{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD075156/checksum.txt"],"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD075156/batch4_of_MS_data119894.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD075156/batch2_of_MS_data117584.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD075156/batch3_of_Ms_data118610.csv"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD075156/118612_MN8_planktonic_MVs__3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD075156/119895_MN8_Biofilm_matrix__4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD075156/117585_Planktonic_MN8_MVs__2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD075156/118610_MN8_biofilm_matrix__3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD075156/117584_MN8_biofilm_Matrix__2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD075156/117586_MN8_biofilm_MVs__2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD075156/118611_MN8_biofilm_MVs__3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD075156/119894_MN8_biofilm_MVs__4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD075156/119897_Planktonic_MN8_MVs__4.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["xgwang@vt.edu"],"submitter":["Jinger Lei"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Biofilm matrix","Mn8","Biofilm","Extracellular vesicles","Staphylococcus aureus"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD075156"],"sample_protocol":["20 ug of each MV sample and matrix proteins were subjected to 10% SDS-PAGE GEL and stained by coommassie blue. Gel bands cotaining proteins were cut, and proteins were extracted, digested, and analyzed by using an LTQ Orbitrap Velons Pro ion-trap mass spectrometer (thermo Fisher) in Taplin Mass Spect facilicity in Harvard Medical School."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Peptide sequences were determined by matching the NCBI Protein database of the S. aureus MN8 genome with the acquired fragmentation pattern by the software program SEQUEST (Thermo Fisher Scientific). Sequence analysis was performed using a database containing protein sequences of Staphylococcus aureus strain MN8 downloaded from NCBI Protein. To remove contaminants and reverse hits, data were filtered to maintain an average 0.8% and 0.1% false discovery rate for protein and peptide identifications, respectively. Protein intensity was quantified as the summation of intensity values (peak height intensity) of individual peptides matched to a given protein. For enhanced confidence in protein identification, individual proteins in each datasetdata set were further filtered to maintain a minimum requirement of two total peptides and one unique peptide in at least two of the three biological replicates."],"omics_type":["Proteomics"],"labhead":["Xiaogang Wang"],"instrument_platform":[""],"labhead_affiliation":["Department of Biomedical Sciences and Pathobiology, Virginia-Maryland College of Veterinary Medicine, Virginia Polytechnic Institute and State University, Blacksburg, Virginia, United States."],"submission_type":["PARTIAL"],"species":["Staphylococcus Aureus Subsp. Aureus Mn8"],"submitter_mail":["jingerlei@vt.edu"],"publication":["41993307 Lei J, Foster M, Ng E, Gloag ES, Wang X. Extracellular membrane vesicles - previously unrecognized components of &lt;i&gt;Staphylococcus aureus&lt;/i&gt; biofilms. bioRxiv. 2026:2026.04.07.717111 10.64898/2026.04.07.717111"],"submitter_affiliation":["Department of Biomedical Sciences and Pathobiology\nVirginia-Maryland College of Veterinary Medicine, Virginia Tech"],"submitter_country":["United States"],"pubmed_abstract":["<i>Staphylococcus aureus</i> is a leading cause of biofilm-associated infections, in which communities of bacterial cells are encased in an extracellular matrix composed of polysaccharides, proteins, and extracellular DNA (eDNA) that protect bacteria from host immune defense and antibiotics. Despite their importance, the mechanisms by which matrix components are released from bacterial cells and incorporated into the biofilm matrix remain poorly understood. Using a drip-flow biofilm system, we showed that MVs were associated with the biofilm matrix formed by <i>S. aureus</i> clinical isolate MN8. Proteomic analysis of biofilm matrix proteins and purified MVs showed that biofilm-derived MVs carried cytoplasmic, membrane, and extracellular proteins that closely resembled the protein composition of the biofilm matrix but differed significantly from MVs produced by planktonic cultures. Biofilm-derived MVs carried significantly higher levels of DNA than MVs from planktonic cultures, and MV-associated DNA was resistant to DNase treatment. Although strain MN8 is known to form polysaccharide-dependent biofilms, exogenously added DNase or proteinase K significantly impaired biofilm formation and integrity. Notably, these inhibitory effects were reversed by the addition of biofilm-derived MVs, which significantly restored biofilm formation in enzyme-treated cultures. Together, these findings provide evidence that <i>S. aureus</i> MVs are generated within biofilms, and that these MVs serve as an important resource of matrix components and contribute to biofilm formation.<h4>Importance</h4>Extracellular membrane vesicles (MVs) are important mediators of intercellular communication and have been implicated in the physiology and pathogenesis of bacterial infections. While MV production in <i>S. aureus</i> planktonic cultures has been recognized for over one decade, their presence and function in <i>S. aureus</i> biofilm formation have remained unexplored. Here, we report for the first time the purification and characterization of MVs derived from <i>S. aureus</i> biofilms. Our studies demonstrate that <i>S. aureus</i> MVs are important components of the biofilm matrix that contribute to biofilm formation by serving as key carriers of matrix proteins and eDNA. This work advances our limited understanding of MVs in Gram-positive bacteria and reveal a previously unrecognized mechanism underlying <i>S. aureus</i> biofilm formation."],"pubmed_title":["Extracellular membrane vesicles - previously unrecognized components of &lt;i&gt;Staphylococcus aureus&lt;/i&gt; biofilms."],"pubmed_authors":["Lei Jinger J, Foster Misaki M, Ng Emery E, Gloag Erin S ES, Wang Xiaogang X"],"additional_accession":[]},"is_claimable":false,"name":"Proteomic analysis of extracellular membrane vesicles produced from Staphylococcus aureus biofilm and planktonic cultures","description":"This project investigates the role of extracellular membrane vesicles (MVs) in Staphylococcus aureus biofilm formation. To elucidate how MVs contribute to this process, we conducted a proteomic analysis to identify and compare proteins present in the S. aureus MN8 biofilm matrix, as well as proteins associated with MVs purified from MN8 biofilm and planktonic cultures. We identified 747 proteins in the biofilm matrix and 730 proteins in MVs purified from the biofilm, of which 576 were shared. Abundance-based correlation analysis revealed a strong positive correlation between these two protein sets. In contrast, only 568 proteins were detected in MVs derived from MN8 planktonic cultures, which exhibited a distinct composition, particularly in the cytoplasmic protein category, compared to biofilm-associated MVs. Overall, our findings demonstrate that the protein cargo of biofilm-derived MVs closely mirrors the biofilm matrix proteome, suggesting that MVs play a significant role in biofilm 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