Proteomics

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ClpP protease modulates bacterial growth, stress response and bacterial virulence in Brucella abortus

ABSTRACT: Intracellular proteolysis via ATP-dependent proteases is a conserved biological process. The ATP-dependent Clp protease is made up of peptidase ClpP and ATP-dependent chaperones and plays an important role in the proteolysis process. In several pathogenic bacteria, the Clp protease is implicated in the stress reponses and contributes to the bacterial virulence. In brucella abortus, the ΔclpP mutant strain exhibited a pronounced growth defect in TSB medium and the results showed that the ΔclpP mutant was sensitive to high temperature, high osmotic environment and iron deficient environment. In addition, deletion of the clpP significantly affected Brucella virulence in macrophage and mice infection models. Based on the iTRAQ analysis, the different expressed proteins were mainly involved in amino acid transport and metabolism, energy production and conversion, and secondary metabolites biosynthesis, transport and catabolism. Overall, our study revealed preliminary molecular mechanism between Clp protease, bacterial growth, stress response and bacterial virulence in Brucella strains

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Brucella Abortus (strain 2308)

TISSUE(S): Cell Culture

SUBMITTER: dongjie sun  

LAB HEAD: Jiabo Ding

PROVIDER: PXD034842 | Pride | 2023-10-24

REPOSITORIES: Pride

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ClpP protease modulates bacterial growth, stress response, and bacterial virulence in Brucella abortus.

Sun Dongjie D   Liu Yufu Y   Peng Xiaowei X   Dong Hao H   Jiang Hui H   Fan Xuezheng X   Feng Yu Y   Sun Jiali J   Han Kun K   Gao Qiang Q   Niu Jianrui J   Ding Jiabo J  

Veterinary research 20230823 1

The process of intracellular proteolysis through ATP-dependent proteases is a biologically conserved phenomenon. The stress responses and bacterial virulence of various pathogenic bacteria are associated with the ATP-dependent Clp protease. In this study, a Brucella abortus 2308 strain, ΔclpP, was constructed to characterize the function of ClpP peptidase. The growth of the ΔclpP mutant strain was significantly impaired in the TSB medium. The results showed that the ΔclpP mutant was sensitive to  ...[more]

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