside. Pretreatment of L. acidophilus FN001 with pepsin and trypsin decreased the adhesive capacity indicating that some cell surface proteins might be involved in the adhesion. L. acidophilus FN001 showed agglutinating activity toward the rabbit red cells in a mannose specific manner, which was decreased after protease pretreatment, suggesting possible occurrence of mannose specific lectin(s) on the L. acidophilus FN001 surface. In adhesion inhibition assay, L. acidophilus NF001, when applied to Peyer's patches first or at the same time with pathogen, significantly inhibited adhesion of Escherichia coli ATCC25922 to Peyer's patches. CONCLUSION:L. acidophilus FN001 contains some mannose-specific protein(s) on its surface that mediates its adhesion to the Peyer's patches. FN001 inhibits the adhesion of E. coli, which also contains mannose specific lectin. Crown
Authors: Pieter Van den Abbeele; Stefan Roos; Venessa Eeckhaut; Donald A MacKenzie; Melanie Derde; Willy Verstraete; Massimo Marzorati; Sam Possemiers; Barbara Vanhoecke; Filip Van Immerseel; Tom Van de Wiele Journal: Microb Biotechnol Date: 2011-10-12 Impact factor: 5.813