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.

journal_name

J Appl Microbiol

authors

Macías-Rodríguez ME,Zagorec M,Ascencio F,Vázquez-Juárez R,Rojas M

doi

10.1111/j.1365-2672.2009.04368.x

subject

Has Abstract

pub_date

2009-12-01 00:00:00

pages

1866-74

issue

6

eissn

1364-5072

issn

1365-2672

pii

JAM4368

journal_volume

107

pub_type

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