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ABSTRACT: Identification of small molecule inhibitors of the Pathogen Box against Vibrio cholerae

PROVIDER: PRJNA771235 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR16345277.fastq.gz	Fastqsanger.gz
	SRR16345278.fastq.gz	Fastqsanger.gz
	SRR16345279.fastq.gz	Fastqsanger.gz
	SRR16345280.fastq.gz	Fastqsanger.gz
	SRR16345281.fastq.gz	Fastqsanger.gz

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Identification of small molecule inhibitors of the Pathogen Box against Vibrio cholerae

Project description:Identification of small molecule inhibitors of the Pathogen Box against Vibrio cholerae

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Identification of small molecule inhibitors of the Pathogen Box against Vibrio cholerae

Project description:Antimicrobial resistance (AMR) has become a serious public and economic threat. The rate of bacteria acquiring AMR surpasses the rate of new antibiotics discovery, projecting more deadly AMR infections in the future. The Pathogen Box is an open-source library of drug-like compounds that can be screened for antibiotic activity. We have screened molecules of the Pathogen Box against Vibrio cholerae, the cholera-causing pathogen, and successfully identified two compounds, MMV687807 and MMV675968, that inhibit growth. RNA-seq analyses of V. cholerae after incubation with each compound revealed that both compounds affect cellular functions on multiple levels including carbon metabolism, iron homeostasis, and biofilm formation. In addition, whole-genome sequencing analysis of spontaneous resistance mutants identified an efflux system that confers resistance to MMV687807. We also identified that the dihydrofolate reductase is the likely target of MMV675968 suggesting it acts as an analog of trimethoprim but with a minimum inhibitory concentration (MIC) 14-fold lower than trimethoprim in molar concentration. In summary, these two compounds that effectively inhibit V. cholerae and other bacteria may lead to the development of new antibiotics for better treatment of the cholera disease.

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Chemoproteomic profiling of host and pathogen enzymes active in cholera

Project description:Activity-based protein profiling (ABPP) is a chemoproteomic tool for detecting active enzymes in complex biological systems. We used ABPP to identify secreted bacterial and host serine hydrolases that are active in animals infected with the cholera pathogen Vibrio cholerae. Four V. cholerae proteases were consistently active in infected rabbits, and one, VC0157 (renamed IvaP), was also active in human cholera stool. Inactivation of IvaP influenced the activity of other secreted V. cholerae and rabbit enzymes in vivo, while genetic disruption of all four proteases increased the abundance and binding of an intestinal lectin—intelectin—to V. cholerae in infected rabbits. Intelectin also bound to other enteric bacterial pathogens, suggesting it may constitute a previously unrecognized mechanism of bacterial surveillance in the intestine that is inhibited by pathogen-secreted proteases. Our work demonstrates the power of activity-based proteomics to reveal host-pathogen enzymatic dialogue in an animal model of infection.

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Project description:The experiment contains ChIP-seq data for Vibrio cholerae strain N16961. The strain was grown at 37 degrees in M9 minimal medium and crosslinked with 1 % (v/v) formaldehyde. After sonication, to break open cells and fragment DNA, immunoprecipitations were done using no antibodies (mock immunoprecipitations) or antibodies against CRP or the RNA polymerase sigma 70 subunit. Libraries were prepared using DNA remaining after immunoprecipitation.

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Three autoinducer molecules act synergistically to control virulence gene expression in Vibrio cholerae [dataset 1]

Project description:Bacteria use quorum sensing (QS) to monitor cell density and coordinate group behaviours. In Vibrio cholerae, the causative agent of cholera disease, QS is linked to virulence gene expression via the autoinducer molecules, AI-2 and CAI-1. Both autoinducers share one signal transduction pathway to control AphA production, a key transcriptional activator of virulence genes. In this study, we demonstrate that the recently identified autoinducer, DPO, also controls AphA production in V. cholerae. DPO acts through the transcriptional activator, VqmA, and the VqmR small RNA to reduce AphA levels at the post-transcriptional level. Consequently, DPO inhibits virulence gene expression in V. cholerae, including repression of the cholera toxin, a key factor required for disease in humans. VqmR-mediated repression of AphA links the AI-2/CAI-1 and DPO-dependent QS pathways of V. cholerae and global transcriptome analysis indicate that all three autoinducers are required for full QS function. Together, our data provide the first view on autoinducer interplay in V. cholerae and highlight the importance of post-transcriptional gene regulation for collective functions in this major human pathogen.

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