PXD037737

PXD037737 is an original dataset announced via ProteomeXchange.

Title	Proteomics reveals virulence adaptation of Pseudomonas aeruginosa phospholipase mutant with altered membrane phospholipid composition
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.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_08:45:00.058.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Gereon Poschmann
SpeciesList	scientific name: Pseudomonas aeruginosa PAO1; NCBI TaxID: 208964;
ModificationList	acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2022-10-26 01:44:19	ID requested
1	2023-04-25 08:48:57	announced
⏵ 2	2023-11-14 08:45:08	announced	2023-11-14: Updated project metadata.

Caliskan M, Poschmann G, Gudzuhn M, Waldera-Lupa D, Molitor R, Strunk CH, Streit WR, Jaeger KE, St, ü, hler K, Kovacic F, Pseudomonas aeruginosa responds to altered membrane phospholipid composition by adjusting the production of two-component systems, proteases and iron uptake proteins. Biochim Biophys Acta Mol Cell Biol Lipids, 1868(6):159317(2023) [pubmed]

submitter keyword: two-component systems, phospholipids, physiology,biofilm, iron homeostasis, proteases, pathogen

Gereon Poschmann
contact affiliation	Proteome Research (AG Stühler) Institute of Molecular Medicine Heinrich Heine University Düsseldorf 40225 Düsseldorf Germany
contact email	gereon.poschmann@hhu.de
lab head
Gereon Poschmann
contact affiliation	Molecular Proteomics Laboratory
contact email	gereon.poschmann@hhu.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD037737
     1. Label: PRIDE project
     2. Name: Proteomics reveals virulence adaptation of Pseudomonas aeruginosa phospholipase mutant with altered membrane phospholipid composition