PXD031809

PXD031809 is an original dataset announced via ProteomeXchange.

Title	Proteomic analysis reveals enzymes for β-D-glucan formation and degradation in Levilactobacillus brevis TMW 1.2112
Description	Bacterial exopolysaccharide (EPS) formation is crucial for biofilm formation, protection against environmental factors or as storage compounds. EPSs produced by lactic acid bacteria (LAB) are appropriate for applications in food fermentation or the pharmaceutical industry, yet the dynam-ics of formation and degradation thereof are rather poorly described. This study focuses on car-bohydrate active enzymes, including glycosyl transferases (GT) and glycoside hydrolases (GH), and their roles in the formation and potential degradation of O2-substituted (1,3)-β-D-glucan of Levilactobacillus (L.) brevis TMW 1.2112. The fermentation broth of L. brevis TMW 1.2112 was ana-lyzed for changes in viscosity, β-glucan and D-glucose concentrations during exponential, sta-tionary and early death phase. While the viscosity reached its maximum during stationary phase and subsequently decreased, the β-glucan concentration only increased to a plateau. Results were correlated with secretome and proteome data to identify involved enzymes and pathways. The suggested pathway for β-glucan biosynthesis involved a β-1,3 glucan synthase (GT2) and en-zymes from maltose phosphorylase (MP) operons. The decreased viscosity appeared to be associ-ated with cell lysis as the β-glucan concentration did not decrease most likely due to missing ex-tracellular carbohydrate active enzymes. In addition, an operon was discovered containing known moonlighting genes, all of which were detected in both proteome and secretome samples.
HostingRepository	PRIDE
AnnounceDate	2022-03-21
AnnouncementXML	Submission_2022-03-21_00:37:35.571.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Christina Ludwig
SpeciesList	scientific name: Levilactobacillus brevis; NCBI TaxID: 1580;
ModificationList	No PTMs are included in the dataset
Instrument	Q Exactive HF-X

Revision	Datetime	Status	ChangeLog Entry
0	2022-02-21 10:47:58	ID requested
⏵ 1	2022-03-21 00:37:35	announced

Dataset with its publication pending

submitter keyword: Levilactobacillus brevis TMW 1.2112, β-glucan, exopolysaccharide, glycosyltransferase, glycosyl hydrolase, moonlighting proteins, secretome, proteome

Christina Ludwig
contact affiliation	Bavarian Center for Biomolecular Mass Spectrometry, Technical University of Munich, Freising, Germany
contact email	tina.ludwig@tum.de
lab head
Christina Ludwig
contact affiliation	TU Munich
contact email	tina.ludwig@tum.de
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/2022/03/PXD031809

PRIDE project URI

• PRIDE
  1. PXD031809
     1. Label: PRIDE project
     2. Name: Proteomic analysis reveals enzymes for β-D-glucan formation and degradation in Levilactobacillus brevis TMW 1.2112