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

Masahiro HATTORI; Glaezel Angelique TORRES; Naoto TANAKA; Sanae OKADA; Akihito ENDO; Junichi NAKAGAWA

doi:10.12938/bmfh.16-019

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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

Masahiro HATTORI, Glaezel Angelique TORRES, Naoto TANAKA, Sanae OKADA, Akihito ENDO, Junichi NAKAGAWA

著者情報

キーワード: penicillin-binding protein, Lactobacillus paracasei, cholate, cell division

ジャーナルフリー早期公開

論文ID: 16-019

DOI https://doi.org/10.12938/bmfh.16-019

この記事には本公開記事があります。

The final version of this article is now available: Vol. 36 (2017), No. 2 pp. 65-72

詳細

抄録

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.

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