Biology subjects

Aussel, L.

Publications and source records attributed to Aussel, L..

3 recordsLinked to original sources

bioRxiv2024

Cooperative colonization of the host and pathogen dissemination involves stochastic and spatially structured expression of virulence traits

Bacteria respond to changing environments by altering gene expression. Some responses display probabilistic cell-to-cell variation within isogenic populations. A few paradigmatic examples in animal pathogens have demonstrated that this phenotypic heterogeneity has biological relevance for virulence. We investigate single-cell flagellar expression in relation to type III secretion expression in the plant pathogen Pseudomonas syringae and describe that both systems undergo phenotypic heterogeneity throughout plant colonization. We establish that high expression of these system carries growth penalties. Stochastic, spatial and time factors shape dynamics of a phenotypically diverse population which displays division of labor during colonization: T3SSON bacteria effectors act as common goods to suppress immunity, allowing the increase of motile bacteria that actively leave the infected tissue before necrosis. This study provides a comprehensive view of how processes underlying bacterial specialization play out in the context of complex and changing environments of biological and applied relevance such as host colonization.

microbiology↗

bioRxiv2022

Periplasmic oxidized-protein repair during copper stress in E. coli: a focus on the metallochaperone CusF.

Methionine residues are particularly sensitive to oxidation by reactive oxygen or chlorine species (ROS/RCS), leading to the appearance of methionine sulfoxide in proteins. This post-translational oxidation can be reversed by omnipresent protein repair pathways involving methionine sulfoxide reductases (Msr). In the periplasm of Escherichia coli, the enzymatic system MsrPQ, whose expression is triggered by the RCS, controls the redox status of methionine residues. Here we report that MsrPQ synthesis is also induced by copper stress via the CusSR two-component system, and that MsrPQ plays a role in copper homeostasis by maintaining the activity of the copper efflux pump, CusCFBA. Genetic and biochemical evidence suggest the metallochaperone CusF is the substrate of MsrPQ and our study reveal that CusF methionines are redox sensitive and can be restored by MsrPQ. Thus, the evolution of a CusSR-dependent synthesis of MsrPQ allows keeping copper homeostasis under aerobic conditions by maintenance of the reduced state of Met residues in copper-trafficking proteins. AUTHOR SUMMARYOur study investigates the interconnection between the copper stress response and the methionine redox homeostasis in the Gram-negative bacterium Escherichia coli. We report that the copper-activation of the CusSR two-component system induces the expression of the periplasmic oxidized-protein repair system, MsrPQ. We demonstrate that MsrPQ is crucial for CusCFBA copper efflux pump activity under aerobic conditions as it maintains the periplasmic component CusF in its functional reduced form. Methionine emerges as a critical residue in copper trafficking proteins: however this naturally-selected advantage must be balanced by methionines high susceptibility to oxidation. Therefore the induction of MsrPQ by copper allows copper homeostasis under aerobic conditions, illustrating that E. coli has developed an integrated and dynamic circuit for sensing and counteracting stress caused by copper and oxidants, thus allowing bacteria to adapt to host cellular defences.

microbiology↗

bioRxiv2021

HypVW is an HOCl-Sensing Two Component System in Escherichia coli

Two component systems (TCS) are signalling pathways that allow bacterial cells to sense, respond and adapt to fluctuating environments. Among the classical TCS of Escherichia coli, YedVW has been recently showed to be involved in the regulation of msrPQ, encoding for the periplasmic methionine sulfoxide reductase system. In this study, we demonstrate that hypochlorous acid (HOCl) induces the expression of msrPQ in a YedVW dependant manner, whereas H2O2, NO and paraquat (a superoxide generator) do not. Therefore, YedV appears to be an HOCl-sensing histidine kinase. Based on this finding, we proposed to rename this system HypVW. Moreover, using a directed mutagenesis approach, we show that Met residues located in the periplasmic loop of HypV (formerly YedV) are important for its activity. Given that HOCl oxidizes preferentially Met residues, we bring evidences that HypV could be activated via the reversible oxidation of its methionine residues, thus conferring to MsrPQ a role in switching HypVW off. Based on these results, we propose that the activation of HypV by HOCl could occur through a Met redox switch. HypVW appears to be the first characterized TCS able to detect HOCl in E. coli. This study represents an important step in understanding the mechanisms of reactive chlorine species resistance in prokaryotes. IMPORTANCEUnderstanding molecularly how bacteria respond to oxidative stress is crucial to fight pathogens. HOCl is one of the most potent industrial and physiological microbiocidal oxidant. Therefore, bacteria have developed counterstrategies to survive HOCl-induced stress. Over the last decade, important insights into these bacterial protection factors have been obtained. Our work establishes HypVW as an HOCl-sensing two component system in Escherichia coli MG1655 which regulates the expression of the periplasmic HOCl-oxidized proteins repair system MsrPQ. Moreover we bring evidences suggesting that HOCl could activate HypV through a methionine redox switch.

microbiology↗