PXD058271

PXD058271 is an original dataset announced via ProteomeXchange.

Title	Multi-omics insights into the response of Aspergillus parasiticus to long-chain alkanes in relation to polyethylene modification
Description	In this study, we employed a multi-omics approach to study the ability of Aspergillus parasiticus MM36, an isolate derived from Tenebrio molitor intestines, to metabolize long-chain alkanes (lcAlk) and secrete enzymes able to modify polyethylene (PE). Following genome sequencing, assembly, and annotation the fungus was grown with hexadecane (C16) or a mixture of long-chain alkanesl (C24 to C36) as carbon sources and secretomes were tested for their ability to modify PE to select timepoints for the multi-omics analysis. The selected conditions were lcAlk after days 2 and 3 and C16 after day 3. Culture supernatants with lcAlk after 3 days contained the most effective secretome in PE functionalization and protein diversity. Proteomic analysis of the secretomes identified a range of induced oxidases potentially involved in lcAlk and PE functionalization. Key enzymes include multicopper oxidases, peroxidases, an unspecific peroxygenase and FAD-dependent monooxygenases. Surfactant proteins facilitating enzymatic and cellular interaction with hydrophobic PE and lcAlk, such as one hydrophobin, three hydrophobic surface-binding proteins (HsbA) and one cerato platanin, were present in all secretomes. Transcriptomic analysis comparing lcAlk to C16 cultures highlighted the enrichment of oxidoreductase activities and carboxylic acid metabolism in both lcAlk days, with transmembrane transporters and transferases predominating on day 2 and biosynthetic processes on day 3. In C16 cultures, hydrolytic enzymes, including esterases, were upregulated alongside Baeyer-Villiger monooxygenases, suggesting a shift toward sub-terminal hydroxylation. Integrating transcriptomic and secretomic data, we propose a mechanism for lcAlk assimilation by A. parasiticus MM36, involving extracellular oxyfunctionalization, hydrocarbon uptake via surface-modifying proteins and channeling through membrane transporters for energy consumption and biosynthesic processes.
HostingRepository	PRIDE
AnnounceDate	2025-05-13
AnnouncementXML	Submission_2025-05-13_01:55:49.374.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD058271
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Romanos Siaperas
SpeciesList	scientific name: Aspergillus parasiticus; NCBI TaxID: 5067;
ModificationList	2-pyrrolidone-5-carboxylic acid (Gln); acetylated residue; monohydroxylated residue; deamidated residue; iodoacetamide derivatized residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2024-11-26 01:21:06	ID requested
⏵ 1	2025-05-13 01:55:50	announced

10.1016/j.envpol.2025.126386;

Siaperas R, Taxeidis G, Gioti A, Nikolaivits E, Topakas E, Multi-omics insights into the response of Aspergillus parasiticus to long-chain alkanes in relation to polyethylene modification. Environ Pollut, 376():126386(2025) [pubmed]

10.6019/PXD058271;

ProteomeXchange project tag: EPIC-XS

submitter keyword: multi-omics, alkanes, Aspergillus,plastic pollution, biodegradation, extracellular, fungi, secretome

Evangelos Topakas
contact affiliation	Industrial Biotechnology & Biocatalysis Group, Biotechnology Laboratory, School of Chemical Engineering, National Technical University of Athens, Athens, Greece
contact email	vtopakas@chemeng.ntua.gr
lab head
Romanos Siaperas
contact affiliation	Industrial Biotechnology & Biocatalysis Group, Biotechnology Laboratory, School of Chemical Engineering, National Technical University of Athens, Athens, Greece
contact email	roman_siap@hotmail.com
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/PXD058271

PRIDE project URI

• PRIDE
  1. PXD058271
     1. Label: PRIDE project
     2. Name: Multi-omics insights into the response of Aspergillus parasiticus to long-chain alkanes in relation to polyethylene modification