ClpP protease modulates bacterial growth, stress response, and bacterial virulence in Brucella abortus.
Brucella
ClpP protease
RNA-seq
iTRAQ analysis
virulence
Journal
Veterinary research
ISSN: 1297-9716
Titre abrégé: Vet Res
Pays: England
ID NLM: 9309551
Informations de publication
Date de publication:
23 Aug 2023
23 Aug 2023
Historique:
received:
25
01
2023
accepted:
20
06
2023
medline:
25
8
2023
pubmed:
24
8
2023
entrez:
23
8
2023
Statut:
epublish
Résumé
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 acidic pH stress, oxidative stress, high temperature, detergents, high osmotic environment, and iron deficient environment. Additionally, the deletion of clpP significantly affected Brucella virulence in macrophage and mouse infection models. Integrated transcriptomic and proteomic analyses of the ΔclpP strain showed that 1965 genes were significantly affected at the mRNA and/or protein levels. The RNA-seq analysis indicated that the ΔclpP strain exhibited distinct gene expression patterns related to energy production and conversion, cell wall/membrane/envelope biogenesis, carbohydrate transport, and metabolism. The iTRAQ analysis revealed that the differentially expressed proteins primarily participated in amino acid transport and metabolism, energy production and conversion, and secondary metabolites biosynthesis, transport and catabolism. This study provided insights into the preliminary molecular mechanism between Clp protease to bacterial growth, stress response, and bacterial virulence in Brucella strains.
Identifiants
pubmed: 37612737
doi: 10.1186/s13567-023-01200-x
pii: 10.1186/s13567-023-01200-x
pmc: PMC10464072
doi:
Substances chimiques
Peptide Hydrolases
EC 3.4.-
Endopeptidase Clp
EC 3.4.21.92
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
68Subventions
Organisme : National Natural Science Foundation of China
ID : 31602055
Organisme : National Natural Science Foundation of China
ID : 31602017
Organisme : Key Technologies Research and Development Program
ID : 2016YFD0500902
Informations de copyright
© 2023. L’Institut National de Recherche en Agriculture, Alimentation et Environnement (INRAE).
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