PXD059432-1

PXD059432 is an original dataset announced via ProteomeXchange.

Title	Lacticaseibacillus paracasei derived Extracellular vesicles LC-MS/MS
Description	Owing to their ability to secrete antimicrobials and benefit human health, lactic acid bacteria (LAB) cultures are an attractive nontoxic alternative to antibiotics for preserving food and combating pathogenic infections. Given that this strategy has several limitations, including strain-dependent antimicrobial effectiveness, reduced efficacy against multidrug-resistant strains, and difficulties in large-scale production without bacterial contamination, current research focuses on identifying and utilizing endolysins (enzymes that degrade bacterial cell walls) produced by novel or engineered LAB cultures to inhibit pathogen growth. The challenges faced by this approach (e.g., bactericidal activity lower than that of antibiotics, susceptibility to degradation by proteases, and high purification and quality control costs) can be overcome using engineered LAB-derived extracellular vesicles (LEVs) displaying pathogen-specific endolysins on their surface to directly recognize and eliminate target pathogens. Given that no LEV surface-displayed proteins (SDPs) have been characterized to date, this study identifies and characterizes a LEV SDP (LP-SDP3) from Lacticaseibacillus paracasei using proteomic analysis, heterologous expression of candidate SDPs, biochemical analysis, and SpyTag–SpyCatcher reactions. LP-SDP3 homologs are found in Escherichia coli and other LAB strains, exhibiting the same function in E. coli and Lactococcus lactis. Endolysin (PlyF307SQ-8C)-displaying LEVs derived from L. paracasei selectively kill Staphylococcus aureus, exhibiting an activity comparable with that of purified PlyF307SQ-8C. This study is the first to identify a universal extracellular vesicle SDP for E. coli and LAB strains, demonstrating its potential as a platform for developing endolysin–extracellular vesicle antibacterials without the need for labor-intensive and costly endolysin preparation.
HostingRepository	PRIDE
AnnounceDate	2025-07-21
AnnouncementXML	Submission_2025-07-20_18:23:01.107.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD059432
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Kwang-sun Kim
SpeciesList	scientific name: Lactobacillus paracasei ATCC 334; NCBI TaxID: 321967;
ModificationList	TMT6plex-126 reporter+balance reagent acylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	liquid chromatography separation

Revision	Datetime	Status	ChangeLog Entry
0	2025-01-03 21:19:40	ID requested
⏵ 1	2025-07-20 18:23:01	announced

10.6019/PXD059432;

10.1016/J.CEJ.2025.162196;

submitter keyword: Surface-displayed protein,Lacticaseibacillus paracasei derived Extracellular vesicles, LC-MS/MS

Kwang-sun Kim
contact affiliation	Department of Chemistry and Chemistry Institute for Functional Materials, Pusan National University, Busan 46241, South Korea
contact email	kwangsun.kim@pusan.ac.kr
lab head
Kwang-sun Kim
contact affiliation	Pusan National University
contact email	kwangsun.kim@pusan.ac.kr
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD059432
     1. Label: PRIDE project
     2. Name: Lacticaseibacillus paracasei derived Extracellular vesicles LC-MS/MS