A preliminary analysis of Bifidobacterium longum exported proteins by two-dimensional electrophoresis |
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Authors: | Sánchez Borja Champomier-Vergès Marie-Christine Anglade Patricia Baraige Fabienne de Los Reyes-Gavilán Clara G Margolles Abelardo Zagorec Monique |
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Institution: | Unité Flore Lactique et Environnement Carné, UR309, INRA, Jouy-en-Josas, France. |
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Abstract: | 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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