Dataset Information

Interaction between Pseudomonas aeruginosa and Achromobacter xylosoxidans: unravelling the molecular basis of competition affecting P. aeruginosa virulence

ABSTRACT: Proteomic analysis carried out to elucidate the molecular basis of P. aeruginosa virulence reduction during interaction with A. xylosoxidans

INSTRUMENT(S):

ORGANISM(S): Achromobacter Xylosoxidans Pseudomonas Aeruginosa

SUBMITTER: Jean ARMENGAUD

LAB HEAD: Jean Armengaud

PROVIDER: PXD058911 | Pride | 2025-07-14

REPOSITORIES: Pride

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Publications

Achromobacter xylosoxidans modulates Pseudomonas aeruginosa virulence through a complex multi-target competition.

Besse Alison A Menetrey Quentin Q Jean-Pierre Vincent V Huc-Brandt Sylvaine S Aujoulat Fabien F Dupont Chloé C Chiron Raphaël R Armengaud Jean J Jumas-Bilak Estelle E Molle Virginie V Grenga Lucia L Marchandin Hélène H

Scientific reports 20250702 1

The colonization and persistence of Pseudomonas aeruginosa in chronically diseased lungs are driven by various virulence factors. However, pulmonary infections in cystic fibrosis (CF) patients are predominantly polymicrobial. While Achromobacter xylosoxidans is an opportunistic pathogen in these patients, its impact on P. aeruginosa virulence during co-infection remains largely unknown. This study investigated P. aeruginosa interaction with two clonally related A. xylosoxidans strains, Ax 198 an ...[more]

PMID: 40603430

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Project description:Membrane protein and phospholipid (PL) compositions change in response to environmental cues and during infections. Covalent modification (e.g., unsaturation and cyclopropanation) and remodeling the acyl chain length of PLs is an important bacterial adaptation mechanism. However, little is known about which bacterial pathways are regulated in response to the alteration of PL composition. Here, we show that P. aeruginosa PlaF, which modulates membrane PL composition, is important for biofilm biogenesis, and we performed whole-cell quantitative proteomics of P. aeruginosa wild-type and ∆plaF biofilms to identify pathways regulated by PlaF. The results revealed profound alterations in the abundance of 14 two-component systems (TCS), including the PprA-PprB, which controls the transition to biofilm. Activation of PprA-the PprB system observed by proteomics was confirmed by mRNA quantification. Furthermore, we have observed a unique phosphorylation pattern of transcriptional regulators, transporters and metabolic enzymes, and differential production of nine proteases in ∆plaF, indicating that PlaF-mediated virulence adaptation involves complex transcriptional and post-transcriptional regulation. Moreover, proteomics revealed that the pyoverdin-mediated iron uptake pathway proteins were depleted in ∆plaF, which agrees with decreased concentrations of extracellular pyoverdine and intracellular iron in ∆plaF and is likely responsible for its prolonged lag phase due to reduced iron uptake. Conversely, the accumulation of proteins from alternative iron-uptake systems in ∆plaF suggests that PlaF may function as a switch between different iron-acquisition pathways. The observation that ∆plaF accumulates PL-acyl chain modifying enzymes and PlsX, an initiator of de novo PL synthesis, reveals novel insights into the relationship between degradation, covalent modification and biosynthesis of PLs for membrane homeostasis. Although the precise mechanism by which PlaF simultaneously affects multiple pathways remains to be elucidated, we suggest that PlaF-catalyzed degradation of PLs is a signal which is amplified by proteins of TCS, phosphorylation and proteolytic degradation systems to elicit the global adaptive response in P. aeruginosa.

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	F491137.dat	Other
	F491137_p0.05.mzid.gz	Mzid
	F491138.dat	Other
	F491138_p0.05.mzid.gz	Mzid
	F491139.dat	Other