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.
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.
Authors: Ingemar von Ossowski; Justus Reunanen; Reetta Satokari; Satu Vesterlund; Matti Kankainen; Heikki Huhtinen; Soile Tynkkynen; Seppo Salminen; Willem M de Vos; Airi Palva Journal: Appl Environ Microbiol Date: 2010-01-29 Impact factor: 4.792
Authors: Ingemar von Ossowski; Reetta Satokari; Justus Reunanen; Sarah Lebeer; Sigrid C J De Keersmaecker; Jos Vanderleyden; Willem M de Vos; Airi Palva Journal: Appl Environ Microbiol Date: 2011-05-20 Impact factor: 4.792
Authors: Jovanka Lukić; Ivana Strahinić; Branko Jovčić; Brankica Filipić; Ljubiša Topisirović; Milan Kojić; Jelena Begović Journal: Appl Environ Microbiol Date: 2012-09-07 Impact factor: 4.792
Authors: Ranjita Sengupta; Eric Altermann; Rachel C Anderson; Warren C McNabb; Paul J Moughan; Nicole C Roy Journal: Mediators Inflamm Date: 2013-03-13 Impact factor: 4.711