PXD014211

PXD014211 is an original dataset announced via ProteomeXchange.

Title	ClpP participates in stress response, biofilm formation, antimicrobials tolerance, and virulence of Enterococcus faecalis and its global substrate proteins were identified by mass spectrometer with Tandem Mass Tags (TMT) labeling
Description	ClpP is important for bacterial growth and plays an indispensable role in cellular protein quality control systems by refolding or degrading damaged proteins, but the role of ClpP on Enterococcus faecalis is still obscure. A clpP deletion mutant (△clpP) was constructed in E. faecalis strain OG1RF in order to elucidate a more comprehensive picture of the effect of ClpP on E. faecalis. Then the global RNA level of genes was detected by RNA sequencing and the global abundance of proteins was determined by mass spectrometer with Tandem Mass Tags (TMT) labeling. We found the ΔclpP mutant strain showed impaired growth at 20℃ or 45℃, at 5% NaCl or 2 mM H2O2. The surviving bacteria of the ΔclpP mutant strain was decreased after exposure to the high concentration of linezolid or minocycline (100 x MIC) for 96 h compared with that of the parent strain. The ΔclpP mutant strain also demonstrated decreased biofilm formation, but increased virulence in a Galleria mellonella model. The abundances of heat shock proteins, regulatory protein Spx (spxA), heat-inducible transcription repressor HrcA, transcriptional regulator CtsR, ATPase/chaperone ClpC and chaperonin GroEL increased in the ΔclpP mutant strain. The FsrA response regulator and its regulating protein gelatinase GelE, acetyl esterase/lipase, adapter protein MecA and fructose-1,6-bisphosphatase (fbp) also up regulated in the ΔclpP mutant strain. However, the abundances of ribosomal protein L4/L1 family protein (rplD) , ribosomal protein L7/L12 (rplL2), 50S ribosomal protein L13 (rplM), L18 (rplR), L20 (rplT), 30S ribosomal protein S14 (rpsN2) and S18 (rpsR) all reduced in the ΔclpP mutant strain. The dihydroorotase (pyrC), orotate phosphoribosyltransferase (pyrE) and orotidine-5'-phosphate decarboxylase (pyrF) also down regulated in the ΔclpP mutant strain. In conclusion, these results suggest that ClpP participates in stress tolerance, biofilm formation, antimicrobials tolerance, and virulence of E. faecalis.
HostingRepository	PRIDE
AnnounceDate	2020-03-06
AnnouncementXML	Submission_2020-03-06_05:57:26.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Jin-xin Zheng
SpeciesList	scientific name: Enterococcus faecalis (Streptococcus faecalis); NCBI TaxID: 1351;
ModificationList	No PTMs are included in the dataset
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2019-06-11 02:00:51	ID requested
⏵ 1	2020-03-06 05:57:26	announced

Dataset with its publication pending

submitter keyword: Enterococcus faecalis

ClpP

stress tolerance

biofilm formation

virulence

Zhi-jian Yu
contact affiliation	Department of Infectious Diseases and the Key Lab of Endogenous Infection, Shenzhen Nanshan People's Hospital and The 6th Affiliated Hospital of Shenzhen University Health Science Center, Shenzhen 518052, China
contact email	yuzhijiansmu@163.com
lab head
Jin-xin Zheng
contact affiliation	Key Laboratory of Medical Molecular Virology of Ministries of Education and Health, School of Basic Medical Science and Institutes of Biomedical Sciences, Shanghai Medical College of Fudan University
contact email	710194599@qq.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD014211
     1. Label: PRIDE project
     2. Name: ClpP participates in stress response, biofilm formation, antimicrobials tolerance, and virulence of Enterococcus faecalis and its global substrate proteins were identified by mass spectrometer with Tandem Mass Tags (TMT) labeling