<HashMap><database>JPOST Repository</database><file_versions><headers><Content-Type>application/xml</Content-Type></headers><body><files><Wiff>https://storage.jpostdb.org/JPST001830/files/210623_Sa+PaOMVs2_SWATH.wiff</Wiff><Wiff>https://storage.jpostdb.org/JPST001830/files/210623_Sa+PaOMVs1_SWATH.wiff.scan</Wiff><Wiff>https://storage.jpostdb.org/JPST001830/files/210623_Sa_Cont3_IDA.wiff</Wiff><Wiff>https://storage.jpostdb.org/JPST001830/files/210623_Sa_Cont3_SWATH.wiff</Wiff><Wiff>https://storage.jpostdb.org/JPST001830/files/210623_Sa+PaOMVs2_IDA.wiff</Wiff><Wiff>https://storage.jpostdb.org/JPST001830/files/210623_Sa+PaOMVs3_IDA.wiff.scan</Wiff><Wiff>https://storage.jpostdb.org/JPST001830/files/210623_Sa+PaOMVs2_IDA.wiff.scan</Wiff><Wiff>https://storage.jpostdb.org/JPST001830/files/210623_Sa+PaOMVs1_SWATH.wiff</Wiff><Wiff>https://storage.jpostdb.org/JPST001830/files/210623_Sa+PaOMVs1_IDA.wiff</Wiff><Wiff>https://storage.jpostdb.org/JPST001830/files/210623_Sa_Cont1_IDA.wiff</Wiff><Wiff>https://storage.jpostdb.org/JPST001830/files/210623_Sa+PaOMVs3_SWATH.wiff</Wiff><Wiff>https://storage.jpostdb.org/JPST001830/files/210623_Sa+PaOMVs1_IDA.wiff.scan</Wiff><Wiff>https://storage.jpostdb.org/JPST001830/files/210623_Sa_Cont2_SWATH.wiff</Wiff><Wiff>https://storage.jpostdb.org/JPST001830/files/210623_Sa+PaOMVs3_SWATH.wiff.scan</Wiff><Wiff>https://storage.jpostdb.org/JPST001830/files/210623_Sa_Cont1_SWATH.wiff</Wiff><Wiff>https://storage.jpostdb.org/JPST001830/files/210623_Sa_Cont3_SWATH.wiff.scan</Wiff><Wiff>https://storage.jpostdb.org/JPST001830/files/210623_Sa+PaOMVs2_SWATH.wiff.scan</Wiff><Wiff>https://storage.jpostdb.org/JPST001830/files/210623_Sa_Cont3_IDA.wiff.scan</Wiff><Wiff>https://storage.jpostdb.org/JPST001830/files/210623_Sa_Cont2_IDA.wiff</Wiff><Wiff>https://storage.jpostdb.org/JPST001830/files/210623_Sa+PaOMVs3_IDA.wiff</Wiff></files><type>primary</type></body><statusCodeValue>200</statusCodeValue><statusCode>OK</statusCode></file_versions><scores/><additional><omics_type>Proteomics</omics_type><submitter>Krisana Asano</submitter><species>Staphylococcus Aureus</species><full_dataset_link>https://repository.jpostdb.org/entry/JPST001830</full_dataset_link><submitter_affiliation>Hirosaki University</submitter_affiliation><sample_protocol></sample_protocol><repository>jPOST</repository><data_protocol></data_protocol><pubmed_abstract>&lt;i>Staphylococcus aureus&lt;/i> and &lt;i>Pseudomonas aeruginosa&lt;/i> are well-known opportunistic pathogens that frequently coexist in chronic wounds and cystic fibrosis. The exoproducts of &lt;i>P. aeruginosa&lt;/i> have been shown to affect the growth and pathogenicity of &lt;i>S. aureus,&lt;/i> but the detailed mechanisms are not well understood. In this study, we investigated the effect of extracellular vesicles from &lt;i>P. aeruginosa&lt;/i> (PaEVs) on the growth of &lt;i>S. aureus&lt;/i>. We found that PaEVs inhibited the &lt;i>S. aureus&lt;/i> growth independently of iron chelation and showed no bactericidal activity. This growth inhibitory effect was also observed with methicillin-resistant &lt;i>S. aureus&lt;/i> but not with &lt;i>Acinetobacter baumannii, Enterococcus faecalis, S.&lt;/i> Typhimurium, &lt;i>E. coli, Listeria monocytogenes&lt;/i>, or &lt;i>Candida albicans&lt;/i>, suggesting that the growth inhibitory effect of PaEVs is highly specific for &lt;i>S. aureus&lt;/i>. To better understand the detailed mechanism, the difference in protein production of &lt;i&gt;S. aureus&lt;/i> between PaEV-treated and non-treated groups was further analyzed. The results revealed that lactate dehydrogenase 2 and formate acetyltransferase enzymes in the pyruvate fermentation pathway were significantly reduced after PaEV treatment. Likewise, the expression of &lt;i>ldh2&lt;/i> gene for lactate dehydrogenase 2 and &lt;i>pflB&lt;/i> gene for formate acetyltransferase in &lt;i>S. aureus&lt;/i> was reduced by PaEV treatment. In addition, this inhibitory effect of PaEVs was abolished by supplementation with pyruvate or oxygen. These results suggest that PaEVs inhibit the growth of &lt;i>S. aureus&lt;/i> by suppressing the pyruvate fermentation pathway. This study reported a mechanism of PaEVs in inhibiting &lt;i>S. aureus&lt;/i> growth which may be important for better management of &lt;i>S. aureus&lt;/i> and &lt;i>P. aeruginosa&lt;/i> co-infections.</pubmed_abstract><pubmed_title>Extracellular vesicles of &lt;i>Pseudomonas aeruginosa&lt;/i> downregulate pyruvate fermentation enzymes and inhibit the initial growth of &lt;i>Staphylococcus aureus&lt;/i>.</pubmed_title><pubmed_authors>Ishiai Takahito T, Subsomwong Phawinee P, Narita Kouj K, Kawai Noriaki N, Teng Wei W, Suzuki Sachio S, Sukchawalit Rojana R, Nakane Akio A, Asano Krisana K</pubmed_authors></additional><is_claimable>false</is_claimable><name>Proteomic analysis of Staphylococcus aureus after treating with extracellular membrane vesicles from Pseudomonas aeruginosa (PaOMVs)</name><description>For proteomic analysis of PaOMV-treated S. aureus, S. aureus (5 × 103 CFU/mL) was incubated with and without 1 µg/mL PaOMVs for 6 h at 37℃ under static condition and proteomic analysis was performed as described above. The identified proteins were searched against S. aureus ATCC1718 (NCBI Genebank: NC_007795.1). In comparison with non-PaOMV treatment, differential protein expression in PaOMV-treated S. aureus was assessed by quantitative proteomics using SWATH analysis.</description><dates><publication>Mon May 08 00:00:00 GMT+01:00 2023</publication></dates><accession>PXD036381</accession><cross_references><TAXONOMY>1280</TAXONOMY><pubmed>37131486</pubmed></cross_references></HashMap>