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Lactate prevents Salmonella enterica biofilm formation by inhibiting curli and cellulose expression

ABSTRACT: Lactate prevents Salmonella enterica biofilm formation by inhibiting curli and cellulose expression

PROVIDER: PRJNA1074366 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR27905669_1.fastq.gz	Fastqsanger.gz
	SRR27905669_2.fastq.gz	Fastqsanger.gz
	SRR27905670_1.fastq.gz	Fastqsanger.gz
	SRR27905670_2.fastq.gz	Fastqsanger.gz
	SRR27905671_1.fastq.gz	Fastqsanger.gz

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Lactate prevents Salmonella enterica biofilm formation by inhibiting curli and cellulose expression

Project description:Salmonella enterica serovar Typhimurium (S. Typhimurium) infection triggers an inflammatory response that changes the concentration of luminal metabolites in the gut, resulting in a distinct environment from a healthy one. We recently demonstrated that S. Typhimurium possesses the ability to form biofilms within the host environment and responds to nitrate as a signaling molecule, enabling it to modulate the transition between sessile and planktonic states. To investigate whether S. Typhimurium utilizes additional metabolites to regulate its behavior, our study delved into the impact of inflammatory metabolites on biofilm formation. Employing a transcriptomic approach we unveiled that lactate enhances the transcription of flagella and invasion genes, highlighting the active role of lactate in modulating the transition of S. Typhimurium from biofilm to motile states. All these findings propose that, as occurring with nitrate, lactate is an inflammatory metabolite being used by S. Typhimurium to support virulence.

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Project description:To evaluate the biological impact of cellulose nanofibrils (CNFs) at the transcriptional level, we conducted whole-genome microarray analyses on human bronchial epithelial cells (BEAS-2B) exposed to CNFs with different physicochemical properties. The results were compared with those from exposures to microcrystalline cellulose (MCC).

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Project description:L. plantarum is known to possess an L-lactate inducible lactate racemase activity (Goffin et al. 2005. J. Bacteriol. 187:6750). In the present study, microarrays were used in order to identify all genes that are up-regulated by L-lactate, but not by a racemic mixture of D- and L-lactate. A mutant of L. plantarum NCIMB8826 deficient for NAD-dependent L-lactate activity (TF101; Ferain et al. 1994. 176:596), and thus producing no L-lactate, was grown in MRS medium at 28Â°C until mid-exponential phase (OD600nm 0.75). The culture was then divided into 3 sub-cultures. Optically pure sodium L-lactate (200 mM) was added to the first sub-culture (TF101 + L-lac 200 mM). An equimolar mixture of sodium D- and L-lactate (100 mM each) was added to the second sub-culture (TF101 + L/D-lac 200 mM). The third sub-culture was not treated (TF101; reference sample). The three sub-cultures were further incubated at 28Â°C for 1h30 (a time known to be sufficient for induction of lactate racemase activity by L-lactate). Cells were harvested by centrifugation. Microarray data were used ot identify genes that are specifically induced by L-lactate (comparison of TF101 with TF101 + L-lac 200 mM), but not by DL-lactate (comparison of TF101 with T101 + L/D-lac 200 mM). There are no biological replicates.

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