Quorum Sensing N-acyl Homoserine Lactones-SdiA Suppresses Escherichia coli-Pseudomonas aeruginosa Conjugation through Inhibiting traI Expression
Autor: | Ni Zhang, Bin Huang, Renxin Cai, Lina Wang, Jianming Zeng, Binning Wu, Shunmei E, Xianzhang Huang, Youqiang Li, Cha Chen, Yang Lu |
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Rok vydání: | 2017 |
Předmět: |
0301 basic medicine
Microbiology (medical) antibiotic resistance Immunology Homoserine SdiA Acyl-Butyrolactones Biology medicine.disease_cause Microbiology 03 medical and health sciences chemistry.chemical_compound N-acyl homoserine lactones Escherichia coli medicine Binding site Gene Original Research Acyl-Homoserine Lactones Pseudomonas aeruginosa Escherichia coli Proteins DNA Helicases food and beverages Promoter Gene Expression Regulation Bacterial biochemical phenomena metabolism and nutrition Quorum sensing P. aeruginosa 030104 developmental biology Infectious Diseases chemistry Biochemistry Conjugation Genetic Trans-Activators conjugation |
Zdroj: | Frontiers in Cellular and Infection Microbiology |
ISSN: | 2235-2988 |
Popis: | Conjugation is a key mechanism for horizontal gene transfer and plays an important role in bacterial evolution, especially with respect to antibiotic resistance. However, little is known about the role of donor and recipient cells in regulation of conjugation. Here, using an Escherichia coli (SM10λπ)-Pseudomonas aeruginosa (PAO1) conjugation model, we demonstrated that deficiency of lasI/rhlI, genes associated with generation of the quorum sensing signals N-acyl homoserine lactones (AHLs) in PAO1, or deletion of the AHLs receptor SdiA in the donor SM10λπ both facilitated conjugation. When using another AHLs-non-producing E. coli strain EC600 as recipient cells, deficiency of sdiA in donor SM10λπ hardly affect the conjugation. More importantly, in the presence of exogenous AHLs, the conjugation efficiency between SM10λπ and EC600 was dramatically decreased, while deficiency of sdiA in SM10λπ attenuated AHLs-inhibited conjugation. These data suggest the conjugation suppression function of AHLs-SdiA chemical signaling. Further bioinformatics analysis, β-galactosidase reporter system and electrophoretic mobility shift assays characterized the binding site of SdiA on the promoter region of traI gene. Furthermore, deletion of lasI/rhlI or sdiA promoted traI mRNA expression in SM10λπ and PAO1 co-culture system, which was abrogated by AHLs. Collectively, our results provide new insight into an important contribution of quorum sensing system AHLs-SdiA to the networks that regulate conjugation. |
Databáze: | OpenAIRE |
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