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Article Dans Une Revue Journal of Molecular Microbiology and Biotechnology Année : 2008

A preliminary analysis of Bifidobacterium longum exported proteins by two-dimensional electrophoresis

Résumé

Extracellular proteins of Bifidobacterium longum may mediate important interactions with the host. Here, we report on a comprehensive analysis of such proteins by using protein-free culture conditions and two-dimensional gel electrophoresis followed by mass spectrometry for protein identification. Seventeen proteins were detected in the culture supernatant, and 14 of them could be identified. Among these were 3 hypothetical solute-binding proteins of ABC transporters, an invasion-associated protein homolog, putative enzymes catalyzing cell wall turnover, several polypeptides with similarity to bacterial conjugation proteins, and 3 proteins of unknown function. Surprisingly, aldolase, usually considered as a cytoplasmic protein, was found in the culture supernatant. All proteins, excluding aldolase, were predicted to contain a signal peptide and a signal peptide cleavage site in their immature form. Some of the excreted proteins are interesting targets for further genetic and physiological studies.
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Dates et versions

hal-02660202 , version 1 (30-05-2020)

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Borja Sánchez, Marie-Christine Champomier Verges, Patricia P. Anglade, Fabienne Baraige, Clara de Los Reyes-Gavilán, et al.. A preliminary analysis of Bifidobacterium longum exported proteins by two-dimensional electrophoresis. Journal of Molecular Microbiology and Biotechnology, 2008, 14 (1-3), pp.74-75. ⟨10.1159/000106085⟩. ⟨hal-02660202⟩

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