PXD064268

PXD064268 is an original dataset announced via ProteomeXchange.

Title	Exploration of phosphoproteins in Acinetobacter baumannii
Description	Acinetobacter baumannii is a multidrug-resistant bacterium that has gained significant attention in recent years due to its involvement in a growing number of hospital-acquired infections. The World Health Organization has classified it as a critical priority pathogen, underscoring the urgent need for new therapeutic strategies. Post-translational modifications, such as phosphorylation, play essential roles in various bacterial processes, including antibiotic resistance, virulence or biofilm formation. Although proteomics has increasingly enabled their characterization, the identification of phosphorylated peptides remains challenging, primarily due to the enrichment procedures. In this study, we focused on characterizing serine, threonine, and tyrosine phosphorylation in the A. baumannii ATCC 17978 strain. We optimized three parameters for the phosphopeptide enrichment using titanium dioxide (TiO₂) beads (number of enrichment fractions between phosphopeptides and TiO2 beads, peptides amount, and loading buffer) to determine the most effective conditions for maximizing phosphopeptide identification. Using this optimized protocol, we identified 384 unique phosphorylation sites across 241 proteins, including 260 novel phosphosites previously unreported in A. baumannii. Several of these phosphorylated proteins are involved in critical bacterial processes such as antimicrobial resistance, biofilm formation or pathogenicity. We discuss these proteins, focusing on the potential functional implications of their phosphorylation. Notably, we identified 34 phosphoproteins with phosphosites localized at functional sites, such as active sites, multimer interfaces, or domains important for structural integrity. Our findings significantly expand the current phosphoproteomic landscape of A. baumannii and support the hypothesis that PTMs, particularly phosphorylation, play a central regulatory role in its physiology and pathogenic potential.
HostingRepository	PRIDE
AnnounceDate	2025-09-04
AnnouncementXML	Submission_2025-09-03_18:24:40.257.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Nicolas Nalpas
SpeciesList	scientific name: Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377); NCBI TaxID: 400667;
ModificationList	phosphorylated residue
Instrument	Orbitrap Eclipse

Revision	Datetime	Status	ChangeLog Entry
0	2025-05-24 17:23:56	ID requested
⏵ 1	2025-09-03 18:24:40	announced

Dataset with its publication pending

submitter keyword: Acinetobacter baumannii

phosphorylation

post-translational modification

proteomic

biofilm

virulence

Julie Hardouin
contact affiliation	University of Rouen Normandie, INSA Rouen Normandie, CNRS, Polymers, Biopolymers, Surfaces Laboratory UMR 6270, F-76000 Rouen, France
contact email	julie.hardouin@univ-rouen.fr
lab head
Nicolas Nalpas
contact affiliation	University of Rouen
contact email	nalpas.nicolas@gmail.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD064268
     1. Label: PRIDE project
     2. Name: Exploration of phosphoproteins in Acinetobacter baumannii