ArticlePloS one2017
Characterization of the molecular chaperone ClpB from the pathogenic spirochaete Leptospira interrogans.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 28 citations in OpenAlex.
- Alternative Sigma Factors of RNA Polymerase as Master Regulators in the Pathogenic SpirochaetePathogens (Basel, Switzerland) · 2025Review
- The ClpA chaperone and the two adaptor proteins modulate the fate of the model substrate tagged with a SsrA-degron of Leptospira.The Biochemical journal · 2025Article
- Evidence for a Putative Regulatory System Consisting of an ECF σInternational journal of molecular sciences · 2025Article
- Article
- Backbone chemical shift assignment and dynamics of the N-terminal domain of ClpB from Francisella tularensis type VI secretion system.Biomolecular NMR assignments · 2022Article
- Proteomic profiling spotlights the molecular targets and the impact of the natural antivirulent umbelliferone on stress response, virulence factors, and the quorum sensing network ofFrontiers in cellular and infection microbiology · 2022Article
- Comparative Proteomic Analysis of Psychrophilic vs. Mesophilic Bacterial Species Reveals Different Strategies to Achieve Temperature Adaptation.Frontiers in microbiology · 2022Article
- The oxidative stress response of pathogenic Leptospira is controlled by two peroxide stress regulators which putatively cooperate in controlling virulence.PLoS pathogens · 2021Article
- The Cryo-EM Effect: Structural Biology of Neurodegenerative Disease Proteostasis Factors.Journal of neuropathology and experimental neurology · 2021Review
- Hsp100 Molecular Chaperone ClpB and Its Role in Virulence of Bacterial Pathogens.International journal of molecular sciences · 2021Review
- 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
- AAA+ Molecular Chaperone ClpB inInternational journal of molecular sciences · 2020Review
- Role of ClpB FromFrontiers in microbiology · 2020Article
- Identification of σInternational journal of molecular sciences · 2019Article
- Spiraling in Control: Structures and Mechanisms of the Hsp104 Disaggregase.Cold Spring Harbor perspectives in biology · 2019Review
- Insights to the Assembly of a Functionally Active Leptospiral ClpP1P2 Protease Complex along with Its ATPase Chaperone ClpX.ACS omega · 2019Article
- Inferring pathogen-host interactions between Leptospira interrogans and Homo sapiens using network theory.Scientific reports · 2019Article
- Isolation and Identification of Putative Protein Substrates of the AAA+ Molecular Chaperone ClpB from the Pathogenic SpirochaeteInternational journal of molecular sciences · 2018Article
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Leptospira interrogans is a spirochaete responsible for leptospirosis in mammals. The molecular mechanisms of the Leptospira virulence remain mostly unknown. Recently, it has been demonstrated that an AAA+ chaperone ClpB (a member of the Hsp100 family) from L. interrogans (ClpBLi) is not only essential for survival of Leptospira under the thermal and oxidative stresses, but also during infection of a host. The aim of this study was to provide further insight into the role of ClpB in the pathogenic spirochaetes and explore its biochemical properties. We found that a non-hydrolysable ATP analogue, ATPγS, but not AMP-PNP induces the formation of ClpBLi hexamers and stabilizes the associated form of the chaperone. ADP also induces structural changes in ClpBLi and promotes its self-assembly, but does not produce full association into the hexamers. We also demonstrated that ClpBLi exhibits a weak ATPase activity that is stimulated by κ-casein and poly-lysine, and may mediate protein disaggregation independently from the DnaK chaperone system. Unexpectedly, the presence of E. coli DnaK/DnaJ/GrpE did not significantly affect the disaggregation activity of ClpBLi and ClpBLi did not substitute for the ClpBEc function in the clpB-null E. coli strain. This result underscores the species-specificity of the ClpB cooperation with the co-chaperones and is most likely due to a loss of interactions between the ClpBLi middle domain and the E. coli DnaK. We also found that ClpBLi interacts more efficiently with the aggregated G6PDH in the presence of ATPγS rather than ATP. Our results indicate that ClpB's importance during infection might be due to its role as a molecular chaperone involved in reactivation of protein aggregates.
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