Differences in the sequence of PlcR transcriptional regulator-binding site affect sphingomyelinase production in Bacillus cereus.


Journal

Microbiology and immunology
ISSN: 1348-0421
Titre abrégé: Microbiol Immunol
Pays: Australia
ID NLM: 7703966

Informations de publication

Date de publication:
Apr 2022
Historique:
revised: 08 12 2021
received: 28 10 2021
accepted: 12 12 2021
pubmed: 17 12 2021
medline: 6 4 2022
entrez: 16 12 2021
Statut: ppublish

Résumé

Bacillus cereus is an opportunistic pathogen that often causes severe infections such as bacteremia, with sphingomyelinase (SMase) being a crucial virulence factor. Although many strains of B. cereus carry the SMase gene, they are classified as SMase-producing and nonproducing strains. The reason for different SMase production among B. cereus strains remains unknown. In this study, we investigated the relationship between SMase and the PlcR transcriptional regulation system to clarify the mechanism leading to varied SMase production among B. cereus strains. We analyzed the sequence of the PlcR box, which is a transcriptional regulator-binding site, located at the promoter region of SMase and phosphatidylcholine-specific phospholipase C. Based on differences in the PlcR box sequences, we classified the B. cereus strains into three groups (I, II, and III). SMase expression and activity were hardly detected in Group III strains. In Group I strains, SMase activity and its expression were maximal at the onset of the stationary phase and decreased during the stationary phase, whereas those were maintained during the stationary phase in Group II stains. On injection of B. cereus strains into mice or incubation with macrophages for phagocytosis assay, the SMase-producing Group I and II strains showed higher pathogenicity than Group III strains. These findings suggest that PlcR box sequence in B. cereus affects the production of SMase, which may provide important clinical information for the detection of highly pathogenic B. cereus strains.

Identifiants

pubmed: 34914844
doi: 10.1111/1348-0421.12959
doi:

Substances chimiques

Bacterial Proteins 0
Trans-Activators 0
Sphingomyelin Phosphodiesterase EC 3.1.4.12

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

157-165

Informations de copyright

© 2022 The Societies and John Wiley & Sons Australia, Ltd.

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Auteurs

Atsushi Yokotani (A)

Department of Microbiology and Infection Control Science, Kyoto Pharmaceutical University, Kyoto, Japan.

Fumi Takahashi (F)

Department of Microbiology and Infection Control Science, Kyoto Pharmaceutical University, Kyoto, Japan.

Ryoko Aoyama (R)

Department of Microbiology and Infection Control Science, Kyoto Pharmaceutical University, Kyoto, Japan.

Go Kamoshida (G)

Department of Microbiology and Infection Control Science, Kyoto Pharmaceutical University, Kyoto, Japan.

Tadashi Kosaka (T)

Department of Pharmacy, University Hospital, Kyoto Prefectural University of Medicine, Kyoto, Japan.

Masaki Nakanishi (M)

Division of Infection Control & Laboratory Medicine, Kyoto Prefectural University of Medicine, Kyoto, Japan.

Naohisa Fujita (N)

Kyoto Prefectural Institute of Public Health and Environment, Kyoto, Japan.

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