Autoinducer-2 and bile salts induce c-di-GMP synthesis to repress the T3SS via a T3SS chaperone

Li, Shuyu; Sun, Hengxi; Li, Jianghan; Zhao, Yujiao; Wang, Ruiying; Xu, Lei; Duan, Chongyi; Li, Jialin; Wang, Zhuo; Liu, Qinmeng; Wang, Yao; Ouyang, Songying; Shen, Xihui; Zhang, Lei

doi:10.1038/s41467-022-34607-9

Cited by 8 publications

(22 citation statements)

References 70 publications

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“…1a). Consistent with our earlier nding 32 , stimulation with bile salts did not alter the intracellular concentration of c-di-GMP in the ΔyedQ mutant, but signi cantly increased intracellular c-di-GMP levels in the wild-type and complemented strains (Supplementary Fig. 1a).…”

Section: Resultssupporting

confidence: 91%

“…In addition, deletion of yedQ that encodes the DGC sensing bile salts also abolished the induction of the T6SS genes after intestinal colonization (Fig. 7a), consistent with previous in vitro ndings that the presence of bile salts does not increase intracellular c-di-GMP levels in the ΔyedQ mutant 32 . These results suggest that bile salts stimulate c-di-GMP synthesis to activate the SPI-6 T6SS of S. Typhimurium through counteracting H-NS-mediated transcriptional repression during intestinal infection.…”

Section: The C-di-gmp-mediated Derepression Of the T6ss Via Targeting...supporting

confidence: 91%

“…3b). The K d value presented here is comparable to those previously reported for other well-established c-di-GMP receptors [31][32][33] . By contrast, interactions of H-NS with c-di-AMP or cGMP were not detected under the same experimental conditions (Supplementary Fig.…”

Section: H-ns Directly and Speci Cally Binds To C-di-gmpsupporting

confidence: 90%

“…While extracellular stimuli can modulate intracellular levels of c-di-GMP by regulating the expression or activity of DGCs or PDEs, c-di-GMP-binding effectors convert dynamic changes in c-di-GMP concentration into speci c cellular responses 30 . c-di-GMPbinding effectors identi ed include mRNA riboswitches, transcription factors, a broad variety of enzymes, adaptor proteins and chaperone proteins [29][30][31][32] .…”

Section: Introductionmentioning

confidence: 99%

“…Bacteria use c-di-GMP to control a wide range of biological processes, including motility, bio lm formation, cell cycle progression and protein secretion 29 . c-di-GMP has been shown to control type II secretion systems (T2SSs), type III secretion systems (T3SSs), as well as type VI secretion systems (T6SSs) [32][33][34] . Although the exact role of c-di-GMP in T2SSs and T3SSs has been clari ed in various pathogenic bacteria 32,33 , c-di-GMP effectors through which this second messenger exerts its effect on T6SSs remain to be identi ed.…”

Section: Introductionmentioning

confidence: 99%

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Cyclic di-GMP rescues H-NS–mediated silencing of bacterial type VI secretion systems

Zhang

Liu

et al. 2023

Preprint

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The type VI secretion system (T6SS) is a widespread versatile machine that is encoded by many gram-negative bacteria and plays crucial roles in interbacterial competition and bacteria-host interactions. Histone-like nucleoid structuring protein (H-NS) is a global regulator that represses the expression of T6SS genes in various pathogens and environmental isolates. Bacteria appear to have evolved regulatory mechanisms to relieve the transcriptional repression mediated by H-NS when the T6SS activity is required, but the underlying molecular mechanism awaits elucidation. Here we show that elevated intracellular cyclic di-GMP (c-di-GMP) levels alleviate the H-NS–mediated repression of the T6SS in Salmonella enterica serovar Typhimurium.Mechanistically, c-di-GMP directly binds to the H-NS protein to abrogate its binding to the T6SS promoters, thus derepressing expression of the T6SS genes. Furthermore, we provide evidence that bile salts-induced increase in intracellular c-di-GMP levels leads to activation of the S. TyphimuriumT6SS within the host gut, facilitating its killing of commensal bacteria and successful colonization. The observations that c-di-GMP derepresses gene expression via targeting the H-NS or H-NS-like proteins in Vibrio parahaemolyticus, Pseudomonas aeruginosaand Pseudomonas putida suggest a general mechanism through which the H-NS family of proteins act as environment-sensing regulators in Gram-negative bacteria.

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Section: Resultssupporting

confidence: 91%

Section: The C-di-gmp-mediated Derepression Of the T6ss Via Targeting...supporting

confidence: 91%

Section: H-ns Directly and Speci Cally Binds To C-di-gmpsupporting

confidence: 90%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Cyclic di-GMP rescues H-NS–mediated silencing of bacterial type VI secretion systems

Zhang

Liu

et al. 2023

Preprint

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Paenibacillus polymyxa YLC1: a promising antagonistic strain for biocontrol of Pseudomonas syringae pv. actinidiae, causing kiwifruit bacterial canker

Wang

Tan

et al. 2023

Pest Management Science

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BackgroundKiwifruit bacterial canker (KBC) caused by Pseudomonas syringae pv. actinidiae (Psa) is the main limiting factor in the kiwifruit industry. This study aimed to identify bacterial strains with antagonistic activity against Psa, analyze antagonistically active substances and provide a new basis for the biological control of KBC.ResultsA total of 142 microorganisms were isolated from the rhizosphere soil of asymptomatic kiwifruit. Among them, an antagonistic bacterial strain was identified as Paenibacillus polymyxa YLC1 by 16S rRNA sequencing. KBC control by strain YLC1 (85.4%) was comparable to copper hydroxide treatment (81.8%) under laboratory conditions and field testing. Active substances of strain YLC1 were identified by genetic sequence analysis using antiSMASH. Six biosynthetic active compound gene clusters were identified as encoding ester peptide synthesis, such as polymyxins. An active fraction was purified and identified as polymyxin B1 using chromatography, hydrogen nuclear magnetic resonance (NMR), and liquid chromatography‐mass spectrometry. In addition, polymyxin B1 also was found significantly to suppress the expression of T3SS‐related genes, but did not affect the growth of Psa at low concentrations.ConclusionIn this study, a biocontrol strain P. polymyxa YLC1 obtained from kiwifruit rhizosphere soil exhibited excellent control effects on KBC in vitro and in field tests. Its active compound was identified as polymyxin B1, which inhibits a variety of pathogenic bacteria. We conclude that P. polymyxa YLC1 is a biocontrol strain with excellent prospects for development and application. © 2023 Society of Chemical Industry.

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c-di-GMP inhibits the DNA binding activity of H-NS in Salmonella

Li,

Liu,

Duan

et al. 2023

Nat Commun

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Cyclic di-GMP (c-di-GMP) is a second messenger that transduces extracellular stimuli into cellular responses and regulates various biological processes in bacteria. H-NS is a global regulatory protein that represses expression of many genes, but how H-NS activity is modulated by environmental signals remains largely unclear. Here, we show that high intracellular c-di-GMP levels, induced by environmental cues, relieve H-NS-mediated transcriptional silencing in Salmonella enterica serovar Typhimurium. We find that c-di-GMP binds to the H-NS protein to inhibit its binding to DNA, thus derepressing genes silenced by H-NS. However, c-di-GMP is unable to displace H-NS from DNA. In addition, a K107A mutation in H-NS abolishes response to c-di-GMP but leaves its DNA binding activity unaffected in vivo. Our results thus suggest a mechanism by which H-NS acts as an environment-sensing regulator in Gram-negative bacteria.

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Autoinducer-2 and bile salts induce c-di-GMP synthesis to repress the T3SS via a T3SS chaperone

Cited by 8 publications

References 70 publications

Cyclic di-GMP rescues H-NS–mediated silencing of bacterial type VI secretion systems

Cyclic di-GMP rescues H-NS–mediated silencing of bacterial type VI secretion systems

Paenibacillus polymyxa YLC1: a promising antagonistic strain for biocontrol of Pseudomonas syringae pv. actinidiae, causing kiwifruit bacterial canker

c-di-GMP inhibits the DNA binding activity of H-NS in Salmonella

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