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

Authors

  • M.E. Macías-Rodríguez,

    1.  Laboratorio de Patogénesis Microbiana. Centro de Investigaciones Biológicas del Noroeste, La Paz, Baja California Sur, México
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  • M. Zagorec,

    1.  Unité Flore Lactique et Environnement Carné (UR309). Institut National de la Recherche Agronomique, Domaine de Vilvert, Jouy-en-Josas, France
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  • F. Ascencio,

    1.  Laboratorio de Patogénesis Microbiana. Centro de Investigaciones Biológicas del Noroeste, La Paz, Baja California Sur, México
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  • R. Vázquez-Juárez,

    1.  Laboratorio de Patogénesis Microbiana. Centro de Investigaciones Biológicas del Noroeste, La Paz, Baja California Sur, México
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  • M. Rojas

    1.  Laboratorio de Ciencia y Tecnología de Alimentos. Área Interdisciplinaria de Ciencias Agropecuarias. Universidad Autónoma de Baja California Sur. Km 5.5, La Paz, Baja California Sur, México
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Maurilia Rojas, Laboratorio de Ciencia y Tecnología de Alimentos, Área Interdisciplinaria de Ciencias Agropecuarias, Universidad Autónoma de Baja California Sur. Km 5.5, Carretera al Sur, 23080 La Paz, Baja California Sur, México. E-mail: mrojas@uabcs.mx

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.

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