Lactobacillus fermentum BCS87 expresses mucus- and mucin-binding proteins on the cell surface
Article first published online: 5 MAY 2009
© 2009 The Authors. Journal compilation © 2009 The Society for Applied Microbiology
Journal of Applied Microbiology
Volume 107, Issue 6, pages 1866–1874, December 2009
How to Cite
Macías-Rodríguez, M.E., Zagorec, M., Ascencio, F., Vázquez-Juárez, R. and Rojas, M. (2009), Lactobacillus fermentum BCS87 expresses mucus- and mucin-binding proteins on the cell surface. Journal of Applied Microbiology, 107: 1866–1874. doi: 10.1111/j.1365-2672.2009.04368.x
- Issue published online: 12 NOV 2009
- Article first published online: 5 MAY 2009
- 2008/1410: received 16 August 2008, revised 31 March 2009 and accepted 15 April 2009
- adhesion-associated proteins;
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.