PXD005505 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | iTRAQ-based quantitative proteomic analysis reveals potential virulence factors of Erysipelothrix rhusiopathiae |
Description | Erysipelothrix rhusiopathiae is a small, facultatively aerobic, gram-positive bacterium that causes erysipelas in swine and a wide spectrum of diseases in other animals, as well as the skin disease erysipeloid in humans. Swine erysipelas caused by E. rhusiopathiae is the most prevalent and economically important of these diseases. In China, swine erysipelas has emerged at an alarming rate, developing from scattered occurrences on a small number of farms to systemic outbreaks since 2012 in many provinces, thereby inflicting large financial losses. Some virulence factors of E. rhusiopathiae have been identified. The capsule is considered essential for resistance to phagocytosis and bacterial virulence. Neuraminidase plays a crucial role in initiating adhesion to endothelial cells. Two surface-adhesion proteins (RspA and RspB) participate in the initiation of biofilm formation by binding to abiotic and biotic surfaces. SpaA is involved in the adhesion of E. rhusiopathiae to porcine endothelial cells. Nevertheless, very little is known about the pathogenesis of E. rhusiopathiae. This knowledge gap has become one of the most important obstacles to controlling infection. Thus, the identification of novel virulence factors is necessary to improve understanding of the pathogenesis of E. rhusiopathiae.Surface proteins of gram-positive bacteria play a critical role in virulence by modifying the environment surrounding the cell. Furthermore, for many bacteria, surface proteins are candidate antigens for subunit vaccines. The examination of bacterial surface-protein fractions, including cell wall-associated proteins (CWPs), is an effective method for identifying novel virulence factors. One proteomic approach involves isobaric Tags for Relative and Absolute Quantitation (iTRAQ) coupled to liquid chromatography (LC)-quadrupole mass spectrometry (MS/MS). This method has been widely used for the comparative quantitative analysis of bacterial proteomes. In this study, iTRAQ combined with LC-MS/MS was applied to compare differentially abundant CWPs of high- and low-virulence strains of E. rhusiopathiae. Proteins with higher abundance in the high-virulence strain were found to aid in predicting potential virulence factors to improve vaccines or disease-control strategies. |
HostingRepository | PRIDE |
AnnounceDate | 2017-03-28 |
AnnouncementXML | Submission_2017-03-28_01:56:40.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Ya Wang |
SpeciesList | scientific name: Erysipelothrix rhusiopathiae; NCBI TaxID: 1648; |
ModificationList | No PTMs are included in the dataset |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2016-12-05 07:00:48 | ID requested | |
⏵ 1 | 2017-03-28 01:56:40 | announced | |
2 | 2017-06-06 08:25:31 | announced | Updated publication reference for PubMed record(s): 28284755. |
Publication List
Dataset with its publication pending |
Keyword List
curator keyword: Biological |
submitter keyword: Erysipelothrix rhusiopathiae, cell wall proteins, comparative proteomics, virulence factor |
Contact List
Meilin Jin |
contact affiliation | College of Animal Science and Veterinary Medicine, Huazhong Agricultural University, Wuhan, China |
contact email | jml8328@126.com |
lab head | |
Ya Wang |
contact affiliation | Huazhong agricultural university |
contact email | aya520123@163.com |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD005505
- Label: PRIDE project
- Name: iTRAQ-based quantitative proteomic analysis reveals potential virulence factors of Erysipelothrix rhusiopathiae