PXD041510 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Tenacibaculum maritimum secretome |
Description | Tenacibaculum maritimum, the etiological agent of tenacibaculosis in marine fish, constitutively secretes extracellular products (ECPs), which play a main role in virulence. However, their protein content has not been yet comprehensively studied. In this study a collection of 64 T. maritimum strains belonging to the four serotypes described so far (O1 to O4) was used to analyse the prevalence of extracellular proteolytic and lipolytic activities related to virulence. Results showed the existence of a large heterogeneity of the enzymatic capacity among serotype O4 isolates. Most notably, the ECPs of T. maritimum SP9.1 belonging to serotype O4 contain a large amount of outer membrane vesicles (OMVs), which were characterized by electron microscopy and purified by successive steps of filtration and centrifugation. Total protein content of ECPs, and the proteins associated to OMVs and soluble fraction of the ECPs (S-ECPs) were identified by nLC-TIMS-QTOF. A total of 641 proteins were identified in ECPs including some virulence related factors, which were mainly found in one of the fractions, either in OMVs or S-ECPs. Outer membrane proteins such as TonB-dependent transporters and the T9SS-related proteins PorP, PorT and SprA appeared to be mainly associated with OMVs. By contrast, putative virulence factors such as sialidase SiaA, chondroitinase CslA, sphingomyelinase Sph, ceramidase Cer and collagenase Col were found only in the S-ECPs. These findings demonstrate that T. maritimum release, through surface blebbing, outer membrane vesicles that are enriched specifically in TonB-dependent siderophore transporters and proteins of the type IX secretion system. Interestingly, our results also showed that OMVs could play a role in virulence by promoting surface adhesion, biofilm formation, and maximizing cytotoxic effects of the ECPs. The T. maritimum secretome analysis provides insights into the extracellular products function and can constitute the basis for future studies aimed to elucidate the role of OMVs in the pathogenesis of fish tenacibaculosis. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_05:46:04.056.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Pilar Escribano |
SpeciesList | scientific name: Tenacibaculum maritimum; NCBI TaxID: 107401; |
ModificationList | dehydrated residue; acetylated residue; monohydroxylated residue; deamidated residue; iodoacetamide derivatized residue |
Instrument | timsTOF Pro |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2023-04-13 03:27:17 | ID requested | |
1 | 2023-05-31 03:09:37 | announced | |
2 | 2023-11-14 06:38:28 | announced | 2023-11-14: Updated project metadata. |
⏵ 3 | 2024-10-22 05:46:04 | announced | 2024-10-22: Updated project metadata. |
Publication List
Keyword List
submitter keyword: Virulence Factors, Outer membrane vesicle (OMV),Tenacibaculum maritimum, Tenacibaculosis, Extracellular products (ECPs) |
Contact List
Manuel L. Lemos |
contact affiliation | University of Santiago de Compostela |
contact email | manuel.lemos@usc.es |
lab head | |
Pilar Escribano |
contact affiliation | University Santiago de Compostela |
contact email | mpilar.escribano@usc.es |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD041510
- Label: PRIDE project
- Name: Tenacibaculum maritimum secretome