Lactobacillus fermentum BCS87 expresses mucus- and mucin-binding proteins on the cell surface.
J Appl Microbiol
; 107(6): 1866-74, 2009 Dec 01.
Article
em En
| MEDLINE
| ID: mdl-19548890
ABSTRACT
AIMS:
To identify and characterize adhesion-associated proteins in the potential probiotic Lactobacillus fermentum BCS87. METHODS ANDRESULTS:
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.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Adesinas Bacterianas
/
Probióticos
/
Limosilactobacillus fermentum
Idioma:
En
Revista:
J Appl Microbiol
Assunto da revista:
MICROBIOLOGIA
Ano de publicação:
2009
Tipo de documento:
Article