Detection and analysis of Lactobacillus paracasei penicillin-binding proteins revealed the presence of cholate-sensitive penicillin-binding protein 3 and an elongated cell shape in a cholate-sensitive strain

Penicillin-binding proteins (PBPs) are responsible for peptidoglycan synthesis. By using biotinylated ampicillin, we detected PBPs of Lactobacillus paracasei strains. Ten PBPs were identified, 7 of which had apparent molecular sizes similar to those of Escherichia coli. In the presence of cholate, s...

Descripción completa

Detalles Bibliográficos
Autores principales: HATTORI, Masahiro, TORRES, Glaezel Angelique, TANAKA, Naoto, OKADA, Sanae, ENDO, Akihito, NAKAGAWA, Junichi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BMFH Press 2016
Materias:
Note
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5395426/
https://www.ncbi.nlm.nih.gov/pubmed/28439489
http://dx.doi.org/10.12938/bmfh.16-019
Descripción
Sumario:Penicillin-binding proteins (PBPs) are responsible for peptidoglycan synthesis. By using biotinylated ampicillin, we detected PBPs of Lactobacillus paracasei strains. Ten PBPs were identified, 7 of which had apparent molecular sizes similar to those of Escherichia coli. In the presence of cholate, strain NRIC 0625 showed an elongated shape, and its putative PBP3 showed cholate-sensitive penicillin-binding activity. Furthermore, this strain was highly sensitive to cefalexin, which is known to inhibit cell division by inactivating PBP3. These results suggest that the septum synthetase PBP3 of lactic acid bacteria can be one of the targets of intestinal bile acid.

Ejemplares similares