PXD019825

PXD019825 is an original dataset announced via ProteomeXchange.

Title	Biophysical, proteomic, and lipidomic characterization of Streptococcus mutans extracellular membrane vesicles from wild-type, ΔsrtA, and Δsfp strains provides novel information regarding vesiculogenesis and its function
Description	Extracellular membrane vesicles (EMVs) are produced by many Gram-positive organisms, but information regarding vesiculogenesis is largely unknown. In this study, we isolated and characterized EMVs derived from the oral pathogen Streptococcus mutans and two deletion mutants, ΔsrtA and Δsfp. ΔsrtA EMVs were notably enlarged, and the AtlA autolysin was unprocessed in this strain. EMVs from all strains contained proteins involved in cell wall biogenesis and cell architecture, bacterial adhesion, biofilm cell density and matrix development, and intermolecular competition with other microorganisms. Proteomic and lipidomic analyses showed that vesicular and cytoplasmic membranes are dissimilar in many respects. A higher proportion of vesicular proteins are transported by the general secretion pathway, with SecA identified as a prominent EMV component. In contrast, cytoplasmic membranes were over-represented in multi-pass transmembrane protein substrates of co-translational transport machineries. EMVs from the wild-type (WT), but not the mutant strains, were enriched in cardiolipin compared to the cytoplasmic membrane, and all EMVs were over-represented in polyketides and flavonoids. Both vesicular and cytoplasmic membranes were rich in long-chain fatty acids, including saturated, monounsaturated, and polyunsaturated, except for Δsfp EMVs that contained exclusively polyunsaturated fatty acids. Lipoproteins were less prevalent in EMVs of all three strains compared to their cytoplasmic membranes. This study provides insight into biophysical characteristics of S. mutans EMVs and indicates discrete partitioning of protein and lipid components between EMVs and corresponding cytoplasmic membranes of both WT and mutant strains.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:15:20.626.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD019825
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Joyce Morales Aparicio
SpeciesList	scientific name: Streptococcus mutans serotype C; NCBI TaxID: 40287;
ModificationList	No PTMs are included in the dataset
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2020-06-16 23:27:56	ID requested
1	2020-11-17 08:54:12	announced
⏵ 2	2024-10-22 05:15:21	announced	2024-10-22: Updated project metadata.

Morales-Aparicio JC, Lara Vasquez P, Mishra S, Barr, á, n-Berd, ó, n AL, Kamat M, Basso KB, Wen ZT, Brady LJ, Extracellular Membrane Vesicle Biogenesis. Front Microbiol, 11():570219(2020) [pubmed]

10.3389/fmicb.2020.570219;

10.6019/PXD019825;

submitter keyword: Vesicles, lipidome, proteome, Streptococcus mutans, membrane

L. Jeannine Brady
contact affiliation	University of Florida, Department of Oral Biology
contact email	jbrady@dental.ufl.edu
lab head
Joyce Morales Aparicio
contact affiliation	University of Florida
contact email	corijoys@ufl.edu
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/2020/11/PXD019825

PRIDE project URI

• PRIDE
  1. PXD019825
     1. Label: PRIDE project
     2. Name: Biophysical, proteomic, and lipidomic characterization of Streptococcus mutans extracellular membrane vesicles from wild-type, ΔsrtA, and Δsfp strains provides novel information regarding vesiculogenesis and its function