PXD048770

PXD048770 is an original dataset announced via ProteomeXchange.

Title	Mapping of mycobacterial lipolytic enzymes involved in triacylglycerol accumulation as intrabacterial lipid inclusions using multi-target inhibitor-like affinity-based probes
Description	Mycobacteria are known for their unique and complex cell wall architecture, characterized by distinct lipid-rich outer layers, making lipid metabolism a central point of their physiological processes. One crucial aspect of all mycobacteria is their ability to metabolize host lipids and to accumulate the resulting neutral lipids in their own cytoplasm in the form of intrabacterial lipid inclusions (ILI). These lipid-rich organelles consist of a hydrophobic core containing neutral lipids, essentially triacylglycerol (TAG), surrounded by a phospholipid monolayer, associated with numerous proteins. These ILI not only serve as reservoirs for energy storage and provide a platform for the synthesis and maintenance of lipids, which are essential for the adaptability and survival of mycobacteria under various environmental stresses. How these mycobacteria acquire host lipids and how ILI are formed remain important and largely unanswered questions. More generally, the anabolism and catabolism of ILI enhance the survival and long-term persistence of mycobacteria and thus represent two major processes controlled by a number of enzymes and regulatory proteins that play an essential role in the biosynthesis, modification, and utilization of these lipid inclusions. In this context, we report here the synthesis of Oxadiazolone (OX) and the Cyclophostin & Cyclipostins (CyC) activity-based probes, and their use for the direct capture of target proteins in M. abscessus growing under carbon excess and nitrogen-deprived in vitro conditions that promote TAG production and ILI-positive phenotype, via bio-orthogonal click-chemistry activity-based protein profiling (CC-ABPP). This approach led to the identification of a set of 65 enzymes potentially involved in the global processes related to ILI anabolism. Among these enzymes, the long-chain-fatty-acid--CoA ligase MAB_1978c/FadD15 has been validated not only as a pivotal enzyme colocalized on ILI, but above all as a major contributor in ILI formation in M. abscessus.
HostingRepository	PRIDE
AnnounceDate	2025-05-12
AnnouncementXML	Submission_2025-05-12_09:07:58.270.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	AUDEBERT Stephane
SpeciesList	scientific name: Mycobacterium abscessus; NCBI TaxID: 36809;
ModificationList	iodoacetamide derivatized residue
Instrument	Q Exactive Plus

Revision	Datetime	Status	ChangeLog Entry
0	2024-01-22 10:52:16	ID requested
⏵ 1	2025-05-12 09:07:58	announced

Dataset with its publication pending

submitter keyword: Mycobacterium, LC_MSMS, Activity-based protein profiling

multitarget inhibitor-like affinity-based probes

lipid metabolism

Cyclipostins & Cyclophostin

Oxadiazolone

Dr Jean-François Cavalier
contact affiliation	Lipolysis and Bacterial Pathogenicity team, LISM UMR7255, CNRS, Aix-Marseille Univ. , IMM FR3479, Marseille, France
contact email	jfcavalier@imm.cnrs.fr
lab head
AUDEBERT Stephane
contact affiliation	Marseille Proteomic, Centre de Recherche en Cancérologie de Marseille, Inserm UMR1068, CNRS UMR7258, Aix Marseille Université U105, Institut Paoli Calmettes, 27 Boulevard Leï Roure CS30059 13273 Marseille Cedex 09 France
contact email	stephane.audebert@inserm.fr
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2025/05/PXD048770

PRIDE project URI

• PRIDE
  1. PXD048770
     1. Label: PRIDE project
     2. Name: Mapping of mycobacterial lipolytic enzymes involved in triacylglycerol accumulation as intrabacterial lipid inclusions using multi-target inhibitor-like affinity-based probes