ArticlePloS one2013
Aggregate-reactivation activity of the molecular chaperone ClpB from Ehrlichia chaffeensis.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 35 citations in OpenAlex.
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- Evaluating EcxR for Its Possible Role inInternational journal of molecular sciences · 2022Article
- Proteome analysis ofFrontiers in cellular and infection microbiology · 2022Article
- Functional Characterization of MultipleInternational journal of molecular sciences · 2021Article
- Hsp100 Molecular Chaperone ClpB and Its Role in Virulence of Bacterial Pathogens.International journal of molecular sciences · 2021Review
- Protein and DNA Biosynthesis Demonstrated in Host Cell-Free Phagosomes Containing Anaplasma phagocytophilum or Ehrlichia chaffeensis in Axenic Media.Infection and immunity · 2021Article
- An integrated transcriptomic and proteomic approach to identify the main Torymus sinensis venom components.Scientific reports · 2021Article
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- The Role of ClpB in Bacterial Stress Responses and Virulence.Frontiers in molecular biosciences · 2021Review
- Biochemical characterization of ClpB3, a chloroplastic disaggregase from Arabidopsis thaliana.Plant molecular biology · 2020Article
- Ehrlichia chaffeensis EplA Interaction With Host Cell Protein Disulfide Isomerase Promotes Infection.Frontiers in cellular and infection microbiology · 2020Article
- Spiraling in Control: Structures and Mechanisms of the Hsp104 Disaggregase.Cold Spring Harbor perspectives in biology · 2019Review
- Sequence Determinants Spanning -10 Motif and Spacer Region Implicated in UniqueFrontiers in microbiology · 2019Article
- Proteome Analysis Revealed Changes in Protein Expression Patterns Caused by Mutations inFrontiers in cellular and infection microbiology · 2019Article
- Protein and DNA synthesis demonstrated in cell-free Ehrlichia chaffeensis organisms in axenic medium.Scientific reports · 2018Article
- Impact of Three Different Mutations in Ehrlichia chaffeensis in Altering the Global Gene Expression Patterns.Scientific reports · 2018Article
- Comparative roles of clpA and clpB in the survival of S. Typhimurium under stress and virulence in poultry.Scientific reports · 2018Article
- Protein aggregation in Ehrlichia chaffeensis during infection of mammalian cells.FEMS microbiology letters · 2017Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Rickettsiale diseases, including human monocytic ehrlichiosis caused by Ehrlichia chaffeensis, are the second leading cause of the tick-borne infections in the USA and a growing health concern. Little is known about how E. chaffeensis survives the host-induced stress in vertebrate and tick hosts. A molecular chaperone ClpB from several microorganisms has been reported to reactivate aggregated proteins in cooperation with the co-chaperones DnaK/DnaJ/GrpE (KJE). In this study, we performed the first biochemical characterization of ClpB from E. chaffeensis. The transcript of E. chaffeensis ClpB (EhClpB) is strongly upregulated after infection of cultured macrophages and its level remains high during the Ehrlichia replicative stage. EhClpB forms ATP-dependent oligomers and catalyzes the ATP hydrolysis, similar to E. coli ClpB (EcClpB), but its ATPase activity is insensitive to the EcClpB activators, casein and poly-lysine. EhClpB in the presence of E. coli KJE efficiently reactivates the aggregated glucose-6-phosphate dehydrogenase (G6PDH) and firefly luciferase. Unlike EcClpB, which requires the co-chaperones for aggregate reactivation, EhClpB reactivates G6PDH even in the absence of KJE. Moreover, EhClpB is functionally distinct from EcClpB as evidenced by its failure to rescue a temperature-sensitive phenotype of the clpB-null E. coli. The clpB expression pattern during the E. chaffeensis infection progression correlates with the pathogen's replicating stage inside host cells and suggests an essential role of the disaggregase activity of ClpB in the pathogen's response to the host-induced stress. This study sets the stage for assessing the importance of the chaperone activity of ClpB for E. chaffeensis growth within the mammalian and tick hosts.
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