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A preliminary analysis of bifidobacterium longum exported proteins by two-Ddmensional electrophoresis

AutorSánchez García, Borja ; Champomier-Vergès, Marie-Christine; Anglade, Patricia; Baraige, Fabienne; González de los Reyes-Gavilán, Clara ; Margolles Barros, Abelardo ; Zagorec, Monique
Palabras claveBifidobacterium longum
Péptido señal
Fecha de publicación2008
EditorS. Karger AG
CitaciónJournal of Molecular Microbiology and Biotechnology 14(1-3): 74-79 (2008)
ResumenExtracellular 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
URIhttp://hdl.handle.net/10261/7119
DOI10.1159/000106085
ISSN1464-1801
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