Lactobacillus fermentum BCS87 expresses mucus- and mucin-binding proteins on the cell surface.

Abstract

AIMS To identify and characterize adhesion-associated proteins in the potential probiotic Lactobacillus fermentum BCS87. METHODS AND RESULTS Protein suspensions obtained from the treatment of Lact. fermentum BCS87 with 1 mol 1(-1) LiCl were analysed by Western blotting using HRP-labelled porcine mucus and mucin. Two adhesion-associated proteins with relative molecular weight of 29 and 32 kDa were identified. The N-terminal and internal peptides of the 32 kDa protein (32-Mmubp) were sequenced, and the corresponding gene (32-mmub) was found by inverse polymerase chain reaction. The complete nucleotide sequence of 32-mmub revealed an open reading frame of 903 bp encoding a primary protein of 300 amino acids and a mature protein of 272 residues. A basic local alignment search showed 47-99% identity to solute-binding components of ATP binding cassette transporter proteins in Lactobacillus, Streptococcus and Clostridium. An OpuAC-conserved domain was identified and phylogenetic relationship analysis confirmed that 32-Mmubp belongs to the OpuAC family. CONCLUSIONS Adhesion of Lact. fermentum BCS87 appeared to be mediated by two surface-associated proteins. 32-Mmubp is a component of ABC transporter system that also functions as an adhesin. SIGNIFICANCE AND IMPACT OF THE STUDY Characterization of 32-Mmubp and 32-mmub will contribute to understanding the host-bacteria interactions of Lact. fermentum with the intestinal tract of pigs.

DOI: 10.1111/j.1365-2672.2009.04368.x
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@article{MacasRodrguez2009LactobacillusFB, title={Lactobacillus fermentum BCS87 expresses mucus- and mucin-binding proteins on the cell surface.}, author={Mar{\'i}a Esther Mac{\'i}as-Rodr{\'i}guez and Monique Zagorec and Felipe Ascencio and Roberto Carlos V{\'a}zquez-Ju{\'a}rez and Marta L. Rojas}, journal={Journal of applied microbiology}, year={2009}, volume={107 6}, pages={1866-74} }